The Guiana extended-spectrum (GES) b-lactamase GESG170H, GESG170L, and GESG170K mutants showed kcat, Km, and kcat/Km values very dissimilar to those of GES-1 and GES-5. The enhancement of the hydrolytic activity against carbapenems is potentially due to a shift of the substrate in the active site that provides better positioning of the deacylating water molecule caused by the presence of the imidazole ring of H170 and of the long side chain of K170 and L170.

Laboratory variants GESG170L, GESG170K, and GESG170H increase carbapenem hydrolysis and confer resistance to clavulanic acid

Piccirilli A.;Segatore B.;Brisdelli F.;Amicosante G.;Perilli M.
2021

Abstract

The Guiana extended-spectrum (GES) b-lactamase GESG170H, GESG170L, and GESG170K mutants showed kcat, Km, and kcat/Km values very dissimilar to those of GES-1 and GES-5. The enhancement of the hydrolytic activity against carbapenems is potentially due to a shift of the substrate in the active site that provides better positioning of the deacylating water molecule caused by the presence of the imidazole ring of H170 and of the long side chain of K170 and L170.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11697/180378
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