Article
Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose.
The Journal of biological chemistry - 24 Nov 2017
Chu Yindi, Tu Tao, Penttinen Leena, Xue Xianli, Wang Xiaoyu, Yi Zhuolin, Gong Li, Rouvinen Juha, Luo Huiying, Hakulinen Nina, Yao Bin, Su Xiaoyun
Abstract excerpt
Bifunctional glycoside hydrolases have potential for cost-savings in enzymatic decomposition of plant cell wall polysaccharides for biofuels and bio-based chemicals. The N-terminal GH10 domain of a bifunctional multimodular enzyme CbXyn10C/Cel48B from Caldicellulosiruptor bescii is an enzyme able to degrade xylan and cellulose simultaneously. However, the molecular mechanism underlying its substrate promiscuity...
Topics
- Amino Acid Sequence
- Biocatalysis
- Catalytic Domain
- Cellulose
- Crystallography, X-Ray
- Endo-1,4-beta Xylanases
- Firmicutes
- Hydrolysis
- Models, Molecular
- Mutagenesis, Site-Directed