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Determination of the molecular states of the processive endocellulase Thermobifida fusca Cel9A during crystalline cellulose depolymerization by Maxim Kostylev; Jose M. Moran-Mirabal; Larry P. Walker; David B. Wilson is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Detailed understanding of cell wall degrading enzymes is important for their modeling and industrial applications, including in the production of biofuels. Here we used Cel9A, a processive endocellulase from __Thermobifida fusca,__ to demonstrate that cellulases that contain a catalytic domain (CD) attached to a cellulose binding module (CBM) by a flexible linker exist in three distinct molecular states. By measuring the ability of a soluble competitor to reduce Cel9A activity on an insoluble substrate, we show that the most common state of Cel9A is bound via its CBM, but with its CD unoccupied by the insoluble substrate. These findings are relevant for kinetic modeling and microscopy studies of modular glycoside hydrolases. Biotechnol. Bioeng. 2012;109: 295–299. © 2011 Wiley Periodicals, Inc.

Who reads Determination of the molecular states of the processive endocellulase Thermobifida fusca Cel9A during crystalline cellulose depolymerization?

Author

Maxim Kostylev; Jose M. Moran-Mirabal; Larry P. Walker; David B. Wilson

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley - V C H Verlag GmbbH & Co.; Wiley (ISSN 0006-3592)

Published

2011

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)