The N-terminal family 22 carbohydrate-binding module of xylanase 10B of Clostridium themocellum is not a thermostabilizing domain
The N-terminal family 22 carbohydrate-binding module of xylanase 10B of Clostridium themocellum is not a thermostabilizing domain
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DOI：
10.1016/j.femsle.2004.07.019
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发表时间：
2004-09-01
影响因子：
2.1
通讯作者：
Fontes, CMGA
中科院分区：
文献类型：
--
作者：
Dias, FMV;Goyal, A;Fontes, CMGA
来自热纤梭菌的木聚糖酶Xyn 10 B是一种模块化酶，其含有家族10糖苷水解酶催化结构域（GH 10）的N-（CBM 22 -1）和C-（CBM 22 -2）末端的两个家族22碳水化合物结合模块。在先前的研究中，我们表明，去除CBM 22 -1降低了对酶热失活的抗性，这表明该模块是一个热稳定域。在这里，我们表明，它是模块边界上的N-末端侧的GH 10赋予电阻热灭活和蛋白水解。因此，CBM 22 -1不作为热稳定结构域发挥作用，并且这种明显无功能的CBM的作用仍然难以捉摸。(C)2004年，欧洲微生物学会联合会。Elsevier B. V.出版，保留所有权利。
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.