Modulation of substrate preference of Thermus maltogenic amylase by mutation of the residues at the interface of a dimer

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dc.contributor.authorS H Park-
dc.contributor.authorH K Kang-
dc.contributor.authorJ H Shim-
dc.contributor.authorEui-jeon Woo-
dc.contributor.authorJ S Hong-
dc.contributor.authorJ W Kim-
dc.contributor.authorB H Oh-
dc.contributor.authorB H Lee-
dc.contributor.authorH Cha-
dc.contributor.authorK H Park-
dc.date.accessioned2017-04-19T09:07:41Z-
dc.date.available2017-04-19T09:07:41Z-
dc.date.issued2007-
dc.identifier.issn0916-8451-
dc.identifier.uri10.1271/bbb.70017ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/7982-
dc.description.abstractTo elucidate the relationship between the substrate size and geometric shape of the catalytic site of Thermus maltogenic amylase, Gly50, Asp109, and Val431, located at the interface of the dimer, were replaced with bulky amino acids. The kcat/Km value of the mutant for amylose increased significantly, whereas that for amylopectin decreased as compared to that of the wild-type enzyme. Thus, the substituted bulky amino acid residues modified the shape of the catalytic site, such that the ability of the enzyme to distinguish between small and large molecules like amylose and amylopectin was enhanced.-
dc.publisherT&F (Taylor & Francis)-
dc.titleModulation of substrate preference of Thermus maltogenic amylase by mutation of the residues at the interface of a dimer-
dc.title.alternativeModulation of substrate preference of Thermus maltogenic amylase by mutation of the residues at the interface of a dimer-
dc.typeArticle-
dc.citation.titleBioscience Biotechnology and Biochemistry-
dc.citation.number6-
dc.citation.endPage1567-
dc.citation.startPage1564-
dc.citation.volume71-
dc.contributor.affiliatedAuthorEui-jeon Woo-
dc.contributor.alternativeName박성훈-
dc.contributor.alternativeName강희권-
dc.contributor.alternativeName심재훈-
dc.contributor.alternativeName우의전-
dc.contributor.alternativeName홍정선-
dc.contributor.alternativeName김정완-
dc.contributor.alternativeName오병하-
dc.contributor.alternativeName이병훈-
dc.contributor.alternativeName차현주-
dc.contributor.alternativeName박관화-
dc.identifier.bibliographicCitationBioscience Biotechnology and Biochemistry, vol. 71, no. 6, pp. 1564-1567-
dc.identifier.doi10.1271/bbb.70017-
dc.subject.keywordAmylopectin-
dc.subject.keywordAmylose-
dc.subject.keywordCyclodextrin-degrading enzyme-
dc.subject.keywordMutagenesis-
dc.subject.keywordThermus sp. Maltogenic amylase (ThMA)-
dc.subject.localAmylopectin-
dc.subject.localAmylose-
dc.subject.localCyclodextrin-degrading enzyme-
dc.subject.localMutagenesis-
dc.subject.localmutagenesis-
dc.subject.localThermus sp. Maltogenic amylase (ThMA)-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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