Physical association of the catalytic and helper modules of a family-9 glycoside hydrolase is essential for activity-Reference-Cited by-同舟云学术

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Physical association of the catalytic and helper modules of a family-9 glycoside hydrolase is essential for activity

Published:2009-02-12 Issue:5 Volume:583 Page:879-884
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Burstein Tal,Shulman Michal,Jindou Sadanari,Petkun Svetlana,Frolow Felix,Shoham Yuval,Bayer Edward A.,Lamed Raphael

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference22 articles.

1. The carbohydrate-active enzymes database (CAZy): an expert resource for glycogenomics;Cantarel;Nucl. Acid Res.,2009

2. Carbohydrate-binding modules: fine-tuning polysaccharide recognition;Boraston;Biochem. J.,2004

3. Cellulose, cellulases and cellulosomes;Bayer;Curr. Opin. Struct. Biol.,1998

4. Cellulose-decomposing prokaryotes and their enzyme systems;Bayer,2006

5. Gene sequence and properties of CelI, a family E endoglucanase from Clostridium thermocellum;Hazlewood;J. Gen. Microbiol.,1993

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2. Molecular mechanism of cellulose depolymerization by the two-domain BlCel9A enzyme from the glycoside hydrolase family 9;Carbohydrate Polymers;2024-04

3. Enhancing the Catalytic Efficiency of Non-Modular Processive Endoglucanase Eg5c-1 by Incorporating an Extra Carbohydrate Binding Module;2024

4. Role of carbohydrate binding modules, CBM3A and CBM3B in stability and catalysis by a β-1,4 endoglucanase, AtGH9C-CBM3A-CBM3B from Acetivibrio thermocellus ATCC 27405;International Journal of Biological Macromolecules;2023-07

5. Processive binding mechanism of Cel9G from Clostridium cellulovorans: molecular dynamics and free energy landscape investigations;Physical Chemistry Chemical Physics;2023

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