Identification of amino acids related to catalytic function of Sulfolobus solfataricus P1 carboxylesterase by site-directed mutagenesis and molecular modeling

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dc.contributor.authorY H Choi-
dc.contributor.authorY N Lee-
dc.contributor.authorYoung-Jun Park-
dc.contributor.authorSung Jin Yoon-
dc.contributor.authorH B Lee-
dc.date.accessioned2017-04-19T10:24:22Z-
dc.date.available2017-04-19T10:24:22Z-
dc.date.issued2016-
dc.identifier.issn1225-8687-
dc.identifier.uri10.5483/BMBRep.2016.49.6.077ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/13326-
dc.description.abstractThe archaeon Sulfolobus solfataricus P1 carboxylesterase is a thermostable enzyme with a molecular mass of 33.5 kDa belonging to the mammalian hormone-sensitive lipase (HSL) family. In our previous study, we purified the enzyme and suggested the expected amino acids related to its catalysis by chemical modification and a sequence homology search. For further validating these amino acids in this study, we modified them using site-directed mutagenesis and examined the activity of the mutant enzymes using spectrophotometric analysis and then estimated by homology modeling and fluorescence analysis. As a result, it was identified that Ser151, Asp244, and His274 consist of a catalytic triad, and Gly80, Gly81, and Ala152 compose an oxyanion hole of the enzyme. In addition, it was also determined that the cysteine residues are located near the active site or at the positions inducing any conformational changes of the enzyme by their replacement with serine residues.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleIdentification of amino acids related to catalytic function of Sulfolobus solfataricus P1 carboxylesterase by site-directed mutagenesis and molecular modeling-
dc.title.alternativeIdentification of amino acids related to catalytic function of Sulfolobus solfataricus P1 carboxylesterase by site-directed mutagenesis and molecular modeling-
dc.typeArticle-
dc.citation.titleBMB Reports-
dc.citation.number6-
dc.citation.endPage354-
dc.citation.startPage349-
dc.citation.volume49-
dc.contributor.affiliatedAuthorYoung-Jun Park-
dc.contributor.affiliatedAuthorSung Jin Yoon-
dc.contributor.alternativeName최윤호-
dc.contributor.alternativeName이예나-
dc.contributor.alternativeName박영준-
dc.contributor.alternativeName윤성진-
dc.contributor.alternativeName이희봉-
dc.identifier.bibliographicCitationBMB Reports, vol. 49, no. 6, pp. 349-354-
dc.identifier.doi10.5483/BMBRep.2016.49.6.077-
dc.subject.keywordCarboxylesterase-
dc.subject.keywordMolecular modeling-
dc.subject.keywordSite-directed mutagenesis-
dc.subject.keywordSulfolobus solfataricus P1-
dc.subject.keywordThermostability-
dc.subject.localCarboxylesterase-
dc.subject.localMolecular modeling-
dc.subject.localsite-directed mutagenesis-
dc.subject.localSite-directed mutagenesis-
dc.subject.localSulfolobus solfataricus P1-
dc.subject.localThermostability-
dc.subject.localthermostability-
dc.description.journalClassY-
Appears in Collections:
Division of Research on National Challenges > Environmental diseases research center > 1. Journal Articles
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