Functional characterization and molecular modeling of methylcatechol 2,3-dioxygenase from o-xylene-degrading Rhodococcus sp. strain DK17

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dc.contributor.authorDockyu Kim-
dc.contributor.authorJ C Chae-
dc.contributor.authorJ Y Jang-
dc.contributor.authorG J Zylstra-
dc.contributor.authorY M Kim-
dc.contributor.authorB S Kang-
dc.contributor.authorE Kim-
dc.date.accessioned2017-04-19T09:02:19Z-
dc.date.available2017-04-19T09:02:19Z-
dc.date.issued2005-
dc.identifier.issn0006291X-
dc.identifier.uri10.1016/j.bbrc.2004.11.123ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6825-
dc.description.abstractRhodococcus sp. strain DK17 is known to metabolize o-xylene and toluene through the intermediates 3,4-dimethylcatechol and 3- and 4-methylcatechol, respectively, which are further cleaved by a common catechol 2,3-dioxygenase. A putative gene encoding this enzyme (akbC) was amplified by PCR, cloned, and expressed in Escherichia coli. Assessment of the enzyme activity expressed in E. coli combined with sequence analysis of a mutant gene demonstrated that the akbC gene encodes the bona fide catechol 2,3-dioxygenase (AkbC) for metabolism of o-xylene and alkylbenzenes such as toluene and ethylbenzene. Analysis of the deduced amino acid sequence indicates that AkbC consists of a new catechol 2,3-dioxygenase class specific for methyl-substituted catechols. A computer-aided molecular modeling studies suggest that amino acid residues (particularly Phe177) in the β10-β11 loop play an essential role in characterizing the substrate specificity of AkbC.-
dc.publisherElsevier-
dc.titleFunctional characterization and molecular modeling of methylcatechol 2,3-dioxygenase from o-xylene-degrading Rhodococcus sp. strain DK17-
dc.title.alternativeFunctional characterization and molecular modeling of methylcatechol 2,3-dioxygenase from o-xylene-degrading Rhodococcus sp. strain DK17-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number4-
dc.citation.endPage886-
dc.citation.startPage880-
dc.citation.volume326-
dc.contributor.alternativeName김덕규-
dc.contributor.alternativeName채종찬-
dc.contributor.alternativeName장정연-
dc.contributor.alternativeNameZylstra-
dc.contributor.alternativeName김영민-
dc.contributor.alternativeName강범식-
dc.contributor.alternativeName김응빈-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 326, no. 4, pp. 880-886-
dc.identifier.doi10.1016/j.bbrc.2004.11.123-
dc.subject.keywordCatechol 2,3-dioxygenase-
dc.subject.keywordMolecular model-
dc.subject.keywordo-Xylene-
dc.subject.keywordRhodococcus-
dc.subject.localCatechol 2,3-dioxygenase-
dc.subject.localMolecular model-
dc.subject.localo-Xylene-
dc.subject.localRhodococcus-
dc.description.journalClassY-
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