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dc.contributor.authorSaral, Ayşegül
dc.contributor.authorLeonard, David A
dc.contributor.authorÖzad Düzgün, Azer
dc.contributor.authorÇopur Çiçek, Ayşegül
dc.contributor.authorJune, Cynthia M
dc.contributor.authorSandallı, Cemal
dc.date.accessioned2019-12-18T11:02:14Z
dc.date.available2019-12-18T11:02:14Z
dc.date.issued2016-12
dc.identifier.urihttps://hdl.handle.net/20.500.12440/1775
dc.identifier.urihttps://www.nature.com/articles/ja201648
dc.description.abstractThe class A β-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 β-lactamases, we expressed, purified and kinetically characterized this novel variant. Our results show that compared with GES-116 × His, GES-226 × His 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 β-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.language.isoengen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subject[No Keywords]en_US
dc.titleKinetic characterization of GES-22 ß-lactamase harboring the M169L clinical mutationen_US
dc.typearticleen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.departmentFakülteler, Mühendislik ve Doğa Bilimleri Fakültesi, Genetik ve Biyomühendislik Bölümüen_US
dc.contributor.institutionauthorÖzad Düzgün, Azer


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