Beta-primeverosidase
From Wikipedia, the free encyclopedia
In enzymology, a beta-primeverosidase (EC 3.2.1.149) is an enzyme that catalyzes the chemical reaction
- a 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside + H2O
6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranose + an alcohol
Thus, the two substrates of this enzyme are 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside and H2O, whereas its two products are 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranose and alcohol.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside 6-O-(beta-D-xylosyl)-beta-D-glucohydrolase.
[edit] References
- IUBMB entry for 3.2.1.149
- BRENDA references for 3.2.1.149 (Recommended.)
- PubMed references for 3.2.1.149
- PubMed Central references for 3.2.1.149
- Google Scholar references for 3.2.1.149
- Nagata T and Sakata K (1998). "Characterization of beta-primeverosidase, being concerned with alcoholic aroma formation in tea leaves to be processed into black tea, and preliminary observations on its substrate specificity". J. Agric. Food Chem. 46: 1712–1718.
- Tong Q and Sakata K (1997). "Purification of a beta-primeverosidase concerned with alcoholic aroma formation in tea leaves (cv. Shuxian) to be processed to oolong tea". J. Agric. Food Chem. 45: 877–882.

