Literature DB >> 24863902

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

Gregg T Beckham1, Jerry Ståhlberg2, Brandon C Knott3, Michael E Himmel4, Michael F Crowley4, Mats Sandgren5, Morten Sørlie6, Christina M Payne7.   

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.
Copyright © 2013 Elsevier Ltd. All rights reserved.

Entities:  

Mesh:

Substances:

Year:  2014        PMID: 24863902     DOI: 10.1016/j.copbio.2013.12.002

Source DB:  PubMed          Journal:  Curr Opin Biotechnol        ISSN: 0958-1669            Impact factor:   9.740


  22 in total

1.  Slow Off-rates and Strong Product Binding Are Required for Processivity and Efficient Degradation of Recalcitrant Chitin by Family 18 Chitinases.

Authors:  Mihhail Kurašin; Silja Kuusk; Piret Kuusk; Morten Sørlie; Priit Väljamäe
Journal:  J Biol Chem       Date:  2015-10-14       Impact factor: 5.157

Review 2.  Physiological and Molecular Understanding of Bacterial Polysaccharide Monooxygenases.

Authors:  Marco Agostoni; John A Hangasky; Michael A Marletta
Journal:  Microbiol Mol Biol Rev       Date:  2017-06-28       Impact factor: 11.056

3.  Advantages of a distant cellulase catalytic base.

Authors:  Tucker Burgin; Jerry Ståhlberg; Heather B Mayes
Journal:  J Biol Chem       Date:  2018-01-10       Impact factor: 5.157

4.  Kinetics of cellobiohydrolase (Cel7A) variants with lowered substrate affinity.

Authors:  Jeppe Kari; Johan Olsen; Kim Borch; Nicolaj Cruys-Bagger; Kenneth Jensen; Peter Westh
Journal:  J Biol Chem       Date:  2014-09-30       Impact factor: 5.157

5.  Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A.

Authors:  Riin Kont; Jeppe Kari; Kim Borch; Peter Westh; Priit Väljamäe
Journal:  J Biol Chem       Date:  2016-10-25       Impact factor: 5.157

6.  Characterization of Wall Teichoic Acid Degradation by the Bacteriophage ϕ29 Appendage Protein GP12 Using Synthetic Substrate Analogs.

Authors:  Cullen L Myers; Ronald G Ireland; Teresa A Garrett; Eric D Brown
Journal:  J Biol Chem       Date:  2015-06-17       Impact factor: 5.157

7.  Probing substrate interactions in the active tunnel of a catalytically deficient cellobiohydrolase (Cel7).

Authors:  Francieli Colussi; Trine H Sørensen; Kadri Alasepp; Jeppe Kari; Nicolaj Cruys-Bagger; Michael S Windahl; Johan P Olsen; Kim Borch; Peter Westh
Journal:  J Biol Chem       Date:  2014-12-04       Impact factor: 5.157

8.  The predominant molecular state of bound enzyme determines the strength and type of product inhibition in the hydrolysis of recalcitrant polysaccharides by processive enzymes.

Authors:  Silja Kuusk; Morten Sørlie; Priit Väljamäe
Journal:  J Biol Chem       Date:  2015-03-12       Impact factor: 5.157

9.  The dissociation mechanism of processive cellulases.

Authors:  Josh V Vermaas; Riin Kont; Gregg T Beckham; Michael F Crowley; Mikael Gudmundsson; Mats Sandgren; Jerry Ståhlberg; Priit Väljamäe; Brandon C Knott
Journal:  Proc Natl Acad Sci U S A       Date:  2019-10-30       Impact factor: 11.205

10.  Reassembly and co-crystallization of a family 9 processive endoglucanase from its component parts: structural and functional significance of the intermodular linker.

Authors:  Svetlana Petkun; Inna Rozman Grinberg; Raphael Lamed; Sadanari Jindou; Tal Burstein; Oren Yaniv; Yuval Shoham; Linda J W Shimon; Edward A Bayer; Felix Frolow
Journal:  PeerJ       Date:  2015-09-15       Impact factor: 2.984

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.