4.6 Review

Glycoside Hydrolases: Catalytic Base/Nucleophile Diversity

Journal

BIOTECHNOLOGY AND BIOENGINEERING
Volume 107, Issue 2, Pages 195-205

Publisher

WILEY
DOI: 10.1002/bit.22838

Keywords

glycoside hydrolases; catalytic mechanism; catalytic base; nucleophile; diversity

Funding

  1. DOE Office of Biological and Environmental Research

Ask authors/readers for more resources

Recent studies have shown that a number of glycoside hydrolase families do not follow the classical catalytic mechanisms, as they lack a typical catalytic base/nucleophile. A variety of mechanisms are used to replace this function, including substrate-assisted catalysis, a network of several residues, and the use of non-carboxylate residues or exogenous nucleophiles. Removal of the catalytic base/nucleophile by mutation can have a profound impact on substrate specificity, producing enzymes with completely new functions. Biotechnol. Bioeng. 2010;107: 195-205. (c) 2010 Wiley Periodicals, Inc.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.6
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available