dc.contributor.author | Saral, Ayşegül | |
dc.contributor.author | Leonard, David A | |
dc.contributor.author | Özad Düzgün, Azer | |
dc.contributor.author | Çopur Çiçek, Ayşegül | |
dc.contributor.author | June, Cynthia M | |
dc.contributor.author | Sandallı, Cemal | |
dc.date.accessioned | 2019-12-18T11:02:14Z | |
dc.date.available | 2019-12-18T11:02:14Z | |
dc.date.issued | 2016-12 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12440/1775 | |
dc.identifier.uri | https://www.nature.com/articles/ja201648 | |
dc.description.abstract | The 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.iso | eng | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | [No Keywords] | en_US |
dc.title | Kinetic characterization of GES-22 ß-lactamase harboring the M169L clinical mutation | en_US |
dc.type | article | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.department | Fakülteler, Mühendislik ve Doğa Bilimleri Fakültesi, Genetik ve Biyomühendislik Bölümü | en_US |
dc.contributor.institutionauthor | Özad Düzgün, Azer | |