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Structural and Kinetic Insights into the "Ceftazidimase" Behavior of the Extended-Spectrum β-Lactamase CTX-M-96.

Biochemistry - 18 Aug 2015

Ghiglione Barbara, Rodríguez María Margarita, Herman Raphaël, Curto Lucrecia, Dropa Milena, Bouillenne Fabrice, Kerff Frédéric, Galleni Moreno, Charlier Paulette, Gutkind Gabriel, Sauvage Eric, Power Pablo

Abstract excerpt

Diversification of the CTX-M β-lactamases led to the emergence of variants responsible for decreased susceptibility to ceftazidime, like the Asp240Gly-harboring "ceftazidimases". We solved the crystallographic structure of the Asp240Gly variant CTX-M-96 at 1.2 Å and evaluated the role of Asp240 in the activity toward oxyimino-cephalosporins through simulated models and kinetics. There seem to be subtle changes in...

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Identifiers

PMID: 26228623
DOI: 10.1021/acs.biochem.5b00313

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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