Selective elongation of the oligosaccharide attached to the second potential glycosylation site of yeast exoglucanase: effects on the activity and properties of the enzyme.

doi:10.1042/bj3040917

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Article

Selective elongation of the oligosaccharide attached to the second potential glycosylation site of yeast exoglucanase: effects on the activity and properties of the enzyme.

The Biochemical journal - 15 Dec 1994

Basco R D, Hernández L M, Muñox M D, Olivero I, Andaluz E, Del Rey F, Larriba G

Abstract excerpt

Three exoglucanases (Exgs), ExgIa, ExgIb and Exg325, are secreted by Saccharomyces cerevisiae cells. They share a common protein portion with two potential glycosylation sites (sequons) but differ in the amount of N-linked carbohydrate [Basco, R.D., Muñoz, M.D., Hernández, L.M., Váquez de Aldana, C. and Larriba, G. (1993) Yeast 9, 221-234]. ExgIb contains two short oligosaccharides attached to asparagines (Asn)...

Topics

Binding Sites
Enzyme Activation
Enzyme Stability
Fungal Proteins
Glucan 1,3-beta-Glucosidase
Glycosylation
Heating
Isoenzymes
Kinetics
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutagenesis, Site-Directed

Mutation

Oligosaccharides

Saccharomyces cerevisiae

Structure-Activity Relationship

Time Factors

beta-Glucosidase

Source

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Identifiers

PMID: 7818498
DOI: 10.1042/bj3040917
PMCID: PMC1137420

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7818498-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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