期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 76, 期 2, 页码 423-428出版社
OXFORD UNIV PRESS
DOI: 10.1271/bbb.110902
关键词
alpha-L-arabinofuranosidase; Thermotoga maritima; glycoside hydrolase family 51; arabinose; xylose
类别
资金
- Priority Program for Disaster-Affected Quantum Beam Facilities [2011G080, 2011A1908]
- New Energy and Industrial Technology Development Organization
- International Center of Research and Education for Molecular Complex Chemistry of Tohoku University Global CUE
- Grants-in-Aid for Scientific Research [22850010, 22550105, 23655094, 21750109] Funding Source: KAKEN
alpha-L-Arabinofuranosidase from the hyperthermophilic bacterium Thermotoga maritima (Tm-AFase) is an extremely thermophilic enzyme belonging to glycoside hydrolase family 51. It can catalyze the transglycosylation of a novel glycosyl donor, 4,6-dimethoxy-1,3,5-triazin-2-yl (DMT)-beta-D-xylopyranoside. In this study we determined the crystal structures of Tm-AFase in substrate-free and complex forms with arabinose and xylose at 1.8-2.3 angstrom resolution to determine the architecture of the substrate binding pocket. Subsite -1 of Tm-AFase is similar to that of alpha-L-arabinofuranosidase from Geobacillus stearothermophilus, but the substrate binding pocket of Tm-AFase is narrower and more hydrophobic. Possible substrate binding modes were investigated by automated docking analysis.
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