The crystal structure of an HSL-homolog EstE5 complex with PMSF reveals a unique configuration that inhibits the nucleophile Ser144 in catalytic triads
DC Field | Value | Language |
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dc.contributor.author | Nam, Ki Hyun | - |
dc.contributor.author | Kim, Soo-Jin | - |
dc.contributor.author | Priyadarshi, Amit | - |
dc.contributor.author | Kim, Hyun Sook | - |
dc.contributor.author | Hwang, Kwang Yeon | - |
dc.date.accessioned | 2021-09-08T11:33:35Z | - |
dc.date.available | 2021-09-08T11:33:35Z | - |
dc.date.created | 2021-06-11 | - |
dc.date.issued | 2009-11-13 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/118926 | - |
dc.description.abstract | The esterase/lipase family (EC 3.1.1.3/EC 3.1.1.1) represents a diverse group of hydrolases that catalyze the cleavage of ester bonds and are widely distributed in animals, plants and microorganisms. Among these enzymes, hormone-sensitive lipases, play a critical role in the regulation of rodent fat cell lipolysis and are regarded as adipose tissue-specific enzymes. Recently, we reported the structural and biological characterization of EstE5 from the metagenome library [K.H. Nam, M.Y. Kim, SJ. Kim, A. Priyadarshi, W.H. Lee, K.Y. Hwang, Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase, Biochem. Biophys. Res. Commun. 379 (2009) 553-556]. The structure of this protein revealed that it belongs to the HSL-family. Here, we report the inhibition of the activity of the HSL-homolog EstE5 protein as determined by the use of esterase/lipase inhibitors. Our results revealed that the EstE5 protein is significantly inhibited by PMSF. In addition, this is the first study to identify the crystal structures of EstE5-PMSF at 2.4 and 2.5 angstrom among the HSL-homolog structures. This structural configuration is similar to that adopted when serine proteases are inhibited by PMSF. The results presented here provide valuable information regarding the properties of the HSL-family. (C) 2009 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | HORMONE-SENSITIVE LIPASE | - |
dc.subject | FUNCTIONAL-ANALYSIS | - |
dc.subject | ESTERASE | - |
dc.subject | CARBOXYLESTERASE | - |
dc.subject | PROTEINS | - |
dc.title | The crystal structure of an HSL-homolog EstE5 complex with PMSF reveals a unique configuration that inhibits the nucleophile Ser144 in catalytic triads | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Hwang, Kwang Yeon | - |
dc.identifier.doi | 10.1016/j.bbrc.2009.08.123 | - |
dc.identifier.scopusid | 2-s2.0-70349322388 | - |
dc.identifier.wosid | 000270764400008 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.389, no.2, pp.247 - 250 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 389 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 247 | - |
dc.citation.endPage | 250 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | HORMONE-SENSITIVE LIPASE | - |
dc.subject.keywordPlus | FUNCTIONAL-ANALYSIS | - |
dc.subject.keywordPlus | ESTERASE | - |
dc.subject.keywordPlus | CARBOXYLESTERASE | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordAuthor | EstE5 | - |
dc.subject.keywordAuthor | Esterase/lipase | - |
dc.subject.keywordAuthor | EstE5-PMSF | - |
dc.subject.keywordAuthor | Charge-relay system | - |
dc.subject.keywordAuthor | Active site inhibition | - |
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