The crystal structure of rice (Oryza sativa L.) Os4BGlu12, an oligosaccharide and tuberonic acid glucoside-hydrolyzing Î²-glucosidase with significant thioglucohydrolase activity

Article ID	Journal	Published Year	Pages	File Type
1925747	Archives of Biochemistry and Biophysics	2011	11 Pages	PDF

Abstract

âº Os4BGlu12 has an extra disulfide bond compared to other plant family GH 1 enzymes. âº Os4BGlu12 stability is not correlated to the disulfide bond. âº Os4BGlu12 Î²-glucosidase intermediate with 2-F-glucoside is similar to myrosinase. âº The Os4BGlu12 thioglucosidase activity is higher than Os3BGlu6 and Os3BGlu7. âº Thioglucosidase activity and structural similarity support phylogenetic analysis.

Keywords

Rice X-ray crystallography Substrate specificity Michaelis complex Covalent intermediate glycoside hydrolase

Related Topics

Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry

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The crystal structure of rice (Oryza sativa L.) Os4BGlu12, an oligosaccharide and tuberonic acid glucoside-hydrolyzing Î²-glucosidase with significant thioglucohydrolase activity

Authors

Sompong Sansenya, Rodjana Opassiri, Buabarn Kuaprasert, Chun-Jung Chen, James R. Ketudat Cairns,