Toggle Main Menu Toggle Search

Open Access padlockePrints

The N-terminal family 22 carbohydrate-binding module of xylanase 10B of Clostridium themocellum is not a thermostabilizing domain

Lookup NU author(s): Emeritus Professor Harry Gilbert


Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


Xylanase Xyn10B from Clostridium thermocellum is a modular enzyme that contains two family 22 carbohydrate binding modules N- (CBM22-1) and C- (CBM22-2) terminal of the family 10 glycoside hydrolase catalytic domain (GH10). In a previous study, we showed that removal of CBM22-1 reduces the resistance to thermoinactivation of the enzyme suggesting that this module is a thermo stabilizing domain. Here, we show that it is the module border on the N-terminal side of GH10 that confers resistance to thermoinactivation and to proteolysis. Therefore, CBM22-1 does not function as a thermostabilizing domain and the role for this apparently non-functional CBM remains elusive. (C) 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.

Publication metadata

Author(s): Dias FMV, Goyal A, Gilbert HJ, Prates JAM, Ferreira LMA, Fontes CMGA

Publication type: Article

Publication status: Published

Journal: FEMS Microbiology Letters

Year: 2004

Volume: 238

Issue: 1

Pages: 71-78

ISSN (print): 0378-1097

ISSN (electronic): 1574-6968

Publisher: Elsevier


DOI: 10.1016/j.femsle.2004.07.019


Altmetrics provided by Altmetric