pubmed-article:12481100 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12481100 | lifeskim:mentions | umls-concept:C0242724 | lld:lifeskim |
pubmed-article:12481100 | lifeskim:mentions | umls-concept:C0039400 | lld:lifeskim |
pubmed-article:12481100 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:12481100 | lifeskim:mentions | umls-concept:C0009015 | lld:lifeskim |
pubmed-article:12481100 | lifeskim:mentions | umls-concept:C0678586 | lld:lifeskim |
pubmed-article:12481100 | lifeskim:mentions | umls-concept:C1554080 | lld:lifeskim |
pubmed-article:12481100 | lifeskim:mentions | umls-concept:C1706198 | lld:lifeskim |
pubmed-article:12481100 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
pubmed-article:12481100 | lifeskim:mentions | umls-concept:C1721326 | lld:lifeskim |
pubmed-article:12481100 | lifeskim:mentions | umls-concept:C1947987 | lld:lifeskim |
pubmed-article:12481100 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:12481100 | pubmed:dateCreated | 2002-12-13 | lld:pubmed |
pubmed-article:12481100 | pubmed:abstractText | 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. | lld:pubmed |
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pubmed-article:12481100 | pubmed:language | eng | lld:pubmed |
pubmed-article:12481100 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12481100 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12481100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12481100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12481100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12481100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12481100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12481100 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12481100 | pubmed:month | Dec | lld:pubmed |
pubmed-article:12481100 | pubmed:issn | 0032-0889 | lld:pubmed |
pubmed-article:12481100 | pubmed:author | pubmed-author:NakaoMasahiro... | lld:pubmed |
pubmed-article:12481100 | pubmed:author | pubmed-author:MaSeung-JinSJ | lld:pubmed |
pubmed-article:12481100 | pubmed:author | pubmed-author:SakataKanzoK | lld:pubmed |
pubmed-article:12481100 | pubmed:author | pubmed-author:Fukuchi-Mizut... | lld:pubmed |
pubmed-article:12481100 | pubmed:author | pubmed-author:MizutaniMasah... | lld:pubmed |
pubmed-article:12481100 | pubmed:author | pubmed-author:NakanishiHide... | lld:pubmed |
pubmed-article:12481100 | pubmed:author | pubmed-author:EmaJun-ichiJ | lld:pubmed |
pubmed-article:12481100 | pubmed:author | pubmed-author:NoguchiEtsuko... | lld:pubmed |
pubmed-article:12481100 | pubmed:author | pubmed-author:Inohara-Ochia... | lld:pubmed |
pubmed-article:12481100 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12481100 | pubmed:volume | 130 | lld:pubmed |
pubmed-article:12481100 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12481100 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12481100 | pubmed:pagination | 2164-76 | lld:pubmed |
pubmed-article:12481100 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
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