Please use this identifier to cite or link to this item: http://hdl.handle.net/10553/35477
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dc.contributor.authorSabatini, Alessiaen_US
dc.contributor.authorBrisdelli, Fabriziaen_US
dc.contributor.authorCelenza, Giuseppeen_US
dc.contributor.authorMarcoccia, Francescaen_US
dc.contributor.authorColapietro, Martinaen_US
dc.contributor.authorTavío Pérez, María del Maren_US
dc.contributor.authorPiccirilli, Alessandraen_US
dc.contributor.authorAmicosante, Gianfrancoen_US
dc.contributor.authorPerilli, Mariagraziaen_US
dc.date.accessioned2018-04-23T09:30:41Z-
dc.date.available2018-04-23T09:30:41Z-
dc.date.issued2017en_US
dc.identifier.issn2213-7165en_US
dc.identifier.urihttp://hdl.handle.net/10553/35477-
dc.description.abstractObjectives: The aim of this study was to evaluate the role of residue 238 in CTX-M-15 and CTX-M-15(G238C) mutant with respect to carbapenems and various beta-lactamase inhibitors. Methods: A CTX-M-15(G238C) laboratory mutant was generated by site-directed mutagenesis from CTX-M-15 enzyme by replacing glycine 238 with cysteine. Thiol titration and p-chloromercuribenzoate (PCMB) inactivation assays were used to ascertain the presence of a disulfide bridge in the active site of CTX-M15(G238C). Kinetic parameters were determined both for CTX-M-15 and CTX-M-15(G238C) enzymes by analysing either the complete hydrolysis time courses or under initial rate conditions. Results: In CTX-M-15(G238C) mutant, the two cysteines (C69 and C238) located in the enzyme active site were unable to form a disulfide bridge. CTX-M-15 and thermostable CTX-M-15(G238C) were used to study the kinetic interaction with carbapenems, which behaved as poor substrates for both enzymes. Meropenem and ertapenem acted as transient inactivators for CTX-M-15 and CTX-M-15(G238C), and for these compounds the variation of k(obs) versus the inactivator concentration was linear. Imipenem behaved as a transient inactivator for CTX-M-15 and as an inactivator (with k(+3) = 0) for CTX-M-15(G238C). In any case, the k(+2)/K values for CTX-M-15(G238C) were higher than those for CTX-M-15. Conclusions: Compared with CTX-M-15, CTX-M-15(G238C) mutant appears to have a more favourable conformation for carbapenem acylation and higher activity against cefotaxime, which could be due to the presence of free -SH groups in the enzyme active site.en_US
dc.languageengen_US
dc.relation.ispartofJournal of Global Antimicrobial Resistanceen_US
dc.sourceJournal of Global Antimicrobial Resistance [ISSN 2213-7165], v. 10, p. 95-100en_US
dc.subject320103 Microbiología clínicaen_US
dc.subject.otherCTX-M-15en_US
dc.subject.otherExtended-spectrum β-lactamaseen_US
dc.subject.otherESBLen_US
dc.subject.otherSite-directed mutagenesisen_US
dc.subject.otherCarbapenemsen_US
dc.titleInteraction of carbapenems and β-lactamase inhibitors towards CTX-M-15 and CTX-M-15G238C mutanten_US
dc.typeinfo:eu-repo/semantics/Articlees
dc.typeinfo:eu-repo/semantics/Articleen_US
dc.typeArticlees
dc.identifier.doi10.1016/j.jgar.2017.04.004
dc.identifier.scopus85025111312
dc.identifier.isi000410653300021-
dc.contributor.authorscopusid55924589200
dc.contributor.authorscopusid6602946643
dc.contributor.authorscopusid12808926200
dc.contributor.authorscopusid56512336600
dc.contributor.authorscopusid56798038900
dc.contributor.authorscopusid6701659492
dc.contributor.authorscopusid57189041486
dc.contributor.authorscopusid7006729208
dc.contributor.authorscopusid7004624865
dc.identifier.eissn2213-7173-
dc.description.lastpage100-
dc.description.firstpage95-
dc.relation.volume10-
dc.investigacionCiencias de la Saluden_US
dc.type2Artículoen_US
dc.contributor.daisngid3452978
dc.contributor.daisngid1376719
dc.contributor.daisngid1006533
dc.contributor.daisngid4635353
dc.contributor.daisngid2128801
dc.contributor.daisngid2590173
dc.contributor.daisngid28245018
dc.contributor.daisngid144499
dc.contributor.daisngid358961
dc.contributor.wosstandardWOS:Sabatini, A
dc.contributor.wosstandardWOS:Brisdelli, F
dc.contributor.wosstandardWOS:Celenza, G
dc.contributor.wosstandardWOS:Marcoccia, F
dc.contributor.wosstandardWOS:Colapietro, M
dc.contributor.wosstandardWOS:Tavio, MM
dc.contributor.wosstandardWOS:Piccirilli, A
dc.contributor.wosstandardWOS:Amicosante, G
dc.contributor.wosstandardWOS:Perilli, M
dc.date.coverdateSeptiembre 2017
dc.identifier.ulpgces
dc.description.sjr0,658
dc.description.jcr2,022
dc.description.sjrqQ2
dc.description.jcrqQ3
dc.description.scieSCIE
item.fulltextSin texto completo-
item.grantfulltextnone-
crisitem.author.deptGIR Investigación Básica y Aplicada en Ciencias de la Salud-
crisitem.author.deptDepartamento de Ciencias Clínicas-
crisitem.author.orcid0000-0002-1808-7461-
crisitem.author.parentorgDepartamento de Ciencias Clínicas-
crisitem.author.fullNameTavío Pérez, María Del Mar-
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