Basit öğe kaydını göster

dc.contributor.authorSaral, Ayşegül
dc.contributor.authorLeonard, David A.
dc.contributor.authorDüzgün, Azer Özad
dc.contributor.authorÇopur Çiçek, Aysegül
dc.contributor.authorJune, Cynthia M.
dc.contributor.authorSandallı, Cemal
dc.date.accessioned2020-04-21T09:07:03Z
dc.date.available2020-04-21T09:07:03Z
dc.date.issued2016en_US
dc.identifier.citationSaral, A., Sandalli, C., Leonard, D. A., June, C. M., Duzgun, A. O., & Cicek, A. C.. (2016). Kinetic characterization of GES-22 β-lactamase harboring the M169L clinical mutation. Journal of Antibiotics, 69(12), 858–862. https://doi.org/10.1038/ja.2016.48en_US
dc.identifier.urihttps://hdl.handle.net/11494/2041
dc.description.abstractThe class A p-lactamase GES-22 has been identified in Acinetobacter baumannii isolates in Turkey, and subsequently shown to differ from GES-11 by a single substitution (M169L). Because M169 is part of the omega loop, a structure that is known to have major effects on substrate selectivity in class A beta-lactamases, we expressed, purified and kinetically characterized this novel variant. Our results show that compared with GES-11(6xHis), GES-22(6xHis) displays more efficient hydrolysis of penicillins, and aztreonam, but a loss of efficiency against ceftazidime. In addition, the M169L substitution confers on GES-22 more efficient hydrolysis of the mechanistic inhibitors clavulanic acid and sulbactam. These effects are highly similar to other mutations at the homologous position in other class A beta-lactamases, suggesting that this methionine has a key structural role in aligning active site residues and in substrate selectivity across the class.en_US
dc.description.sponsorshipRecep Tayyip Erdogan University:BAP-2013.102.03.12 Turkiye Bilimsel ve Teknolojik Arastirma Kurumu (TUBITAK): TUBITAK-113Z054 United States Department of Health & Human Services National Institutes of Health (NIH) - USA 1R15AI082416 Turkiye Bilimsel ve Teknolojik Arastirma Kurumu (TUBITAK) 2214-A
dc.language.isoengen_US
dc.publisherJapan Antibiotics Research Assocen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subject[No Keywords Available]en_US
dc.titleKinetic characterization of GES-22 beta-lactamase harboring the M169L clinical mutationen_US
dc.typearticleen_US
dc.relation.journalJournal Of Antibioticsen_US
dc.departmentAÇÜ, Sağlık Bilimleri Fakültesien_US
dc.identifier.volume69en_US
dc.identifier.issue12en_US
dc.identifier.startpage858en_US
dc.identifier.endpage862en_US
dc.relation.publicationcategoryMakale - Ulusal Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.1038/ja.2016.48en_US
dc.contributor.institutionauthorSaral, Ayşegülen_US


Bu öğenin dosyaları:

Thumbnail

Bu öğe aşağıdaki koleksiyon(lar)da görünmektedir.

Basit öğe kaydını göster