Open AccessThe N‐terminal family 22 carbohydrate‐binding module of xylanase 10B of Clostridium themocellum is not a thermostabilizing domain
Author(s) -
Dias Fernando M.V.,
Goyal Arun,
Gilbert Harry J.,
Prates José A.M.,
Ferreira Luís M.A.,
Fontes Carlos M.G.A.
Publication year - 2004
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2004.tb09739.x
Subject(s) - terminal (telecommunication) , xylanase , carbohydrate , chemistry , carbohydrate binding module , domain (mathematical analysis) , biochemistry , computer science , glycoside hydrolase , enzyme , mathematics , telecommunications , mathematical analysis
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 thermostabilizing 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.