PubMed:9147049 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/9147049","sourcedb":"PubMed","sourceid":"9147049","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/9147049","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 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