Structural basis for the beta-lactamase activity of EstU1, a family VIII carboxylesterase SCIE SCOPUS
DC Field | Value | Language |
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dc.contributor.author | Cha, Sun-Shin | - |
dc.contributor.author | An, Young Jun | - |
dc.contributor.author | Jeong, Chang-Sook | - |
dc.contributor.author | Kim, Min-Kyu | - |
dc.contributor.author | Jeon, Jeong Ho | - |
dc.contributor.author | Lee, Chang-Muk | - |
dc.contributor.author | Lee, Hyun Sook | - |
dc.contributor.author | Kang, Sung Gyun | - |
dc.contributor.author | Lee, Jung-Hyun | - |
dc.date.accessioned | 2020-04-20T05:25:25Z | - |
dc.date.available | 2020-04-20T05:25:25Z | - |
dc.date.created | 2020-01-28 | - |
dc.date.issued | 2013-11 | - |
dc.identifier.issn | 0887-3585 | - |
dc.identifier.uri | https://sciwatch.kiost.ac.kr/handle/2020.kiost/3069 | - |
dc.description.abstract | EstU1 is a unique family VIII carboxylesterase that displays hydrolytic activity toward the amide bond of clinically used -lactam antibiotics as well as the ester bond of p-nitrophenyl esters. EstU1 assumes a -lactamase-like modular architecture and contains the residues Ser100, Lys103, and Tyr218, which correspond to the three catalytic residues (Ser64, Lys67, and Tyr150, respectively) of class C -lactamases. The structure of the EstU1/cephalothin complex demonstrates that the active site of EstU1 is not ideally tailored to perform an efficient deacylation reaction during the hydrolysis of -lactam antibiotics. This result explains the weak -lactamase activity of EstU1 compared with class C -lactamases. Finally, structural and sequential comparison of EstU1 with other family VIII carboxylesterases elucidates an operative molecular strategy used by family VIII carboxylesterases to extend their substrate spectrum. Proteins 2013; 81:2045-2051. (c) 2013 Wiley Periodicals, Inc. | - |
dc.description.uri | 1 | - |
dc.language | English | - |
dc.publisher | WILEY-BLACKWELL | - |
dc.subject | TRANSITION-STATE ANALOG | - |
dc.subject | BURKHOLDERIA-GLADIOLI | - |
dc.subject | LIPASES | - |
dc.subject | ENZYMES | - |
dc.subject | CLASSIFICATION | - |
dc.subject | CEPHALOSPORINS | - |
dc.subject | BIOTECHNOLOGY | - |
dc.subject | INHIBITION | - |
dc.subject | HYDROLASE | - |
dc.subject | SUBSTRATE | - |
dc.title | Structural basis for the beta-lactamase activity of EstU1, a family VIII carboxylesterase | - |
dc.type | Article | - |
dc.citation.endPage | 2051 | - |
dc.citation.startPage | 2045 | - |
dc.citation.title | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | - |
dc.citation.volume | 81 | - |
dc.citation.number | 11 | - |
dc.contributor.alternativeName | 차선신 | - |
dc.contributor.alternativeName | 안영준 | - |
dc.contributor.alternativeName | 정창숙 | - |
dc.contributor.alternativeName | 김민규 | - |
dc.contributor.alternativeName | 전정호 | - |
dc.contributor.alternativeName | 이현숙 | - |
dc.contributor.alternativeName | 강성균 | - |
dc.contributor.alternativeName | 이정현 | - |
dc.identifier.bibliographicCitation | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, v.81, no.11, pp.2045 - 2051 | - |
dc.identifier.doi | 10.1002/prot.24334 | - |
dc.identifier.scopusid | 2-s2.0-84885796337 | - |
dc.identifier.wosid | 000325980300017 | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | TRANSITION-STATE ANALOG | - |
dc.subject.keywordPlus | BURKHOLDERIA-GLADIOLI | - |
dc.subject.keywordPlus | LIPASES | - |
dc.subject.keywordPlus | ENZYMES | - |
dc.subject.keywordPlus | CLASSIFICATION | - |
dc.subject.keywordPlus | CEPHALOSPORINS | - |
dc.subject.keywordPlus | BIOTECHNOLOGY | - |
dc.subject.keywordPlus | INHIBITION | - |
dc.subject.keywordPlus | HYDROLASE | - |
dc.subject.keywordPlus | SUBSTRATE | - |
dc.subject.keywordAuthor | family VIII carboxylesterases | - |
dc.subject.keywordAuthor | EstU1 | - |
dc.subject.keywordAuthor | crystal structure of EstU1 | - |
dc.subject.keywordAuthor | crystal structure of the EstU1 | - |
dc.subject.keywordAuthor | cephalothin complex | - |
dc.subject.keywordAuthor | -lactamase activity | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |