Alteration of a single amino acid changes the substrate specificity of dihydroflavonol 4-reductase

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dc.contributor.authorJohnson, Eric T.ko
dc.contributor.authorRyu, Sunhyoko
dc.contributor.authorYi, Hankuilko
dc.contributor.authorShin, Byongchulko
dc.contributor.authorCheong, Hyeonsookko
dc.contributor.authorChoi, Giltsuko
dc.date.accessioned2013-03-04T15:19:52Z-
dc.date.available2013-03-04T15:19:52Z-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.issued2001-02-
dc.identifier.citationPLANT JOURNAL, v.25, no.3, pp.325 - 333-
dc.identifier.issn0960-7412-
dc.identifier.urihttp://hdl.handle.net/10203/83050-
dc.description.abstractMany plant species exhibit a reduced range of flower colors due to the lack of an essential gene or to the substrate specificity of a biosynthetic enzyme. Petunia does not produce orange flowers because dihydroflavonol 4-reductase (DFR) from this species, an enzyme involved in anthocyanin biosynthesis, inefficiently reduces dihydrokaempferol, the precursor to orange pelargonidin-type anthocyanins. The substrate specificity of DFR, however, has not been investigated at the molecular level. By analyzing chimeric DFRs of Petunia and Gerbera, we identified a region that determines the substrate specificity of DFR. Furthermore, by changing a single amino acid in this presumed substrate-binding region, we developed a DFR enzyme that preferentially reduces dihydrokaempferol. Our results imply that the substrate specificity of DFR can be altered by minor changes in DFR.-
dc.languageEnglish-
dc.publisherBLACKWELL SCIENCE LTD-
dc.subjectUDP-GALACTOSE 4-EPIMERASE-
dc.subjectPETUNIA-HYBRIDA-
dc.subjectESCHERICHIA-COLI-
dc.subjectFLOWER COLOR-
dc.subjectANTHOCYANIN BIOSYNTHESIS-
dc.subjectFLAVONOID BIOSYNTHESIS-
dc.subjectALCOHOL-DEHYDROGENASE-
dc.subjectANGSTROM RESOLUTION-
dc.subjectCRYSTAL-STRUCTURES-
dc.subjectMOLECULAR-CLONING-
dc.titleAlteration of a single amino acid changes the substrate specificity of dihydroflavonol 4-reductase-
dc.typeArticle-
dc.identifier.wosid000167007600008-
dc.identifier.scopusid2-s2.0-0035115023-
dc.type.rimsART-
dc.citation.volume25-
dc.citation.issue3-
dc.citation.beginningpage325-
dc.citation.endingpage333-
dc.citation.publicationnamePLANT JOURNAL-
dc.identifier.doi10.1046/j.1365-313x.2001.00962.x-
dc.contributor.localauthorChoi, Giltsu-
dc.contributor.nonIdAuthorJohnson, Eric T.-
dc.contributor.nonIdAuthorRyu, Sunhyo-
dc.contributor.nonIdAuthorYi, Hankuil-
dc.contributor.nonIdAuthorShin, Byongchul-
dc.contributor.nonIdAuthorCheong, Hyeonsook-
dc.type.journalArticleArticle-
dc.subject.keywordAuthordihydroflavonol 4-reductase-
dc.subject.keywordAuthorpelargonidin-
dc.subject.keywordAuthoranthocyanin-
dc.subject.keywordAuthorsubstrate specificity-
dc.subject.keywordAuthorsite-directed mutagenesis-
dc.subject.keywordPlusUDP-GALACTOSE 4-EPIMERASE-
dc.subject.keywordPlusPETUNIA-HYBRIDA-
dc.subject.keywordPlusESCHERICHIA-COLI-
dc.subject.keywordPlusFLOWER COLOR-
dc.subject.keywordPlusANTHOCYANIN BIOSYNTHESIS-
dc.subject.keywordPlusFLAVONOID BIOSYNTHESIS-
dc.subject.keywordPlusALCOHOL-DEHYDROGENASE-
dc.subject.keywordPlusANGSTROM RESOLUTION-
dc.subject.keywordPlusCRYSTAL-STRUCTURES-
dc.subject.keywordPlusMOLECULAR-CLONING-
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