PubMed:9147049 JSONTXT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":485,"end":498},"obj":"http://purl.obolibrary.org/obo/MAT_0000073"},{"id":"T2","span":{"begin":493,"end":498},"obj":"http://purl.obolibrary.org/obo/MAT_0000021"},{"id":"T3","span":{"begin":932,"end":945},"obj":"http://purl.obolibrary.org/obo/MAT_0000073"},{"id":"T4","span":{"begin":940,"end":945},"obj":"http://purl.obolibrary.org/obo/MAT_0000021"}],"text":"Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.\nAs the enzyme that initiates the maturation phase of the oligosaccharide moiety of N-linked glycoproteins, glucosidase I controls the flux of carbohydrate during the biosynthesis of these proteins. In a previous study to elucidate the structure-function relationships, we reported the presence of a cysteine residue at or near the active site of the enzyme from the bovine mammary gland (Pukazhenthi,B.S., Muniappa,N. and Vijay,I.K., 1993, J. Biol. Chem., 268, 6445-6452). We have now extended this approach to identify the participation of an arginine and a tryptophan residue in the enzyme that may play an important role in binding the substrate. The data have been combined with the results of the previous study and the cDNA-derived sequence to propose a ERHLDLRCW motif in the active site of the enzyme in the rat mammary gland that is involved in binding the incipient glycoprotein substrate for processing."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":111},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":112,"end":309},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":310,"end":554},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":555,"end":560},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":561,"end":584},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":585,"end":761},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":762,"end":1026},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":111},"obj":"Sentence"},{"id":"T2","span":{"begin":112,"end":309},"obj":"Sentence"},{"id":"T3","span":{"begin":310,"end":584},"obj":"Sentence"},{"id":"T4","span":{"begin":585,"end":761},"obj":"Sentence"},{"id":"T5","span":{"begin":762,"end":1026},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":111},"obj":"Sentence"},{"id":"T2","span":{"begin":112,"end":309},"obj":"Sentence"},{"id":"T3","span":{"begin":310,"end":554},"obj":"Sentence"},{"id":"T4","span":{"begin":555,"end":560},"obj":"Sentence"},{"id":"T5","span":{"begin":561,"end":584},"obj":"Sentence"},{"id":"T6","span":{"begin":585,"end":761},"obj":"Sentence"},{"id":"T7","span":{"begin":762,"end":1026},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.\nAs the enzyme that initiates the maturation phase of the oligosaccharide moiety of N-linked glycoproteins, glucosidase I controls the flux of carbohydrate during the biosynthesis of these proteins. In a previous study to elucidate the structure-function relationships, we reported the presence of a cysteine residue at or near the active site of the enzyme from the bovine mammary gland (Pukazhenthi,B.S., Muniappa,N. and Vijay,I.K., 1993, J. Biol. Chem., 268, 6445-6452). We have now extended this approach to identify the participation of an arginine and a tryptophan residue in the enzyme that may play an important role in binding the substrate. The data have been combined with the results of the previous study and the cDNA-derived sequence to propose a ERHLDLRCW motif in the active site of the enzyme in the rat mammary gland that is involved in binding the incipient glycoprotein substrate for processing."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":51,"end":62},"obj":"FMAID:196728"},{"id":"_T2","span":{"begin":51,"end":62},"obj":"FMAID:82739"},{"id":"_T3","span":{"begin":169,"end":184},"obj":"FMAID:82742"},{"id":"_T4","span":{"begin":169,"end":184},"obj":"FMAID:196731"},{"id":"_T5","span":{"begin":204,"end":217},"obj":"FMAID:62925"},{"id":"_T6","span":{"begin":204,"end":217},"obj":"FMAID:167256"},{"id":"_T7","span":{"begin":254,"end":266},"obj":"FMAID:82737"},{"id":"_T8","span":{"begin":254,"end":266},"obj":"FMAID:197276"},{"id":"_T9","span":{"begin":300,"end":308},"obj":"FMAID:67257"},{"id":"_T10","span":{"begin":300,"end":308},"obj":"FMAID:165447"},{"id":"_T11","span":{"begin":411,"end":419},"obj":"FMAID:196740"},{"id":"_T12","span":{"begin":411,"end":419},"obj":"FMAID:82751"},{"id":"_T13","span":{"begin":485,"end":498},"obj":"FMAID:157661"},{"id":"_T14","span":{"begin":493,"end":498},"obj":"FMAID:86294"},{"id":"_T15","span":{"begin":493,"end":498},"obj":"FMAID:172512"},{"id":"_T16","span":{"begin":493,"end":498},"obj":"FMAID:200677"},{"id":"_T17","span":{"begin":656,"end":664},"obj":"FMAID:82763"},{"id":"_T18","span":{"begin":656,"end":664},"obj":"FMAID:196752"},{"id":"_T19","span":{"begin":671,"end":681},"obj":"FMAID:82767"},{"id":"_T20","span":{"begin":671,"end":681},"obj":"FMAID:196756"},{"id":"_T21","span":{"begin":928,"end":945},"obj":"FMAID:157669"},{"id":"_T22","span":{"begin":928,"end":945},"obj":"FMAID:157665"},{"id":"_T23","span":{"begin":928,"end":945},"obj":"FMAID:57987"},{"id":"_T24","span":{"begin":928,"end":945},"obj":"FMAID:57991"},{"id":"_T25","span":{"begin":932,"end":945},"obj":"FMAID:157661"},{"id":"_T26","span":{"begin":940,"end":945},"obj":"FMAID:86294"},{"id":"_T27","span":{"begin":940,"end":945},"obj":"FMAID:200677"},{"id":"_T28","span":{"begin":940,"end":945},"obj":"FMAID:172512"},{"id":"_T29","span":{"begin":988,"end":1000},"obj":"FMAID:167256"},{"id":"_T30","span":{"begin":988,"end":1000},"obj":"FMAID:62925"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.\nAs the enzyme that initiates the maturation phase of the oligosaccharide moiety of N-linked glycoproteins, glucosidase I controls the flux of carbohydrate during the biosynthesis of these proteins. In a previous study to elucidate the structure-function relationships, we reported the presence of a cysteine residue at or near the active site of the enzyme from the bovine mammary gland (Pukazhenthi,B.S., Muniappa,N. and Vijay,I.K., 1993, J. Biol. Chem., 268, 6445-6452). We have now extended this approach to identify the participation of an arginine and a tryptophan residue in the enzyme that may play an important role in binding the substrate. The data have been combined with the results of the previous study and the cDNA-derived sequence to propose a ERHLDLRCW motif in the active site of the enzyme in the rat mammary gland that is involved in binding the incipient glycoprotein substrate for processing."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":278,"end":290},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T2","span":{"begin":278,"end":308},"obj":"http://purl.obolibrary.org/obo/GO_0006412"},{"id":"T3","span":{"begin":443,"end":468},"obj":"http://purl.obolibrary.org/obo/GO_0018307"},{"id":"T4","span":{"begin":895,"end":920},"obj":"http://purl.obolibrary.org/obo/GO_0018307"}],"text":"Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.\nAs the enzyme that initiates the maturation phase of the oligosaccharide moiety of N-linked glycoproteins, glucosidase I controls the flux of carbohydrate during the biosynthesis of these proteins. In a previous study to elucidate the structure-function relationships, we reported the presence of a cysteine residue at or near the active site of the enzyme from the bovine mammary gland (Pukazhenthi,B.S., Muniappa,N. and Vijay,I.K., 1993, J. Biol. Chem., 268, 6445-6452). We have now extended this approach to identify the participation of an arginine and a tryptophan residue in the enzyme that may play an important role in binding the substrate. The data have been combined with the results of the previous study and the cDNA-derived sequence to propose a ERHLDLRCW motif in the active site of the enzyme in the rat mammary gland that is involved in binding the incipient glycoprotein substrate for processing."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":75,"end":82},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T2","span":{"begin":739,"end":746},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":966,"end":973},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T4","span":{"begin":75,"end":82},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T5","span":{"begin":739,"end":746},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T6","span":{"begin":966,"end":973},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T7","span":{"begin":75,"end":82},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T8","span":{"begin":739,"end":746},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T9","span":{"begin":966,"end":973},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T10","span":{"begin":75,"end":82},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T11","span":{"begin":739,"end":746},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12","span":{"begin":966,"end":973},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.\nAs the enzyme that initiates the maturation phase of the oligosaccharide moiety of N-linked glycoproteins, glucosidase I controls the flux of carbohydrate during the biosynthesis of these proteins. In a previous study to elucidate the structure-function relationships, we reported the presence of a cysteine residue at or near the active site of the enzyme from the bovine mammary gland (Pukazhenthi,B.S., Muniappa,N. and Vijay,I.K., 1993, J. Biol. Chem., 268, 6445-6452). We have now extended this approach to identify the participation of an arginine and a tryptophan residue in the enzyme that may play an important role in binding the substrate. The data have been combined with the results of the previous study and the cDNA-derived sequence to propose a ERHLDLRCW motif in the active site of the enzyme in the rat mammary gland that is involved in binding the incipient glycoprotein substrate for processing."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":485,"end":498},"obj":"http://purl.obolibrary.org/obo/UBERON_0001911"},{"id":"T2","span":{"begin":932,"end":945},"obj":"http://purl.obolibrary.org/obo/UBERON_0001911"},{"id":"T3","span":{"begin":493,"end":498},"obj":"http://purl.obolibrary.org/obo/UBERON_0002530"},{"id":"T4","span":{"begin":940,"end":945},"obj":"http://purl.obolibrary.org/obo/UBERON_0002530"}],"text":"Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.\nAs the enzyme that initiates the maturation phase of the oligosaccharide moiety of N-linked glycoproteins, glucosidase I controls the flux of carbohydrate during the biosynthesis of these proteins. In a previous study to elucidate the structure-function relationships, we reported the presence of a cysteine residue at or near the active site of the enzyme from the bovine mammary gland (Pukazhenthi,B.S., Muniappa,N. and Vijay,I.K., 1993, J. Biol. Chem., 268, 6445-6452). We have now extended this approach to identify the participation of an arginine and a tryptophan residue in the enzyme that may play an important role in binding the substrate. The data have been combined with the results of the previous study and the cDNA-derived sequence to propose a ERHLDLRCW motif in the active site of the enzyme in the rat mammary gland that is involved in binding the incipient glycoprotein substrate for processing."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":485,"end":498},"obj":"http://purl.obolibrary.org/obo/MAT_0000073"},{"id":"T2","span":{"begin":493,"end":498},"obj":"http://purl.obolibrary.org/obo/MAT_0000021"},{"id":"T3","span":{"begin":932,"end":945},"obj":"http://purl.obolibrary.org/obo/MAT_0000073"},{"id":"T4","span":{"begin":940,"end":945},"obj":"http://purl.obolibrary.org/obo/MAT_0000021"}],"text":"Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.\nAs the enzyme that initiates the maturation phase of the oligosaccharide moiety of N-linked glycoproteins, glucosidase I controls the flux of carbohydrate during the biosynthesis of these proteins. In a previous study to elucidate the structure-function relationships, we reported the presence of a cysteine residue at or near the active site of the enzyme from the bovine mammary gland (Pukazhenthi,B.S., Muniappa,N. and Vijay,I.K., 1993, J. Biol. Chem., 268, 6445-6452). We have now extended this approach to identify the participation of an arginine and a tryptophan residue in the enzyme that may play an important role in binding the substrate. The data have been combined with the results of the previous study and the cDNA-derived sequence to propose a ERHLDLRCW motif in the active site of the enzyme in the rat mammary gland that is involved in binding the incipient glycoprotein substrate for processing."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":485,"end":498},"obj":"http://purl.obolibrary.org/obo/UBERON_0001911"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":932,"end":945},"obj":"http://purl.obolibrary.org/obo/UBERON_0001911"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":493,"end":498},"obj":"http://purl.obolibrary.org/obo/UBERON_0002530"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":940,"end":945},"obj":"http://purl.obolibrary.org/obo/UBERON_0002530"}],"text":"Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.\nAs the enzyme that initiates the maturation phase of the oligosaccharide moiety of N-linked glycoproteins, glucosidase I controls the flux of carbohydrate during the biosynthesis of these proteins. In a previous study to elucidate the structure-function relationships, we reported the presence of a cysteine residue at or near the active site of the enzyme from the bovine mammary gland (Pukazhenthi,B.S., Muniappa,N. and Vijay,I.K., 1993, J. Biol. Chem., 268, 6445-6452). We have now extended this approach to identify the participation of an arginine and a tryptophan residue in the enzyme that may play an important role in binding the substrate. The data have been combined with the results of the previous study and the cDNA-derived sequence to propose a ERHLDLRCW motif in the active site of the enzyme in the rat mammary gland that is involved in binding the incipient glycoprotein substrate for processing."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":478,"end":484},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":928,"end":931},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9913"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10114"},{"id":"A3","pred":"db_id","subj":"T2","obj":"10116"}],"text":"Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.\nAs the enzyme that initiates the maturation phase of the oligosaccharide moiety of N-linked glycoproteins, glucosidase I controls the flux of carbohydrate during the biosynthesis of these proteins. In a previous study to elucidate the structure-function relationships, we reported the presence of a cysteine residue at or near the active site of the enzyme from the bovine mammary gland (Pukazhenthi,B.S., Muniappa,N. and Vijay,I.K., 1993, J. Biol. Chem., 268, 6445-6452). We have now extended this approach to identify the participation of an arginine and a tryptophan residue in the enzyme that may play an important role in binding the substrate. The data have been combined with the results of the previous study and the cDNA-derived sequence to propose a ERHLDLRCW motif in the active site of the enzyme in the rat mammary gland that is involved in binding the incipient glycoprotein substrate for processing."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":485,"end":498},"obj":"Body_part"},{"id":"T3","span":{"begin":932,"end":945},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001911"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0005200"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001911"},{"id":"A4","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0005200"}],"text":"Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.\nAs the enzyme that initiates the maturation phase of the oligosaccharide moiety of N-linked glycoproteins, glucosidase I controls the flux of carbohydrate during the biosynthesis of these proteins. In a previous study to elucidate the structure-function relationships, we reported the presence of a cysteine residue at or near the active site of the enzyme from the bovine mammary gland (Pukazhenthi,B.S., Muniappa,N. and Vijay,I.K., 1993, J. Biol. Chem., 268, 6445-6452). We have now extended this approach to identify the participation of an arginine and a tryptophan residue in the enzyme that may play an important role in binding the substrate. The data have been combined with the results of the previous study and the cDNA-derived sequence to propose a ERHLDLRCW motif in the active site of the enzyme in the rat mammary gland that is involved in binding the incipient glycoprotein substrate for processing."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":485,"end":498},"obj":"Body_part"},{"id":"T2","span":{"begin":932,"end":945},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000073"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000073"}],"text":"Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.\nAs the enzyme that initiates the maturation phase of the oligosaccharide moiety of N-linked glycoproteins, glucosidase I controls the flux of carbohydrate during the biosynthesis of these proteins. In a previous study to elucidate the structure-function relationships, we reported the presence of a cysteine residue at or near the active site of the enzyme from the bovine mammary gland (Pukazhenthi,B.S., Muniappa,N. and Vijay,I.K., 1993, J. Biol. Chem., 268, 6445-6452). We have now extended this approach to identify the participation of an arginine and a tryptophan residue in the enzyme that may play an important role in binding the substrate. The data have been combined with the results of the previous study and the cDNA-derived sequence to propose a ERHLDLRCW motif in the active site of the enzyme in the rat mammary gland that is involved in binding the incipient glycoprotein substrate for processing."}