A new esterase showing similarity to putative dienelactone hydrolase from a strict marine bacterium, Vibrio sp GMD509 SCIE SCOPUS
DC Field | Value | Language |
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dc.contributor.author | Park, Sang-Yi | - |
dc.contributor.author | Kim, Jun-Tae | - |
dc.contributor.author | Kang, Sung Gyun | - |
dc.contributor.author | Woo, Jung-Hee | - |
dc.contributor.author | Lee, Jung-Hyun | - |
dc.contributor.author | Choi, Hyoung-Tae | - |
dc.contributor.author | Kim, Sang-Jin | - |
dc.date.accessioned | 2020-04-20T11:40:17Z | - |
dc.date.available | 2020-04-20T11:40:17Z | - |
dc.date.created | 2020-01-28 | - |
dc.date.issued | 2007-11 | - |
dc.identifier.issn | 0175-7598 | - |
dc.identifier.uri | https://sciwatch.kiost.ac.kr/handle/2020.kiost/4624 | - |
dc.description.abstract | Vibrio sp. GMD509, a marine bacterium isolated from eggs of the sea hare, exhibited lipolytic activity on tributyrin (TBN) plate, and the gene representing lipolytic activity was cloned. As a result, an open reading frame (ORF) consisting of 1,017 bp (338 aa) was found, and the deduced amino acid sequence of the ORF showed low similarity (< 20%) to alpha/beta hydrolases such as dienelactone hydrolases and esterase/lipase with G-X-1-S-X-2-G sequence conserved. Phylogenetic analysis suggested that the protein belonged to a new family of esterase/lipase together with various hypothetical proteins. The enzyme was overexpressed in Escherichia coli and purified to homogeneity. The purified enzyme (Vlip509) showed the best hydrolyzing activity toward p-nitrophenyl butyrate (C-4) among various p-nitrophenyl esters (C-2 to C-18), and optimal activity of Vlip509 occurred at 30 degrees C and pH 8.5, respectively. Kinetic parameters toward p-nitrophenyl butyrate were determined as K (m) (307 mu M), k(cat) (5.72 s(-1)), and k(cat)/K-m (18.61 s(-1) mM(-1)). Furthermore, Vlip509 preferentially hydrolyzed the S-enantiomer of racemic ofloxacin ester. Despite its sequence homology to dienelactone hydrolase, Vlip509 showed no dienelactone hydrolase activity. This study represents the identification of a novel lipolytic enzyme from marine environment. | - |
dc.description.uri | 1 | - |
dc.language | English | - |
dc.publisher | SPRINGER | - |
dc.subject | THERMOSTABLE ESTERASE | - |
dc.subject | SEQUENCE SIMILARITY | - |
dc.subject | METAGENOMIC LIBRARY | - |
dc.subject | LIPASE | - |
dc.subject | BIOCATALYSIS | - |
dc.subject | PURIFICATION | - |
dc.subject | ENZYMES | - |
dc.subject | CLONING | - |
dc.subject | CLASSIFICATION | - |
dc.subject | ALIGNMENT | - |
dc.title | A new esterase showing similarity to putative dienelactone hydrolase from a strict marine bacterium, Vibrio sp GMD509 | - |
dc.type | Article | - |
dc.citation.endPage | 115 | - |
dc.citation.startPage | 107 | - |
dc.citation.title | APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | - |
dc.citation.volume | 77 | - |
dc.citation.number | 1 | - |
dc.contributor.alternativeName | 김준태 | - |
dc.contributor.alternativeName | 강성균 | - |
dc.contributor.alternativeName | 우정희 | - |
dc.contributor.alternativeName | 이정현 | - |
dc.contributor.alternativeName | 김상진 | - |
dc.identifier.bibliographicCitation | APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, v.77, no.1, pp.107 - 115 | - |
dc.identifier.doi | 10.1007/s00253-007-1134-2 | - |
dc.identifier.scopusid | 2-s2.0-35348843459 | - |
dc.identifier.wosid | 000250115200012 | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | THERMOSTABLE ESTERASE | - |
dc.subject.keywordPlus | SEQUENCE SIMILARITY | - |
dc.subject.keywordPlus | METAGENOMIC LIBRARY | - |
dc.subject.keywordPlus | LIPASE | - |
dc.subject.keywordPlus | BIOCATALYSIS | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | ENZYMES | - |
dc.subject.keywordPlus | CLONING | - |
dc.subject.keywordPlus | CLASSIFICATION | - |
dc.subject.keywordPlus | ALIGNMENT | - |
dc.subject.keywordAuthor | screening | - |
dc.subject.keywordAuthor | lipase/esterase | - |
dc.subject.keywordAuthor | dienelactone hydrolase | - |
dc.subject.keywordAuthor | Vibrio | - |
dc.subject.keywordAuthor | marine microorganism | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |