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嗜热细菌粪堆梭菌的模块化纤维素酶CelZ含有一个热稳定结构域。

The modular cellulase CelZ of the thermophilic bacterium Clostridium stercorarium contains a thermostabilizing domain.

作者信息

Riedel K, Ritter J, Bauer S, Bronnenmeier K

机构信息

Institut für Mikrobiologie, Technische Universität München, Germany.

出版信息

FEMS Microbiol Lett. 1998 Jul 15;164(2):261-7. doi: 10.1111/j.1574-6968.1998.tb13096.x.

DOI:10.1111/j.1574-6968.1998.tb13096.x
PMID:9682475
Abstract

The non-catalytic region of the Clostridium stercorarium cellulase CelZ (Avicelase I) comprises two protein segments (C and C') grouped into different subfamilies of cellulose-binding domain (CBD) family III. The C-terminally located family IIIb domain C was identified as a true cellulose-binding domain responsible for anchoring the CelZ enzyme to cellulose. The family IIIc domain C' immediately adjacent to the catalytic domain was unable to mediate binding to cellulose. A deletion study revealed a lack of independence of this pair of domains: almost the entire C' domain was required to maintain the catalytic activity and the thermostability of the enzyme.

摘要

粪堆梭菌纤维素酶CelZ（微晶纤维素酶I）的非催化区域由两个蛋白质片段（C和C'）组成，它们属于纤维素结合结构域（CBD）家族III的不同亚家族。位于C末端的家族IIIb结构域C被鉴定为真正的纤维素结合结构域，负责将CelZ酶锚定到纤维素上。紧邻催化结构域的家族IIIc结构域C'无法介导与纤维素的结合。一项缺失研究表明这两个结构域缺乏独立性：几乎整个C'结构域对于维持酶的催化活性和热稳定性都是必需的。

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