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热纤梭菌几丁质酶 C 端结构域和催化结构域末端残基对酶活性和热稳定性的影响。

Effect of the C-terminal domains and terminal residues of catalytic domain on enzymatic activity and thermostability of lichenase from Clostridium thermocellum.

机构信息

College of Animal Sciences, Zhejiang University, 310029, Hangzhou, China.

出版信息

Biotechnol Lett. 2010 Jul;32(7):963-7. doi: 10.1007/s10529-010-0241-9. Epub 2010 Mar 13.

DOI:10.1007/s10529-010-0241-9
PMID:20229062
Abstract

To elucidate the effects of C-terminal domains of LicMB (mature lichenase from Clostridium thermocellum) and terminal residues of LicMB-CD (catalytic domain of LicMB) on the properties of lichenase, a series of truncated genes were constructed and expressed in E. coli. The Thr-Pro box had a positive effect while the dockerin domain had a negative impact on the properties of LicMB. The N-terminal 10-25th and C-terminal 1-9th residues of LicMB-CD were necessary to retain high thermostability while the N-terminal 1-7th and C-terminal 1-3rd residues were not necessary to maintain enzymatic activity.

摘要

为了阐明来自热纤梭菌的 C 端结构域的 LicMB(成熟的几丁质酶)和 LicMB-CD(LicMB 的催化结构域)的末端残基对几丁质酶性质的影响,构建了一系列截短基因,并在大肠杆菌中进行表达。Thr-Pro 盒具有积极影响,而 dockerin 结构域对 LicMB 的性质具有负面影响。LicMB-CD 的 N 端 10-25 位和 C 端 1-9 位残基是保留高耐热性所必需的,而 N 端 1-7 位和 C 端 1-3 位残基对于保持酶活性不是必需的。

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