Format

Send to

Choose Destination
See comment in PubMed Commons below
Curr Opin Biotechnol. 2014 Jun;27:96-106. doi: 10.1016/j.copbio.2013.12.002. Epub 2014 Jan 4.

Towards a molecular-level theory of carbohydrate processivity in glycoside hydrolases.

Author information

1
National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401, United States. Electronic address: Gregg.Beckham@nrel.gov.
2
Swedish University of Agricultural Sciences, SE 75007 Uppsala, Sweden. Electronic address: Jerry.Stahlberg@slu.edu.
3
National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401, United States.
4
Biosciences Center, National Renewable Energy Laboratory, Golden, CO 80401, United States.
5
Swedish University of Agricultural Sciences, SE 75007 Uppsala, Sweden.
6
Department of Chemistry, Biotechnology, and Food Science, Norwegian University of Life Sciences, N-1432 Ås, Norway.
7
Department of Chemical and Materials Engineering, University of Kentucky, Lexington, KY 40506, United States; Center for Computational Sciences, University of Kentucky, Lexington, KY 40506, United States. Electronic address: Christy.Payne@uky.edu.

Abstract

Polysaccharide depolymerization in nature is primarily accomplished by processive glycoside hydrolases (GHs), which abstract single carbohydrate chains from polymer crystals and cleave glycosidic linkages without dissociating after each catalytic event. Understanding the molecular-level features and structural aspects of processivity is of importance due to the prevalence of processive GHs in biomass-degrading enzyme cocktails. Here, we describe recent advances towards the development of a molecular-level theory of processivity for cellulolytic and chitinolytic enzymes, including the development of novel methods for measuring rates of key steps in processive action and insights gained from structural and computational studies. Overall, we present a framework for developing structure-function relationships in processive GHs and outline additional progress towards developing a fundamental understanding of these industrially important enzymes.

PMID:
24863902
DOI:
10.1016/j.copbio.2013.12.002
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center