Cloning and characterization of a fish microsomal epoxide hydrolase of Danio rerio and application to kinetic resolution of racemic styrene oxide SCIE SCOPUS

DC Field Value Language
dc.contributor.author Kim, HS -
dc.contributor.author Lee, SJ -
dc.contributor.author Lee, EJ -
dc.contributor.author Hwang, JW -
dc.contributor.author Park, S -
dc.contributor.author Kim, SJ -
dc.contributor.author Lee, EY -
dc.date.accessioned 2020-04-20T13:55:09Z -
dc.date.available 2020-04-20T13:55:09Z -
dc.date.created 2020-01-28 -
dc.date.issued 2005-12-01 -
dc.identifier.issn 1381-1177 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/4989 -
dc.description.abstract Gene mining of the genome database of the zebra fish Danio rerio revealed the presence of a putative microsomal epoxide hydrolase (mEH)-like protein containing the characteristic catalytic triad composed of ASp(223), Glu(402), and His(429) as well as the oxyanion hole common to all mEH. Based on the sequence information, a new EH gene was cloned by PCR amplification of cDNA of the zebra fish Danio rerio and expressed heterologously in Escherichia coli. The recombinant E. coli exhibited the enantiopreference toward (R)-styrene oxide with the maximum hydrolytic activity of 11.4 mu mol min(-1) (mg dcw)(-1). When the kinetic resolution was conducted with 40 mM of racemic styrene oxide, enantiopure (S)-styrene oxide was obtained with an enantiomeric excess (ee) higher than 99 and 23.5% yield at 30 min. These results demonstrate that the recombinant fish EH has the possible application as a biocatalyst for the production of enantiopure epoxides. (c) 2005 Elsevier B.V. All rights reserved. -
dc.description.uri 1 -
dc.language English -
dc.publisher ELSEVIER SCIENCE BV -
dc.subject RHODOTORULA-GLUTINIS -
dc.subject ENANTIOSELECTIVE HYDROLYSIS -
dc.subject ASPERGILLUS-NIGER -
dc.subject PURIFICATION -
dc.subject HALOHYDRINS -
dc.subject EXPRESSION -
dc.subject YEASTS -
dc.subject ENZYME -
dc.title Cloning and characterization of a fish microsomal epoxide hydrolase of Danio rerio and application to kinetic resolution of racemic styrene oxide -
dc.type Article -
dc.citation.endPage 35 -
dc.citation.startPage 30 -
dc.citation.title JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC -
dc.citation.volume 37 -
dc.citation.number 1-6 -
dc.contributor.alternativeName 김상진 -
dc.identifier.bibliographicCitation JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, v.37, no.1-6, pp.30 - 35 -
dc.identifier.doi 10.1016/j.molcatb.2005.09.003 -
dc.identifier.scopusid 2-s2.0-27944452636 -
dc.identifier.wosid 000234026100005 -
dc.type.docType Article -
dc.description.journalClass 1 -
dc.subject.keywordPlus RHODOTORULA-GLUTINIS -
dc.subject.keywordPlus ENANTIOSELECTIVE HYDROLYSIS -
dc.subject.keywordPlus ASPERGILLUS-NIGER -
dc.subject.keywordPlus PURIFICATION -
dc.subject.keywordPlus HALOHYDRINS -
dc.subject.keywordPlus EXPRESSION -
dc.subject.keywordPlus YEASTS -
dc.subject.keywordPlus ENZYME -
dc.subject.keywordAuthor enantiopure styrene oxide -
dc.subject.keywordAuthor Danio rerio -
dc.subject.keywordAuthor epoxide hydrolase -
dc.subject.keywordAuthor gene mining -
dc.subject.keywordAuthor kinetic resolution -
dc.relation.journalWebOfScienceCategory Biochemistry & Molecular Biology -
dc.relation.journalWebOfScienceCategory Chemistry, Physical -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.relation.journalResearchArea Biochemistry & Molecular Biology -
dc.relation.journalResearchArea Chemistry -
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