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dc.citation.endPage 369 -
dc.citation.number 3 -
dc.citation.startPage 365 -
dc.citation.title BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS -
dc.citation.volume 444 -
dc.contributor.author Kim, Eun-Jung -
dc.contributor.author Son, Hyeoncheol Francis -
dc.contributor.author Kim, Sangwoo -
dc.contributor.author Ahn, Jae-Woo -
dc.contributor.author Kim, Kyung-Jin -
dc.date.accessioned 2023-12-22T03:07:13Z -
dc.date.available 2023-12-22T03:07:13Z -
dc.date.created 2014-02-17 -
dc.date.issued 2014-02 -
dc.description.abstract ReBktB is a β-keto thiolase from Ralstonia eutropha H16 that catalyzes condensation reactions between acetyl-CoA with acyl-CoA molecules that contains different numbers of carbon atoms, such as acetyl-CoA, propionyl-CoA, and butyryl-CoA, to produce valuable bioproducts, such as polyhydroxybutyrate, polyhydroxybutyrate-hydroxyvalerate, and hexanoate. We solved a crystal structure of ReBktB at 2.3 Å, and the overall structure has a similar fold to that of type II biosynthetic thiolases, such as PhbA from Zoogloea ramigera (ZrPhbA). The superposition of this structure with that of ZrPhbA complexed with CoA revealed the residues that comprise the catalytic and substrate binding sites of ReBktB. The catalytic site of ReBktB contains three conserved residues, Cys90, His350, and Cys380, which may function as a covalent nucleophile, a general base, and second nucleophile, respectively. For substrate binding, ReBktB stabilized the ADP moiety of CoA in a distinct way compared to ZrPhbA with His219, Arg221, and Asp228 residues, whereas the stabilization of β-mercaptoethyamine and pantothenic acid moieties of CoA was quite similar between these two enzymes. Kinetic study of ReBktB revealed that Km, Vmax, and Kcat values of 11.58 μM, 1.5 μmol/min, and 102.18 s-1, respectively, and the catalytic and substrate binding sites of ReBktB were further confirmed by site-directed mutagenesis experiments. -
dc.identifier.bibliographicCitation BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.444, no.3, pp.365 - 369 -
dc.identifier.doi 10.1016/j.bbrc.2014.01.055 -
dc.identifier.issn 0006-291X -
dc.identifier.scopusid 2-s2.0-84894075072 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/4085 -
dc.identifier.wosid 000332139200014 -
dc.language 영어 -
dc.publisher ACADEMIC PRESS INC ELSEVIER SCIENCE -
dc.title Crystal structure and biochemical characterization of beta-keto thiolase CrossMark B from polyhydroxyalkanoate-producing bacterium Ralstonia eutropha H16 -
dc.type Article -
dc.description.isOpenAccess FALSE -
dc.relation.journalWebOfScienceCategory Biochemistry & Molecular Biology; Biophysics -
dc.relation.journalResearchArea Biochemistry & Molecular Biology; Biophysics -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -

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