当前位置： SCI文献检索 > APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY期刊下所有文献 > Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02.

Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02.

Abstract：

:By sequence comparison, the majority of 1,4-α-glucan-branching enzymes (GBEs) consist of an N-terminal carbohydrate-binding domain, a TIM-barrel catalytic domain, and a C-terminal all-beta domain. Among these structures, the GBE from Geobacillus thermoglucosidans STB02 uniquely has a highly charged 26-amino-acid C-terminal extension, whose functional roles are the least understood. In this research, the functional significance of the C-terminal domain in GBE from G. thermoglucosidans STB02 and its extension were assessed using a C-terminal deletion analysis. Mutants lacking of more than 7 residues of the C-terminal all-beta domain could not be detected in lysates of their Escherichia coli expression strains, suggesting that an intact all-beta domain is required for structural stability. In contrast, truncation of the C-terminal extension resulted in greater stability and solubility than the wild type, as well as a lower sensitivity to the presence of added metal ions. Comparison of this mutant with the wild type suggests that the interaction of metal ions with the C-terminal extension influences performance of this enzyme.

journal_name

Appl Biochem Biotechnol

journal_title

Applied biochemistry and biotechnology

authors

Ban X,Li C,Zhang Y,Gu Z,Cheng L,Hong Y,Li Z

doi

10.1007/s12010-019-03150-7

subject

Has Abstract

pub_date

2020-03-01 00:00:00

pages

1010-1022

issue

3

eissn

0273-2289

issn

1559-0291

pii

10.1007/s12010-019-03150-7

journal_volume

190

pub_type

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