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Substrate-Binding Mechanism of a TypeⅠ Extradiol Dioxygenase

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dc.contributor.authorKim, Kyungsun-
dc.contributor.authorKyung Jin Kim-
dc.contributor.authorHa Yeon Cho-
dc.contributor.authorKim, Dockyu-
dc.contributor.authorKim, Eungbin-
dc.contributor.authorKang, Beom Sik-
dc.contributor.authorSeo Yean Sohn-
dc.contributor.authorHyo Je Cho-
dc.date.issued2010-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/8537-
dc.description.abstractA meta-cleavage pathway for the aerobic degradation of aromatic hydrocarbons is catalyzed by extradiol dioxygenases via a two-step mechanism: catechol substrate binding and dioxygen incorporation. The binding of substrate triggers the release of water, thereby opening a coordination site for molecular oxygen. The crystal structures of Selenomethionine-substituted AkbC, a type I extradiol dioxygenase, and the enzyme-substrate (3-methylcatechol) complex revealed the substrate-binding process of extradiol dioxygenase. AkbC was found to be composed of eight identical subunits, each containing one ferrous ion. AkbC is composed of an N-domain (residues M1-G138) and an active C-domain (K139-G284), which contains iron coordinated by a 2-His-1-carboxylate facial triad motif (H149, H212, and E263). The C-domain includes a β-hairpin structure (β11-β12) and a C-terminal tail (H285-G300). In substrate-bound AkbC, 3-methylcatechol interacts with the iron via a single hydroxyl group, which represents an intermediate stage in the substrate-binding process. Structure-based mutagenesis combined with structural analyses reveals that the C-terminal tail and β-hairpin form part of the substrate-binding pocket that is responsible for substrate specificity by blocking substrate entry. Once a substrate enters the active site, these structural elements also play a role in the correct positioning of the substrate. Based on the results presented here, a putative substrate-binding mechanism is proposed.-
dc.languageEnglish-
dc.titleSubstrate-Binding Mechanism of a TypeⅠ Extradiol Dioxygenase-
dc.title.alternativeTypeⅠ Extradiol Dioxygenase의 기질결합 기작-
dc.typeProceeding-
dc.identifier.bibliographicCitationKim, Kyungsun, et al. 2010. Substrate-Binding Mechanism of a TypeⅠ Extradiol Dioxygenase. 한국미생물학회연합. 한국미생물학회연합. 2010.10.14~.-
dc.citation.volume1-
dc.citation.number1-
dc.citation.conferenceDate2010.10.14~-
dc.citation.conferenceName한국미생물학회연합-
dc.citation.conferencePlace한국미생물학회연합-
dc.description.articleClassificationPro(초록)국내-
dc.subject.keywordExtradiol dioxygenase-
dc.subject.keywordRhodococcus-
dc.subject.keywordSubstrate-binding-
dc.identifier.localId2010-0208-
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2006-2010, Procurement and utilization of polar genetic resources (06-10) / Lee, Hong Kum; Yim, Joung Han (PE06050, PE07050, PE08050, PE09050, PE10050)
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