GH10 family of glycoside hydrolases: Structure and evolutionary connections
- 作者: Naumoff D.G.1
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隶属关系:
- Winogradsky Institute of Microbiology
- 期: 卷 50, 编号 1 (2016)
- 页面: 132-140
- 栏目: Bioinformatics
- URL: https://journal-vniispk.ru/0026-8933/article/view/162479
- DOI: https://doi.org/10.1134/S0026893315060205
- ID: 162479
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详细
Evolutionary connections were analyzed for endo-β-xylanases, which possess the GH10 family catalytic domains. A homology search yielded thrice as many proteins as are available from the Carbohydrate-Active Enzymes (CAZy) database. Lateral gene transfer was shown to play an important role in evolution of bacterial proteins of the family, especially in the phyla Acidobacteria, Cyanobacteria, Planctomycetes, Spirochaetes, and Verrucomicrobia. In the case of Verrucomicrobia, 23 lateral transfers from organisms of other phyla were detected. Evolutionary relationships were observed between the GH10 family domains and domains with the TIM-barrel tertiary structure from several other glycosidase families. The GH39 family of glycoside hydrolases showed the closest relationship. Unclassified homologs were grouped into 12 novel families of putative glycoside hydrolases (GHL51–GHL62).
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作者简介
D. Naumoff
Winogradsky Institute of Microbiology
编辑信件的主要联系方式.
Email: daniil_naumoff@yahoo.com
俄罗斯联邦, Moscow, 117312
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