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Glycobiology. 1997 Apr;7(3):399-404.

Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.

Author information

1
Department of Animal Sciences, University of Maryland, College Park 20742, USA.

Abstract

As 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.

PMID:
9147049
DOI:
10.1093/glycob/7.3.399
[Indexed for MEDLINE]

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