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Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae

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dc.contributor.authorDo, Hackwon-
dc.contributor.authorYoo Wanki-
dc.contributor.authorWang Ying-
dc.contributor.author남예원-
dc.contributor.authorShin, Seung Chul-
dc.contributor.authorKim, Han-Woo-
dc.contributor.authorKim Kyeong Kyu-
dc.contributor.authorLee, Jun Hyuck-
dc.date.accessioned2023-12-06T16:37:34Z-
dc.date.available2023-12-06T16:37:34Z-
dc.date.issued2023-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/14845-
dc.description.abstractEsterase, a member of the serine hydrolase family, catalyzes the cleavage and formation of ester bonds with high regio- and stereospecificity, making them attractive biocatalysts for the synthesis of optically pure molecules. In this study, we performed an in-depth biochemical and structural characterization of a novel microbial acetylesterase, LgEstI, from the bacterial fish pathogen Lactococcus garvieae. The dimeric LgEstI displayed substrate preference for the short acyl chain of p-nitrophenyl esters and exhibited increased activity with F207A mutation. Comparative analysis with other esterases indicated that LgEstI has a narrow and shallow active site that may exhibit substrate specificity to short acyl chains. Unlike other esterases, LgEstI contains bulky residues such as Trp89, Phe194, and Trp217, which block the acyl chain channel. Furthermore, immobilized LgEstI retained approximately 90% of its initial activity, indicating its potential in industrial applications. This study expands our understanding of LgEstI and proposes novel ideas for improving its catalytic efficiency and substrate specificity for various applications.-
dc.languageEnglish-
dc.subject.classificationKing Sejong Station-
dc.titleCrystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae-
dc.title.alternative해양어류 병원균 (Lactococcus garvieae) 유래 acetylesterase (LgEstI) 효소의 삼차구조 및 생화학적 특성 분석-
dc.typeArticle-
dc.identifier.bibliographicCitationDo, Hackwon, et al. 2023. "Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae". <em>PLOS ONE</em>, 18(2): 1-15.-
dc.citation.titlePLOS ONE-
dc.citation.volume18-
dc.citation.number2-
dc.identifier.doi10.1371/journal.pone.0280988-
dc.citation.startPage1-
dc.citation.endPage15-
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2021:39.189-
dc.subject.keywordCrystal structure-
dc.subject.keywordEsterase-
dc.subject.keywordLactococcus garvieae-
dc.subject.keywordprotein engineering-
dc.identifier.localId2023-0020-
Appears in Collections  
2023-2023, Development of potential antibiotic compounds using polar organism resources (23-23) / Lee, Jun Hyuck (PM23030)
2023-2023, Development of microbial enzymes degrading recalcitrant materials from the Arctic Circle (23-23) / Kim, Han-Woo (PN23014)
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