Roles of Ile66 and Ala107 of d-psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its substrate, d-fructose

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dc.contributor.authorH J Kim-
dc.contributor.authorB C Lim-
dc.contributor.authorSoo Jin Yeom-
dc.contributor.authorY S Kim-
dc.contributor.authorDoo Il Kim-
dc.contributor.authorD K Oh-
dc.date.accessioned2017-04-19T09:16:48Z-
dc.date.available2017-04-19T09:16:48Z-
dc.date.issued2010-
dc.identifier.issn0141-5492-
dc.identifier.uri10.1007/s10529-009-0115-1ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9315-
dc.description.abstractUsing site-directed mutagenesis, we investigated the roles of Ile66 and Ala107 of d-psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its true substrate, D-fructose. When Ile66 was substituted with alanine, glycine, cysteine, leucine, phenylalanine, tryptophan, tyrosine or valine, all the mutants dramatically increased the Km for d-tagatose but slightly decreased the Km for d-fructose, indicating that Ile66 is involved in substrate recognition. When Ala107 was substituted by either isoleucine or valine, the substituted mutants had lower thermostability than the wild-type enzyme whereas the proline-substituted mutant had higher thermostability. Thus, Ala107 is involved in enzyme stability.-
dc.publisherSpringer-
dc.titleRoles of Ile66 and Ala107 of d-psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its substrate, d-fructose-
dc.title.alternativeRoles of Ile66 and Ala107 of d-psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its substrate, d-fructose-
dc.typeArticle-
dc.citation.titleBiotechnology Letters-
dc.citation.number1-
dc.citation.endPage118-
dc.citation.startPage113-
dc.citation.volume32-
dc.contributor.affiliatedAuthorSoo Jin Yeom-
dc.contributor.affiliatedAuthorDoo Il Kim-
dc.contributor.alternativeName김혜정-
dc.contributor.alternativeName임병철-
dc.contributor.alternativeName염수진-
dc.contributor.alternativeName김영수-
dc.contributor.alternativeName김두일-
dc.contributor.alternativeName오덕근-
dc.identifier.bibliographicCitationBiotechnology Letters, vol. 32, no. 1, pp. 113-118-
dc.identifier.doi10.1007/s10529-009-0115-1-
dc.subject.keywordAgrobacterium tumefaciens-
dc.subject.keywordD-Psicose 3-epimerase-
dc.subject.keywordProtein stability-
dc.subject.keywordSite-directed mutagenesis-
dc.subject.keywordSubstrate specificity-
dc.subject.localagrobacterium tumefaciens-
dc.subject.localAgrobacterium tumefaciens-
dc.subject.locald-Psicose 3-epimerase-
dc.subject.localD-Psicose 3-epimerase-
dc.subject.localProtein stability-
dc.subject.localprotein stability-
dc.subject.localsite-directed mutagenesis-
dc.subject.localSite-directed mutagenesis-
dc.subject.localSubstrate specificity-
dc.subject.localsubstrate specificity-
dc.description.journalClassY-
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