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Bioscience, Biotechnology, and Biochemistry
Vol. 76 (2012) No. 2 P 423-428



Biochemistry & Molecular Biology Communications

α-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)-β-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 Å resolution to determine the architecture of the substrate binding pocket. Subsite −1 of Tm-AFase is similar to that of α-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.

Copyright © 2012 by Japan Society for Bioscience, Biotechnology, and Agrochemistry

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