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- Title
Importance of C-Terminal Extension in Thermophilic 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02.
- Authors
Ban, Xiaofeng; Li, Caiming; Zhang, Yuzhu; Gu, Zhengbiao; Cheng, Li; Hong, Yan; Li, Zhaofeng
- 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.
- Subjects
C-terminal residues; N-terminal residues; ENZYMES; CATALYTIC domains; CHEMICAL stability; METAL ions
- Publication
Applied Biochemistry & Biotechnology, 2020, Vol 190, Issue 3, p1010
- ISSN
0273-2289
- Publication type
Article
- DOI
10.1007/s12010-019-03150-7