Full metadata record

DC Field Value Language
dc.contributor.authorPriyadarshi, Amit-
dc.contributor.authorLee, Eun Hye-
dc.contributor.authorSung, Min Woo-
dc.contributor.authorNam, Ki Hyun-
dc.contributor.authorLee, Won Ho-
dc.contributor.authorKim, Eunice EunKyeong-
dc.contributor.authorHwang, Kwang Yeon-
dc.date.accessioned2024-01-20T21:04:18Z-
dc.date.available2024-01-20T21:04:18Z-
dc.date.created2021-09-03-
dc.date.issued2009-07-
dc.identifier.issn1570-9639-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/132345-
dc.description.abstractAlanine racemase (AlaR) is a bacterial enzyme that belongs to the fold-type III group of pyridoxal 5'-phosphate (PLP)-dependent enzymes. AlaR. catalyzes the interconversion between L- and D-alanine, which is important for peptidoglycan biosynthesis. This enzyme is common in prokaryotes, but absent in eukaryotes, which makes it an attractive target for the design of new antibacterial drugs. Here, we report the crystal structures of both the apoenzyme and the D-cycloserine (DCS) complex of AlaR from the pathogenic bacterium Enterococcus faecalis v583, at a resolution of 2.5 angstrom. DCS is a suicide inhibitor of AlaR and, as such, serves as an antimicrobial agent and has been used to treat tuberculosis and urinary tract infection-related diseases, and makes several hydrogen bonds with the conserved active site residues, Tyr44 and Ser207, respectively. The apoenzyme crystal structure of AlaR consists of three monomers in the asymmetric unit, including a polyethylene glycol molecule in the dimer interface that surrounds one of the His 293 residues and also sits close to one side of the His 293 residue in the opposite monomer. Our results provide structural insights into AlaR that may be used for the development of new antibiotics targeting the alanine racemase in pathogenic bacteria. (C) 2009 Elsevier B.V. All rights reserved.-
dc.languageEnglish-
dc.publisherELSEVIER-
dc.subjectBACILLUS-STEAROTHERMOPHILUS-
dc.subjectCRYSTAL-STRUCTURE-
dc.subjectSIDE-REACTION-
dc.subjectTRANSAMINATION-
dc.subjectEVOLUTION-
dc.subjectMODEL-
dc.subjectMECHANISM-
dc.subjectCONTAINS-
dc.subjectENZYMES-
dc.subjectBINDS-
dc.titleStructural insights into the alanine racemase from Enterococcus faecalis-
dc.typeArticle-
dc.identifier.doi10.1016/j.bbapap.2009.03.006-
dc.description.journalClass1-
dc.identifier.bibliographicCitationBIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v.1794, no.7, pp.1030 - 1040-
dc.citation.titleBIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS-
dc.citation.volume1794-
dc.citation.number7-
dc.citation.startPage1030-
dc.citation.endPage1040-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000266744700006-
dc.identifier.scopusid2-s2.0-67349206089-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-
dc.type.docTypeArticle-
dc.subject.keywordPlusBACILLUS-STEAROTHERMOPHILUS-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusSIDE-REACTION-
dc.subject.keywordPlusTRANSAMINATION-
dc.subject.keywordPlusEVOLUTION-
dc.subject.keywordPlusMODEL-
dc.subject.keywordPlusMECHANISM-
dc.subject.keywordPlusCONTAINS-
dc.subject.keywordPlusENZYMES-
dc.subject.keywordPlusBINDS-
dc.subject.keywordAuthorAlanine racemase-
dc.subject.keywordAuthorD-cycloserine-
dc.subject.keywordAuthorPEG-
dc.subject.keywordAuthorPLP-
dc.subject.keywordAuthorEnterococcus faecalis-
Appears in Collections:
KIST Article > 2009
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE