Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Do, Hackwon | - |
dc.contributor.author | Yoo, Wanki | - |
dc.contributor.author | Wang, Ying | - |
dc.contributor.author | Nam, Yewon | - |
dc.contributor.author | Shin, Seung Chul | - |
dc.contributor.author | Kim, Han-Woo | - |
dc.contributor.author | Kim, Kyeong Kyu | - |
dc.contributor.author | Lee, Jun Hyuck | - |
dc.date.accessioned | 2023-11-08T06:50:28Z | - |
dc.date.available | 2023-11-08T06:50:28Z | - |
dc.date.issued | 2023-02 | - |
dc.identifier.issn | 1932-6203 | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/152030 | - |
dc.description.abstract | Esterase, 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. © 2023 Do et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | Public Library of Science | - |
dc.title | Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae | - |
dc.type | Article | - |
dc.publisher.location | 미국 | - |
dc.identifier.doi | 10.1371/journal.pone.0280988 | - |
dc.identifier.scopusid | 2-s2.0-85147536405 | - |
dc.identifier.wosid | 000960745300001 | - |
dc.identifier.bibliographicCitation | PLoS ONE, v.18, no.2 | - |
dc.citation.title | PLoS ONE | - |
dc.citation.volume | 18 | - |
dc.citation.number | 2 | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | Y | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.subject.keywordPlus | ESTERASE | - |
dc.subject.keywordPlus | DATABASE | - |
dc.subject.keywordPlus | RESOLUTION | - |
dc.subject.keywordPlus | IMMOBILIZATION | - |
dc.subject.keywordPlus | CLASSIFICATION | - |
dc.subject.keywordPlus | SPECIFICITY | - |
dc.subject.keywordPlus | SECONDARY | - |
dc.subject.keywordPlus | ENZYMES | - |
dc.subject.keywordPlus | TOOLS | - |
dc.identifier.url | https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0280988 | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
Sookmyung Women's University. Cheongpa-ro 47-gil 100 (Cheongpa-dong 2ga), Yongsan-gu, Seoul, 04310, Korea02-710-9127
Copyright©Sookmyung Women's University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.