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Beta-primeverosidase

From Wikipedia, the free encyclopedia
beta-primeverosidase
Identifiers
EC no.3.2.1.149
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

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.

References

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  • Nagata T, 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 (5): 1712–1718. doi:10.1021/jf970576g.
  • Tong Q, 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 (3): 877–882. doi:10.1021/jf960543l.