Rhea - reaction knowledgebase

Enzymes

Enzyme class ^help_outline	EC 3.2.1.149 beta-primeverosidase
GO Molecular Function ^help_outline	GO:0050535 beta-primeverosidase activity

Reaction participants Show >> << Hide

Name ^help_outline a 6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside Identifier CHEBI:2220 Charge 0 Formula C11H19O10R SMILES^help_outline O[C@@H]1CO[C@@H](OC[C@H]2O[C@@H](O[*])[C@H](O)[C@@H](O)[C@@H]2O)[C@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H₂O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) ^help_outline Charge 0 Formula H2O InChIKey^help_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILES^help_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline a 6-O-(β-D-xylopyranosyl)-β-D-glucopyranose Identifier CHEBI:16405 Charge 0 Formula C11H20O10 InChIKey^help_outline QYNRIDLOTGRNML-IGQSMMPPSA-N SMILES^help_outline O[C@@H]1CO[C@@H](OC[C@H]2O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]2O)[C@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline an alcohol Identifier CHEBI:30879 Charge 0 Formula HOR SMILES^help_outline O[*] 2D coordinates Mol file for the small molecule Search links Involved in 1,506 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:24480	RHEA:24481	RHEA:24482	RHEA:24483
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline
EC numbers ^help_outline	3.2.1.149
Gene Ontology ^help_outline	GO:0050535
KEGG ^help_outline				R05788
MetaCyc ^help_outline		3.2.1.149-RXN

Publications

Cloning of beta-primeverosidase from tea leaves, a key enzyme in tea aroma formation.

Mizutani M., Nakanishi H., Ema J., Ma S.J., Noguchi E., Inohara-Ochiai M., Fukuchi-Mizutani M., Nakao M., Sakata K.

A beta-primeverosidase from tea (Camellia sinensis) plants is a unique disaccharide-specific glycosidase, which hydrolyzes aroma precursors of beta-primeverosides (6-O-beta-D-xylopyranosyl-beta-D-glucopyranosides) to liberate various aroma compounds, and the enzyme is deeply concerned with the flo ... >> More

A beta-primeverosidase from tea (Camellia sinensis) plants is a unique disaccharide-specific glycosidase, which hydrolyzes aroma precursors of beta-primeverosides (6-O-beta-D-xylopyranosyl-beta-D-glucopyranosides) to liberate various aroma compounds, and the enzyme is deeply concerned with the floral aroma formation in oolong tea and black tea during the manufacturing process. The beta-primeverosidase was purified from fresh leaves of a cultivar for green tea (C. sinensis var sinensis cv Yabukita), and its partial amino acid sequences were determined. The beta-primeverosidase cDNA has been isolated from a cDNA library of cv Yabukita using degenerate oligonucleotide primers. The cDNA insert encodes a polypeptide consisting of an N-terminal signal peptide of 28 amino acid residues and a 479-amino acid mature protein. The beta-primeverosidase protein sequence was 50% to 60% identical to beta-glucosidases from various plants and was classified in a family 1 glycosyl hydrolase. The mature form of the beta-primeverosidase expressed in Escherichia coli was able to hydrolyze beta-primeverosides to liberate a primeverose unit and aglycons, but did not act on 2-phenylethyl beta-D-glucopyranoside. These results indicate that the beta-primeverosidase selectively recognizes the beta-primeverosides as substrates and specifically hydrolyzes the beta-glycosidic bond between the disaccharide and the aglycons. The stereochemistry for enzymatic hydrolysis of 2-phenylethyl beta-primeveroside by the beta-primeverosidase was followed by (1)H-nuclear magnetic resonance spectroscopy, revealing that the enzyme hydrolyzes the beta-primeveroside by a retaining mechanism. The roles of the beta-primeverosidase in the defense mechanism in tea plants and the floral aroma formation during tea manufacturing process are also discussed. << Less

Plant Physiol 130:2164-2176(2002) [PubMed] [EuropePMC]

Comments

Published in: Ogawa, K., Ijima, Y., Guo, W., Watanabe, N., Usui, T., Dong, S., Tong, Q. and Sakata, K. 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 (1997) 877–882. Ijima, Y., Ogawa, K., Watanabe, N., Usui, T., Ohnishi-Kameyama, M., Nagata, T. and Sakata, K. 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 (1998) 1712–1718.