PubMed:10085243 JSONTXT

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":10,"end":15},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"T2","span":{"begin":417,"end":422},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"T3","span":{"begin":567,"end":572},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"T4","span":{"begin":940,"end":945},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"T5","span":{"begin":1075,"end":1080},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"T6","span":{"begin":1113,"end":1118},"obj":"https://acgg.asia/db/ggdb/info/gg219"}],"text":"Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis.\nGlycosylphosphatidylinositol (GPI) is used as a membrane anchor by many eukaryotic cell-surface proteins. The second step of GPI biosynthesis is de-N-acetylation of N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI). We have previously cloned the rat PIG-L gene by expression cloning that complemented a mutant Chinese hamster ovary cell line defective in this step. Here we show that recombinant rat PIG-L protein purified from Escherichia coli as a complex with GroEL has GlcNAc-PI de-N-acetylase activity in vitro. The activity was not enhanced by GTP, which is known to enhance the de-N-acetylase activity of mammalian cell microsomes. As with other de-N-acetylases that act on the GlcNAc moiety, metal ions, in particular Mn2+ and Ni2+, enhanced the enzyme activity of PIG-L. The Saccharomyces cerevisiae YMR281W open reading frame encodes a protein (termed Gpi12p) with 24% amino acid identity with rat PIG-L. On transfection into mammalian PIG-L-deficient cells, this gene, GPI12, restored the cell-surface expression of GPI-anchored proteins and GlcNAc-PI de-N-acetylase activity. The disruption of the gene caused lethality in S. cerevisiae. These results indicate that GlcNAc-PI de-N-acetylase is conserved between mammals and yeasts and that the de-N-acetylation step is also indispensable in yeasts."}

{"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":0,"end":163},"obj":"Sentence"},{"id":"T2","span":{"begin":164,"end":269},"obj":"Sentence"},{"id":"T3","span":{"begin":270,"end":382},"obj":"Sentence"},{"id":"T4","span":{"begin":383,"end":532},"obj":"Sentence"},{"id":"T5","span":{"begin":533,"end":683},"obj":"Sentence"},{"id":"T6","span":{"begin":684,"end":805},"obj":"Sentence"},{"id":"T7","span":{"begin":806,"end":946},"obj":"Sentence"},{"id":"T8","span":{"begin":947,"end":1081},"obj":"Sentence"},{"id":"T9","span":{"begin":1082,"end":1254},"obj":"Sentence"},{"id":"T10","span":{"begin":1255,"end":1316},"obj":"Sentence"},{"id":"T11","span":{"begin":1317,"end":1477},"obj":"Sentence"}],"text":"Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis.\nGlycosylphosphatidylinositol (GPI) is used as a membrane anchor by many eukaryotic cell-surface proteins. The second step of GPI biosynthesis is de-N-acetylation of N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI). We have previously cloned the rat PIG-L gene by expression cloning that complemented a mutant Chinese hamster ovary cell line defective in this step. Here we show that recombinant rat PIG-L protein purified from Escherichia coli as a complex with GroEL has GlcNAc-PI de-N-acetylase activity in vitro. The activity was not enhanced by GTP, which is known to enhance the de-N-acetylase activity of mammalian cell microsomes. As with other de-N-acetylases that act on the GlcNAc moiety, metal ions, in particular Mn2+ and Ni2+, enhanced the enzyme activity of PIG-L. The Saccharomyces cerevisiae YMR281W open reading frame encodes a protein (termed Gpi12p) with 24% amino acid identity with rat PIG-L. On transfection into mammalian PIG-L-deficient cells, this gene, GPI12, restored the cell-surface expression of GPI-anchored proteins and GlcNAc-PI de-N-acetylase activity. The disruption of the gene caused lethality in S. cerevisiae. These results indicate that GlcNAc-PI de-N-acetylase is conserved between mammals and yeasts and that the de-N-acetylation step is also indispensable in yeasts."}

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":10,"end":15},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"T2","span":{"begin":417,"end":422},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"T3","span":{"begin":567,"end":572},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"T4","span":{"begin":940,"end":945},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"T5","span":{"begin":1075,"end":1080},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"T6","span":{"begin":1113,"end":1118},"obj":"https://acgg.asia/db/ggdb/info/gg219"}],"text":"Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis.\nGlycosylphosphatidylinositol (GPI) is used as a membrane anchor by many eukaryotic cell-surface proteins. The second step of GPI biosynthesis is de-N-acetylation of N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI). We have previously cloned the rat PIG-L gene by expression cloning that complemented a mutant Chinese hamster ovary cell line defective in this step. Here we show that recombinant rat PIG-L protein purified from Escherichia coli as a complex with GroEL has GlcNAc-PI de-N-acetylase activity in vitro. The activity was not enhanced by GTP, which is known to enhance the de-N-acetylase activity of mammalian cell microsomes. As with other de-N-acetylases that act on the GlcNAc moiety, metal ions, in particular Mn2+ and Ni2+, enhanced the enzyme activity of PIG-L. The Saccharomyces cerevisiae YMR281W open reading frame encodes a protein (termed Gpi12p) with 24% amino acid identity with rat PIG-L. On transfection into mammalian PIG-L-deficient cells, this gene, GPI12, restored the cell-surface expression of GPI-anchored proteins and GlcNAc-PI de-N-acetylase activity. The disruption of the gene caused lethality in S. cerevisiae. These results indicate that GlcNAc-PI de-N-acetylase is conserved between mammals and yeasts and that the de-N-acetylation step is also indispensable in yeasts."}

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":10,"end":15},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":417,"end":422},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":567,"end":572},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":636,"end":639},"obj":"https://acgg.asia/db/ggdb/info/gg135"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":940,"end":945},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":1075,"end":1080},"obj":"https://acgg.asia/db/ggdb/info/gg219"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":1113,"end":1118},"obj":"https://acgg.asia/db/ggdb/info/gg219"}],"text":"Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis.\nGlycosylphosphatidylinositol (GPI) is used as a membrane anchor by many eukaryotic cell-surface proteins. The second step of GPI biosynthesis is de-N-acetylation of N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI). We have previously cloned the rat PIG-L gene by expression cloning that complemented a mutant Chinese hamster ovary cell line defective in this step. Here we show that recombinant rat PIG-L protein purified from Escherichia coli as a complex with GroEL has GlcNAc-PI de-N-acetylase activity in vitro. The activity was not enhanced by GTP, which is known to enhance the de-N-acetylase activity of mammalian cell microsomes. As with other de-N-acetylases that act on the GlcNAc moiety, metal ions, in particular Mn2+ and Ni2+, enhanced the enzyme activity of PIG-L. The Saccharomyces cerevisiae YMR281W open reading frame encodes a protein (termed Gpi12p) with 24% amino acid identity with rat PIG-L. On transfection into mammalian PIG-L-deficient cells, this gene, GPI12, restored the cell-surface expression of GPI-anchored proteins and GlcNAc-PI de-N-acetylase activity. The disruption of the gene caused lethality in S. cerevisiae. These results indicate that GlcNAc-PI de-N-acetylase is conserved between mammals and yeasts and that the de-N-acetylation step is also indispensable in yeasts."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":371,"end":377},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":640,"end":646},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":852,"end":858},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T4","span":{"begin":1220,"end":1226},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T5","span":{"begin":1345,"end":1351},"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":"Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis.\nGlycosylphosphatidylinositol (GPI) is used as a membrane anchor by many eukaryotic cell-surface proteins. The second step of GPI biosynthesis is de-N-acetylation of N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI). We have previously cloned the rat PIG-L gene by expression cloning that complemented a mutant Chinese hamster ovary cell line defective in this step. Here we show that recombinant rat PIG-L protein purified from Escherichia coli as a complex with GroEL has GlcNAc-PI de-N-acetylase activity in vitro. The activity was not enhanced by GTP, which is known to enhance the de-N-acetylase activity of mammalian cell microsomes. As with other de-N-acetylases that act on the GlcNAc moiety, metal ions, in particular Mn2+ and Ni2+, enhanced the enzyme activity of PIG-L. The Saccharomyces cerevisiae YMR281W open reading frame encodes a protein (termed Gpi12p) with 24% amino acid identity with rat PIG-L. On transfection into mammalian PIG-L-deficient cells, this gene, GPI12, restored the cell-surface expression of GPI-anchored proteins and GlcNAc-PI de-N-acetylase activity. The disruption of the gene caused lethality in S. cerevisiae. These results indicate that GlcNAc-PI de-N-acetylase is conserved between mammals and yeasts and that the de-N-acetylation step is also indispensable in yeasts."}