Structural features of cephalosporin acylase reveal the basis of autocatalytic activation
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, Ki Joon | - |
dc.contributor.author | Kim, Jin Kwang | - |
dc.contributor.author | Lee, Ji-Hye | - |
dc.contributor.author | Shin, Hye Jeong | - |
dc.contributor.author | Park, Sung Soo | - |
dc.contributor.author | Kim, Kyung Hyun | - |
dc.date.accessioned | 2021-09-08T10:40:57Z | - |
dc.date.available | 2021-09-08T10:40:57Z | - |
dc.date.created | 2021-06-11 | - |
dc.date.issued | 2009-12-11 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/118750 | - |
dc.description.abstract | Cephalosporin acylase (CA), a member of the N-terminal nucleophile hydrolase family, is activated through two steps of intramolecular autoproteolysis, the first mediated by a serine residue, and the second by a glutamate, which releases the pro-segment and produces an active enzyme. In this study, we have determined the crystal structures of mutants which could affect primary or secondary auto-cleavage and of sequential intermediates of a slow-processing mutant at 2.0-2.5 angstrom resolutions. The pro-segments of the mutants undergo dynamic conformational changes during activation and adopt surprisingly different loop conformations from one another. However, the autoproteolytic site was found to form a catalytically competent conformation with a solvent water molecule, which was essentially conserved in the CA mutants. (C) 2009 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | 7-AMINOCEPHALOSPORANIC ACID ACYLASE | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | AUTOPROTEOLYTIC ACTIVATION | - |
dc.subject | PENICILLIN ACYLASE | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | HYDROLASE FAMILY | - |
dc.subject | PROTEIN | - |
dc.subject | PROTEASOME | - |
dc.subject | RESOLUTION | - |
dc.subject | INSIGHTS | - |
dc.title | Structural features of cephalosporin acylase reveal the basis of autocatalytic activation | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Kyung Hyun | - |
dc.identifier.doi | 10.1016/j.bbrc.2009.09.134 | - |
dc.identifier.scopusid | 2-s2.0-70350128754 | - |
dc.identifier.wosid | 000271552400031 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.390, no.2, pp.342 - 348 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 390 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 342 | - |
dc.citation.endPage | 348 | - |
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 | 7-AMINOCEPHALOSPORANIC ACID ACYLASE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | AUTOPROTEOLYTIC ACTIVATION | - |
dc.subject.keywordPlus | PENICILLIN ACYLASE | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | HYDROLASE FAMILY | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | PROTEASOME | - |
dc.subject.keywordPlus | RESOLUTION | - |
dc.subject.keywordPlus | INSIGHTS | - |
dc.subject.keywordAuthor | Autoproteolysis | - |
dc.subject.keywordAuthor | Precursor activation | - |
dc.subject.keywordAuthor | Cephalosporin acylase | - |
dc.subject.keywordAuthor | Slow-processing mutant | - |
dc.subject.keywordAuthor | Intermediate structure | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
(02841) 서울특별시 성북구 안암로 14502-3290-1114
COPYRIGHT © 2021 Korea 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.