PubMed:12145188 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":261,"end":268},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T2","span":{"begin":1532,"end":1539},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlyCosmos600-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":261,"end":268},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T2","span":{"begin":1532,"end":1539},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlyCosmos600-CLO","denotations":[{"id":"T1","span":{"begin":762,"end":773},"obj":"http://purl.obolibrary.org/obo/CL_0000057"},{"id":"T2","span":{"begin":830,"end":835},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":908,"end":913},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":1108,"end":1119},"obj":"http://purl.obolibrary.org/obo/CL_0000057"},{"id":"T5","span":{"begin":1703,"end":1714},"obj":"http://purl.obolibrary.org/obo/CL_0000057"},{"id":"T6","span":{"begin":2511,"end":2522},"obj":"http://purl.obolibrary.org/obo/CLO_0051721"},{"id":"T7","span":{"begin":2511,"end":2522},"obj":"http://purl.obolibrary.org/obo/CLO_0051654"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":261,"end":268},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":1532,"end":1539},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":102,"end":228},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":229,"end":387},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":388,"end":587},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":588,"end":706},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":707,"end":914},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":915,"end":1080},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1081,"end":1264},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1265,"end":1501},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1502,"end":1857},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1858,"end":2076},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":2077,"end":2226},"obj":"Sentence"},{"id":"TextSentencer_T13","span":{"begin":2227,"end":2396},"obj":"Sentence"},{"id":"TextSentencer_T14","span":{"begin":2397,"end":2567},"obj":"Sentence"},{"id":"TextSentencer_T15","span":{"begin":2568,"end":2786},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":101},"obj":"Sentence"},{"id":"T2","span":{"begin":102,"end":228},"obj":"Sentence"},{"id":"T3","span":{"begin":229,"end":387},"obj":"Sentence"},{"id":"T4","span":{"begin":388,"end":587},"obj":"Sentence"},{"id":"T5","span":{"begin":588,"end":706},"obj":"Sentence"},{"id":"T6","span":{"begin":707,"end":914},"obj":"Sentence"},{"id":"T7","span":{"begin":915,"end":1080},"obj":"Sentence"},{"id":"T8","span":{"begin":1081,"end":1264},"obj":"Sentence"},{"id":"T9","span":{"begin":1265,"end":1501},"obj":"Sentence"},{"id":"T10","span":{"begin":1502,"end":1857},"obj":"Sentence"},{"id":"T11","span":{"begin":1858,"end":2076},"obj":"Sentence"},{"id":"T12","span":{"begin":2077,"end":2226},"obj":"Sentence"},{"id":"T13","span":{"begin":2227,"end":2396},"obj":"Sentence"},{"id":"T14","span":{"begin":2397,"end":2567},"obj":"Sentence"},{"id":"T15","span":{"begin":2568,"end":2786},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":261,"end":268},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T2","span":{"begin":1532,"end":1539},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlycoBiology-GDGDB","denotations":[{"id":"_T1","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00360"},{"id":"_T2","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00343"},{"id":"_T3","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00344"},{"id":"_T4","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00345"},{"id":"_T5","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00346"},{"id":"_T6","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00347"},{"id":"_T7","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00348"},{"id":"_T8","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00349"},{"id":"_T9","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00350"},{"id":"_T10","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00351"},{"id":"_T11","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00352"},{"id":"_T12","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00353"},{"id":"_T13","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00354"},{"id":"_T14","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00355"},{"id":"_T15","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00356"},{"id":"_T16","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00620"},{"id":"_T17","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00627"},{"id":"_T18","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00622"},{"id":"_T19","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00623"},{"id":"_T20","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00624"},{"id":"_T21","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00625"},{"id":"_T22","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00358"},{"id":"_T23","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00359"},{"id":"_T24","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00361"},{"id":"_T25","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00362"},{"id":"_T26","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00363"},{"id":"_T27","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00364"},{"id":"_T28","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00365"},{"id":"_T29","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00367"},{"id":"_T30","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00626"},{"id":"_T31","span":{"begin":132,"end":168},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00621"},{"id":"_T32","span":{"begin":170,"end":177},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00359"},{"id":"_T33","span":{"begin":170,"end":177},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00344"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":0,"end":15},"obj":"FMAID:165414"},{"id":"_T2","span":{"begin":0,"end":15},"obj":"FMAID:67601"},{"id":"_T3","span":{"begin":23,"end":35},"obj":"FMAID:197276"},{"id":"_T4","span":{"begin":23,"end":35},"obj":"FMAID:82737"},{"id":"_T5","span":{"begin":261,"end":268},"obj":"FMAID:82743"},{"id":"_T6","span":{"begin":261,"end":268},"obj":"FMAID:196732"},{"id":"_T7","span":{"begin":286,"end":296},"obj":"FMAID:196739"},{"id":"_T8","span":{"begin":286,"end":296},"obj":"FMAID:82750"},{"id":"_T9","span":{"begin":360,"end":375},"obj":"FMAID:82742"},{"id":"_T10","span":{"begin":360,"end":375},"obj":"FMAID:196731"},{"id":"_T11","span":{"begin":432,"end":440},"obj":"FMAID:165656"},{"id":"_T12","span":{"begin":432,"end":440},"obj":"FMAID:67745"},{"id":"_T13","span":{"begin":493,"end":497},"obj":"FMAID:198663"},{"id":"_T14","span":{"begin":507,"end":517},"obj":"FMAID:70637"},{"id":"_T15","span":{"begin":507,"end":517},"obj":"FMAID:171495"},{"id":"_T16","span":{"begin":553,"end":563},"obj":"FMAID:171495"},{"id":"_T17","span":{"begin":553,"end":563},"obj":"FMAID:70637"},{"id":"_T18","span":{"begin":762,"end":773},"obj":"FMAID:63877"},{"id":"_T19","span":{"begin":762,"end":773},"obj":"FMAID:162340"},{"id":"_T20","span":{"begin":830,"end":835},"obj":"FMAID:68646"},{"id":"_T21","span":{"begin":830,"end":835},"obj":"FMAID:169002"},{"id":"_T22","span":{"begin":872,"end":884},"obj":"FMAID:179268"},{"id":"_T23","span":{"begin":872,"end":884},"obj":"FMAID:74531"},{"id":"_T24","span":{"begin":908,"end":913},"obj":"FMAID:68646"},{"id":"_T25","span":{"begin":908,"end":913},"obj":"FMAID:169002"},{"id":"_T26","span":{"begin":1108,"end":1119},"obj":"FMAID:162340"},{"id":"_T27","span":{"begin":1108,"end":1119},"obj":"FMAID:63877"},{"id":"_T28","span":{"begin":1270,"end":1276},"obj":"FMAID:146304"},{"id":"_T29","span":{"begin":1270,"end":1276},"obj":"FMAID:50596"},{"id":"_T30","span":{"begin":1532,"end":1539},"obj":"FMAID:82801"},{"id":"_T31","span":{"begin":1532,"end":1539},"obj":"FMAID:196796"},{"id":"_T32","span":{"begin":1550,"end":1563},"obj":"FMAID:62925"},{"id":"_T33","span":{"begin":1550,"end":1563},"obj":"FMAID:167256"},{"id":"_T34","span":{"begin":1659,"end":1671},"obj":"FMAID:82737"},{"id":"_T35","span":{"begin":1659,"end":1671},"obj":"FMAID:197276"},{"id":"_T36","span":{"begin":1703,"end":1714},"obj":"FMAID:162340"},{"id":"_T37","span":{"begin":1703,"end":1714},"obj":"FMAID:63877"},{"id":"_T38","span":{"begin":2101,"end":2105},"obj":"FMAID:198663"},{"id":"_T39","span":{"begin":2120,"end":2125},"obj":"FMAID:198073"},{"id":"_T40","span":{"begin":2120,"end":2125},"obj":"FMAID:84120"},{"id":"_T41","span":{"begin":2145,"end":2152},"obj":"FMAID:84121"},{"id":"_T42","span":{"begin":2145,"end":2152},"obj":"FMAID:198075"},{"id":"_T43","span":{"begin":2158,"end":2162},"obj":"FMAID:198073"},{"id":"_T44","span":{"begin":2158,"end":2162},"obj":"FMAID:84120"},{"id":"_T45","span":{"begin":2328,"end":2332},"obj":"FMAID:198073"},{"id":"_T46","span":{"begin":2328,"end":2332},"obj":"FMAID:84120"},{"id":"_T47","span":{"begin":2517,"end":2522},"obj":"FMAID:68646"},{"id":"_T48","span":{"begin":2517,"end":2522},"obj":"FMAID:169002"},{"id":"_T49","span":{"begin":2604,"end":2611},"obj":"FMAID:165447"},{"id":"_T50","span":{"begin":2604,"end":2611},"obj":"FMAID:67257"},{"id":"_T51","span":{"begin":2709,"end":2720},"obj":"FMAID:82739"},{"id":"_T52","span":{"begin":2709,"end":2720},"obj":"FMAID:196728"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":1038,"end":1049},"obj":"http://www.uniprot.org/uniprot/Q16706"},{"id":"T2","span":{"begin":1046,"end":1064},"obj":"http://www.uniprot.org/uniprot/P33908"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":1038,"end":1049},"obj":"http://www.uniprot.org/uniprot/P27046"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":441,"end":453},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1369269"},{"id":"T2","span":{"begin":830,"end":835},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T3","span":{"begin":908,"end":913},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":2517,"end":2522},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":155,"end":168},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T2","span":{"begin":2016,"end":2029},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T3","span":{"begin":790,"end":812},"obj":"http://purl.obolibrary.org/obo/GO_0004573"},{"id":"T4","span":{"begin":1292,"end":1314},"obj":"http://purl.obolibrary.org/obo/GO_0004573"},{"id":"T5","span":{"begin":1610,"end":1632},"obj":"http://purl.obolibrary.org/obo/GO_0004573"},{"id":"T6","span":{"begin":1171,"end":1191},"obj":"http://purl.obolibrary.org/obo/GO_0015923"},{"id":"T7","span":{"begin":1247,"end":1263},"obj":"http://purl.obolibrary.org/obo/GO_0009299"},{"id":"T8","span":{"begin":1252,"end":1263},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T9","span":{"begin":1477,"end":1486},"obj":"http://purl.obolibrary.org/obo/GO_0007588"},{"id":"T10","span":{"begin":2380,"end":2395},"obj":"http://purl.obolibrary.org/obo/GO_0003824"},{"id":"T11","span":{"begin":2548,"end":2566},"obj":"http://purl.obolibrary.org/obo/GO_0003824"},{"id":"T12","span":{"begin":2752,"end":2773},"obj":"http://purl.obolibrary.org/obo/GO_0018307"},{"id":"T13","span":{"begin":2764,"end":2773},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":2633,"end":2640},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":2633,"end":2640},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T3","span":{"begin":2633,"end":2640},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T4","span":{"begin":2633,"end":2640},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":830,"end":835},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":908,"end":913},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":2517,"end":2522},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":23,"end":35},"obj":"http://edamontology.org/topic_0152"},{"id":"T2","span":{"begin":420,"end":427},"obj":"http://edamontology.org/topic_0634"},{"id":"T3","span":{"begin":462,"end":471},"obj":"http://edamontology.org/topic_0199"},{"id":"T4","span":{"begin":715,"end":722},"obj":"http://edamontology.org/topic_3678"},{"id":"T5","span":{"begin":1252,"end":1263},"obj":"http://edamontology.org/topic_3512"},{"id":"T6","span":{"begin":1252,"end":1263},"obj":"http://edamontology.org/topic_3308"},{"id":"T7","span":{"begin":1252,"end":1263},"obj":"http://edamontology.org/topic_0110"},{"id":"T8","span":{"begin":1252,"end":1263},"obj":"http://edamontology.org/topic_0203"},{"id":"T9","span":{"begin":1389,"end":1396},"obj":"http://edamontology.org/topic_0602"},{"id":"T10","span":{"begin":1659,"end":1671},"obj":"http://edamontology.org/topic_0152"},{"id":"T11","span":{"begin":2081,"end":2086},"obj":"http://edamontology.org/topic_2815"},{"id":"T12","span":{"begin":2120,"end":2125},"obj":"http://edamontology.org/topic_3512"},{"id":"T13","span":{"begin":2120,"end":2125},"obj":"http://edamontology.org/topic_2397"},{"id":"T14","span":{"begin":2145,"end":2152},"obj":"http://edamontology.org/topic_3512"},{"id":"T15","span":{"begin":2145,"end":2152},"obj":"http://edamontology.org/topic_2754"},{"id":"T16","span":{"begin":2158,"end":2162},"obj":"http://edamontology.org/topic_2397"},{"id":"T17","span":{"begin":2158,"end":2162},"obj":"http://edamontology.org/topic_3512"},{"id":"T18","span":{"begin":2240,"end":2249},"obj":"http://edamontology.org/topic_0199"},{"id":"T19","span":{"begin":2328,"end":2332},"obj":"http://edamontology.org/topic_3512"},{"id":"T20","span":{"begin":2328,"end":2332},"obj":"http://edamontology.org/topic_2397"},{"id":"T21","span":{"begin":2421,"end":2429},"obj":"http://edamontology.org/topic_0199"},{"id":"T22","span":{"begin":2604,"end":2611},"obj":"http://edamontology.org/topic_0078"},{"id":"T23","span":{"begin":2709,"end":2720},"obj":"http://edamontology.org/topic_0154"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":0,"end":10},"obj":"http://edamontology.org/operation_0004"},{"id":"T2","span":{"begin":0,"end":10},"obj":"http://edamontology.org/operation_2409"},{"id":"T3","span":{"begin":115,"end":123},"obj":"http://edamontology.org/data_2048"},{"id":"T4","span":{"begin":269,"end":276},"obj":"http://edamontology.org/data_1756"},{"id":"T5","span":{"begin":969,"end":979},"obj":"http://edamontology.org/operation_0004"},{"id":"T6","span":{"begin":969,"end":979},"obj":"http://edamontology.org/operation_2409"},{"id":"T7","span":{"begin":1247,"end":1263},"obj":"http://edamontology.org/operation_0372"},{"id":"T8","span":{"begin":1389,"end":1396},"obj":"http://edamontology.org/data_2600"},{"id":"T9","span":{"begin":1514,"end":1522},"obj":"http://edamontology.org/operation_2945"},{"id":"T10","span":{"begin":1737,"end":1746},"obj":"http://edamontology.org/operation_2409"},{"id":"T11","span":{"begin":1737,"end":1746},"obj":"http://edamontology.org/operation_0004"},{"id":"T12","span":{"begin":1864,"end":1874},"obj":"http://edamontology.org/data_0883"},{"id":"T13","span":{"begin":1889,"end":1893},"obj":"http://edamontology.org/data_0006"},{"id":"T14","span":{"begin":2054,"end":2060},"obj":"http://edamontology.org/operation_3435"},{"id":"T15","span":{"begin":2318,"end":2324},"obj":"http://edamontology.org/data_2619"},{"id":"T16","span":{"begin":2537,"end":2547},"obj":"http://edamontology.org/data_3108"},{"id":"T17","span":{"begin":2604,"end":2611},"obj":"http://edamontology.org/format_1208"},{"id":"T18","span":{"begin":2604,"end":2611},"obj":"http://edamontology.org/data_1467"},{"id":"T19","span":{"begin":2764,"end":2773},"obj":"http://edamontology.org/operation_0335"},{"id":"T20","span":{"begin":2764,"end":2773},"obj":"http://edamontology.org/format_1915"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlyCosmos600-FMA","denotations":[{"id":"T1","span":{"begin":23,"end":35},"obj":"Body_part"},{"id":"T2","span":{"begin":261,"end":268},"obj":"Body_part"},{"id":"T3","span":{"begin":360,"end":375},"obj":"Body_part"},{"id":"T4","span":{"begin":493,"end":497},"obj":"Body_part"},{"id":"T5","span":{"begin":762,"end":773},"obj":"Body_part"},{"id":"T6","span":{"begin":830,"end":835},"obj":"Body_part"},{"id":"T7","span":{"begin":908,"end":913},"obj":"Body_part"},{"id":"T8","span":{"begin":1108,"end":1119},"obj":"Body_part"},{"id":"T9","span":{"begin":1247,"end":1251},"obj":"Body_part"},{"id":"T10","span":{"begin":1532,"end":1539},"obj":"Body_part"},{"id":"T11","span":{"begin":1550,"end":1563},"obj":"Body_part"},{"id":"T12","span":{"begin":1659,"end":1671},"obj":"Body_part"},{"id":"T13","span":{"begin":1703,"end":1714},"obj":"Body_part"},{"id":"T14","span":{"begin":2101,"end":2105},"obj":"Body_part"},{"id":"T15","span":{"begin":2145,"end":2152},"obj":"Body_part"},{"id":"T16","span":{"begin":2158,"end":2162},"obj":"Body_part"},{"id":"T17","span":{"begin":2328,"end":2332},"obj":"Body_part"},{"id":"T18","span":{"begin":2517,"end":2522},"obj":"Body_part"},{"id":"T19","span":{"begin":2604,"end":2611},"obj":"Body_part"},{"id":"T20","span":{"begin":2709,"end":2720},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"fma_id","subj":"T1","obj":"http://purl.org/sig/ont/fma/fma82737"},{"id":"A2","pred":"fma_id","subj":"T2","obj":"http://purl.org/sig/ont/fma/fma82743"},{"id":"A3","pred":"fma_id","subj":"T3","obj":"http://purl.org/sig/ont/fma/fma82742"},{"id":"A4","pred":"fma_id","subj":"T4","obj":"http://purl.org/sig/ont/fma/fma74402"},{"id":"A5","pred":"fma_id","subj":"T5","obj":"http://purl.org/sig/ont/fma/fma63877"},{"id":"A6","pred":"fma_id","subj":"T6","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A7","pred":"fma_id","subj":"T7","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A8","pred":"fma_id","subj":"T8","obj":"http://purl.org/sig/ont/fma/fma63877"},{"id":"A9","pred":"fma_id","subj":"T9","obj":"http://purl.org/sig/ont/fma/fma67122"},{"id":"A10","pred":"fma_id","subj":"T10","obj":"http://purl.org/sig/ont/fma/fma82801"},{"id":"A11","pred":"fma_id","subj":"T11","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A12","pred":"fma_id","subj":"T12","obj":"http://purl.org/sig/ont/fma/fma82737"},{"id":"A13","pred":"fma_id","subj":"T13","obj":"http://purl.org/sig/ont/fma/fma63877"},{"id":"A14","pred":"fma_id","subj":"T14","obj":"http://purl.org/sig/ont/fma/fma74402"},{"id":"A15","pred":"fma_id","subj":"T15","obj":"http://purl.org/sig/ont/fma/fma84121"},{"id":"A16","pred":"fma_id","subj":"T16","obj":"http://purl.org/sig/ont/fma/fma84120"},{"id":"A17","pred":"fma_id","subj":"T17","obj":"http://purl.org/sig/ont/fma/fma84120"},{"id":"A18","pred":"fma_id","subj":"T18","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A19","pred":"fma_id","subj":"T19","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A20","pred":"fma_id","subj":"T20","obj":"http://purl.org/sig/ont/fma/fma82739"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlyCosmos600-GlycoProteins","denotations":[{"id":"PD-GlycoProteins-B_T1","span":{"begin":1247,"end":1251},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005542"},{"id":"PD-GlycoProteins-B_T2","span":{"begin":1247,"end":1251},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005543"},{"id":"PD-GlycoProteins-B_T3","span":{"begin":1247,"end":1251},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005544"},{"id":"PD-GlycoProteins-B_T4","span":{"begin":1247,"end":1251},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005545"},{"id":"PD-GlycoProteins-B_T5","span":{"begin":1162,"end":1182},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000585"},{"id":"PD-GlycoProteins-B_T6","span":{"begin":1412,"end":1432},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000585"},{"id":"PD-GlycoProteins-B_T7","span":{"begin":1162,"end":1182},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000648"},{"id":"PD-GlycoProteins-B_T8","span":{"begin":1412,"end":1432},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000648"},{"id":"PD-GlycoProteins-B_T9","span":{"begin":1162,"end":1182},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000773"},{"id":"PD-GlycoProteins-B_T10","span":{"begin":1412,"end":1432},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000773"},{"id":"PD-GlycoProteins-B_T11","span":{"begin":1162,"end":1182},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001141"},{"id":"PD-GlycoProteins-B_T12","span":{"begin":1412,"end":1432},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001141"},{"id":"PD-GlycoProteins-B_T13","span":{"begin":1162,"end":1182},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001144"},{"id":"PD-GlycoProteins-B_T14","span":{"begin":1412,"end":1432},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001144"},{"id":"PD-GlycoProteins-B_T15","span":{"begin":1162,"end":1182},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002027"},{"id":"PD-GlycoProteins-B_T16","span":{"begin":1412,"end":1432},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002027"},{"id":"PD-GlycoProteins-B_T17","span":{"begin":1162,"end":1182},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002028"},{"id":"PD-GlycoProteins-B_T18","span":{"begin":1412,"end":1432},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002028"},{"id":"PD-GlycoProteins-B_T19","span":{"begin":1162,"end":1182},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004660"},{"id":"PD-GlycoProteins-B_T20","span":{"begin":1412,"end":1432},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004660"},{"id":"PD-GlycoProteins-B_T21","span":{"begin":1162,"end":1182},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005222"},{"id":"PD-GlycoProteins-B_T22","span":{"begin":1412,"end":1432},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005222"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":318,"end":324},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":1841,"end":1847},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"12145188-1#112#125#gene7841","span":{"begin":214,"end":227},"obj":"gene7841"},{"id":"12145188-1#68#75#diseaseC1853736","span":{"begin":170,"end":177},"obj":"diseaseC1853736"}],"relations":[{"id":"112#125#gene784168#75#diseaseC1853736","pred":"associated_with","subj":"12145188-1#112#125#gene7841","obj":"12145188-1#68#75#diseaseC1853736"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

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g2Of","subj":"EnjuParser_T354","obj":"EnjuParser_T351"},{"id":"EnjuParser_R346","pred":"arg1Of","subj":"EnjuParser_T354","obj":"EnjuParser_T352"},{"id":"EnjuParser_R347","pred":"arg1Of","subj":"EnjuParser_T354","obj":"EnjuParser_T353"},{"id":"EnjuParser_R348","pred":"arg1Of","subj":"EnjuParser_T348","obj":"EnjuParser_T355"}],"namespaces":[{"prefix":"_base","uri":"http://kmcs.nii.ac.jp/enju/"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"glycosmos-test-glycan-structure","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":1532,"end":1539},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":261,"end":268},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa210/trivialname"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"glycosmos-test-structure-v1","denotations":[{"id":"PD-GlycanStructures-B_T2","span":{"begin":261,"end":268},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa210/trivialname"},{"id":"PD-GlycanStructures-B_T1","span":{"begin":1532,"end":1539},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlyCosmos600-GlycoGenes","denotations":[{"id":"PD-GlycoGenes-B_T1","span":{"begin":2182,"end":2187},"obj":"GGDB:LARGE"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":1793,"end":1802},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":311,"end":314},"obj":"https://acgg.asia/db/lfdb/LfDB0217"},{"id":"Lectin_T2","span":{"begin":1046,"end":1049},"obj":"https://acgg.asia/db/lfdb/LfDB0217"},{"id":"Lectin_T3","span":{"begin":1497,"end":1500},"obj":"https://acgg.asia/db/lfdb/LfDB0217"},{"id":"Lectin_T4","span":{"begin":1832,"end":1835},"obj":"https://acgg.asia/db/lfdb/LfDB0217"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":1540,"end":1547},"obj":"id"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G59743JO\""},{"id":"GlycanIUPAC_T2","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G59743JO\""},{"id":"GlycanIUPAC_T3","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G59743JO\""},{"id":"GlycanIUPAC_T4","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G22515CP\""},{"id":"GlycanIUPAC_T5","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G22515CP\""},{"id":"GlycanIUPAC_T6","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G22515CP\""},{"id":"GlycanIUPAC_T7","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G50260YT\""},{"id":"GlycanIUPAC_T8","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G50260YT\""},{"id":"GlycanIUPAC_T9","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G50260YT\""},{"id":"GlycanIUPAC_T10","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G59271KV\""},{"id":"GlycanIUPAC_T11","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G59271KV\""},{"id":"GlycanIUPAC_T12","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G59271KV\""},{"id":"GlycanIUPAC_T13","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G41080ZB\""},{"id":"GlycanIUPAC_T14","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G41080ZB\""},{"id":"GlycanIUPAC_T15","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G41080ZB\""},{"id":"GlycanIUPAC_T16","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G28051VF\""},{"id":"GlycanIUPAC_T17","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G28051VF\""},{"id":"GlycanIUPAC_T18","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G28051VF\""},{"id":"GlycanIUPAC_T19","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G44775RL\""},{"id":"GlycanIUPAC_T20","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G44775RL\""},{"id":"GlycanIUPAC_T21","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G44775RL\""},{"id":"GlycanIUPAC_T22","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G05723ZI\""},{"id":"GlycanIUPAC_T23","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G05723ZI\""},{"id":"GlycanIUPAC_T24","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G05723ZI\""},{"id":"GlycanIUPAC_T25","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G80753ZP\""},{"id":"GlycanIUPAC_T26","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G80753ZP\""},{"id":"GlycanIUPAC_T27","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G80753ZP\""},{"id":"GlycanIUPAC_T28","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G09675LS\""},{"id":"GlycanIUPAC_T29","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G09675LS\""},{"id":"GlycanIUPAC_T30","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G09675LS\""},{"id":"GlycanIUPAC_T31","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G32374SR\""},{"id":"GlycanIUPAC_T32","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G32374SR\""},{"id":"GlycanIUPAC_T33","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G32374SR\""},{"id":"GlycanIUPAC_T34","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G35562XQ\""},{"id":"GlycanIUPAC_T35","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G35562XQ\""},{"id":"GlycanIUPAC_T36","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G35562XQ\""},{"id":"GlycanIUPAC_T37","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G79798HI\""},{"id":"GlycanIUPAC_T38","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G79798HI\""},{"id":"GlycanIUPAC_T39","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G79798HI\""},{"id":"GlycanIUPAC_T40","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G60629WC\""},{"id":"GlycanIUPAC_T41","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G60629WC\""},{"id":"GlycanIUPAC_T42","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G60629WC\""},{"id":"GlycanIUPAC_T43","span":{"begin":304,"end":307},"obj":"\"http://rdf.glycoinfo.org/glycan/G28900GG\""},{"id":"GlycanIUPAC_T44","span":{"begin":1490,"end":1493},"obj":"\"http://rdf.glycoinfo.org/glycan/G28900GG\""},{"id":"GlycanIUPAC_T45","span":{"begin":1825,"end":1828},"obj":"\"http://rdf.glycoinfo.org/glycan/G28900GG\""},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"\"http://rdf.glycoinfo.org/glycan/G87709OA\""},{"id":"GlycanIUPAC_T901","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G46661GX\""},{"id":"GlycanIUPAC_T902","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G46661GX\""},{"id":"GlycanIUPAC_T903","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G53431DX\""},{"id":"GlycanIUPAC_T904","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G53431DX\""},{"id":"GlycanIUPAC_T905","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G71815PL\""},{"id":"GlycanIUPAC_T906","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G71815PL\""},{"id":"GlycanIUPAC_T907","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G97173UR\""},{"id":"GlycanIUPAC_T908","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G97173UR\""},{"id":"GlycanIUPAC_T909","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G53453JD\""},{"id":"GlycanIUPAC_T910","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G53453JD\""},{"id":"GlycanIUPAC_T911","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G48975CP\""},{"id":"GlycanIUPAC_T912","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G48975CP\""},{"id":"GlycanIUPAC_T913","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G87775XT\""},{"id":"GlycanIUPAC_T914","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G87775XT\""},{"id":"GlycanIUPAC_T915","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G48463GY\""},{"id":"GlycanIUPAC_T916","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G48463GY\""},{"id":"GlycanIUPAC_T917","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G54042BQ\""},{"id":"GlycanIUPAC_T918","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G54042BQ\""},{"id":"GlycanIUPAC_T919","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G99993MV\""},{"id":"GlycanIUPAC_T920","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G99993MV\""},{"id":"GlycanIUPAC_T921","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G81407LL\""},{"id":"GlycanIUPAC_T922","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G81407LL\""},{"id":"GlycanIUPAC_T923","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G46430YF\""},{"id":"GlycanIUPAC_T924","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G46430YF\""},{"id":"GlycanIUPAC_T925","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G86548QQ\""},{"id":"GlycanIUPAC_T926","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G86548QQ\""},{"id":"GlycanIUPAC_T927","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G25645HZ\""},{"id":"GlycanIUPAC_T928","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G25645HZ\""},{"id":"GlycanIUPAC_T929","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G73880WZ\""},{"id":"GlycanIUPAC_T930","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G73880WZ\""},{"id":"GlycanIUPAC_T931","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G12979RT\""},{"id":"GlycanIUPAC_T932","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G12979RT\""},{"id":"GlycanIUPAC_T933","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G36146RU\""},{"id":"GlycanIUPAC_T934","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G36146RU\""},{"id":"GlycanIUPAC_T935","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G23944RZ\""},{"id":"GlycanIUPAC_T936","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G23944RZ\""},{"id":"GlycanIUPAC_T937","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G67041BN\""},{"id":"GlycanIUPAC_T938","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G67041BN\""},{"id":"GlycanIUPAC_T939","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G95408HX\""},{"id":"GlycanIUPAC_T940","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G95408HX\""},{"id":"GlycanIUPAC_T941","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G31094CC\""},{"id":"GlycanIUPAC_T942","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G31094CC\""},{"id":"GlycanIUPAC_T943","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G99598GU\""},{"id":"GlycanIUPAC_T944","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G99598GU\""},{"id":"GlycanIUPAC_T945","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G94072IC\""},{"id":"GlycanIUPAC_T946","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G94072IC\""},{"id":"GlycanIUPAC_T947","span":{"begin":670,"end":673},"obj":"\"http://rdf.glycoinfo.org/glycan/G09523ZS\""},{"id":"GlycanIUPAC_T948","span":{"begin":2291,"end":2294},"obj":"\"http://rdf.glycoinfo.org/glycan/G09523ZS\""}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":214,"end":227},"obj":"gene:7841"},{"id":"T1","span":{"begin":132,"end":151},"obj":"disease:C0242354"},{"id":"T2","span":{"begin":214,"end":227},"obj":"gene:7841"},{"id":"T3","span":{"begin":170,"end":177},"obj":"disease:C1853736"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"},{"id":"R2","pred":"associated_with","subj":"T2","obj":"T3"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":61,"end":85},"obj":"Disease"},{"id":"T2","span":{"begin":87,"end":99},"obj":"Disease"},{"id":"T3","span":{"begin":132,"end":168},"obj":"Disease"},{"id":"T4","span":{"begin":170,"end":177},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0011629"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0011629"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0015286"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0011629"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":48,"end":55},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":392,"end":399},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":493,"end":500},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":2068,"end":2075},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":2081,"end":2086},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"137249"},{"id":"A4","pred":"db_id","subj":"T3","obj":"695940"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"},{"id":"A6","pred":"db_id","subj":"T6","obj":"9606"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":762,"end":773},"obj":"Body_part"},{"id":"T2","span":{"begin":1108,"end":1119},"obj":"Body_part"},{"id":"T3","span":{"begin":1477,"end":1486},"obj":"Body_part"},{"id":"T4","span":{"begin":1703,"end":1714},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000057"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000057"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000174"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000057"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}

{"project":"Glycosmos15-CL","denotations":[{"id":"T1","span":{"begin":762,"end":773},"obj":"Cell"},{"id":"T2","span":{"begin":1108,"end":1119},"obj":"Cell"},{"id":"T3","span":{"begin":1703,"end":1714},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000057"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000057"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000057"}],"text":"Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb).\nRecently, we reported a novel congenital disorder of glycosylation (CDG-IIb) caused by severe deficiency of the glucosidase I. The enzyme cleaves the alpha1,2-glucose residue from the asparagine-linked Glc(3)-Man(9)-GlcNAc(2) precursor, which is crucial for oligosaccharide maturation. The patient suffering from this disease was compound-heterozygous for two mutations in the glucosidase I gene, a T--\u003eC transition in the paternal allele and a G--\u003eC transition in the maternal allele. This gives rise in the glucosidase I polypeptide to the substitution of Arg486 by Thr and Phe652 by Leu, respectively. Kinetic studies using detergent extracts from cultured fibroblasts showed that the glucosidase I activity in the patient's cells was \u003c 1% of the control level, with intermediate values in the parental cells. No significant differences in the activities of other processing enzymes, including oligosaccharyltransferase, glucosidase II, and Man(9)-mannosidase, were observed. By contrast, the patient's fibroblasts displayed a two- to threefold higher endo-alpha1,2-mannosidase activity, associated with an increased level of enzyme-specific mRNA-transcripts. This points to the lack of glucosidase I activity being compensated for, to some extent, by increase in the activity of the pathway involving endo-alpha1,2-mannosidase; this would also explain the marked urinary excretion of Glc(3)-Man. Comparative analysis of [(3)H]mannose-labeled N-glycoproteins showed that, despite the dramatically reduced glucosidase I activity, the bulk of the N-linked carbohydrate chains (\u003e80%) in the patient's fibroblasts appeared to have been processed correctly, with only approximately 16% of the N-glycans being arrested at the Glc(3)-Man(9-7)-GlcNAc(2) stage. These structural and enzymatic data provide a reasonable basis for the observation that the sialotransferrin pattern, which frequently depends on the type of glycosylation disorder, appears to be normal in the patient. The human glucosidase I gene contains four exons separated by three introns with exon-4 encoding for the large 64-kDa catalytic domain of the enzyme. The two base mutations giving rise to substitution of Arg486 by Thr and Phe652 by Leu both reside in exon-4, consistent with their deleterious effect on enzyme activity. Incorporation of either mutation into wild-type glucosidase I resulted in the overexpression of enzyme mutants in COS 1 cells displaying no measurable catalytic activity. The Phe652Leu but not the Arg486Thr protein mutant showed a weak binding to a glucosidase I-specific affinity resin, indicating that the two amino acids affect polypeptide folding and active site formation differently."}