Author:
Perilli Mariagrazia,Mancini Alisia,Celenza Giuseppe,Bottoni Carlo,Bellio Pierangelo,Sabatini Alessia,Di Pietro Letizia,Brisdelli Fabrizia,Segatore Bernardetta,Amicosante Gianfranco
Abstract
ABSTRACTIn the present study, we performed a detailed kinetic analysis of the enzymes TEM-149, TEM-149H240, and TEM-149H164-H240versus a large panel of inhibitors/inactivators, including penicillins, penems, carbapenems, monobactams, cephamycin, and carbacephem. These compounds behaved as poor substrates versus TEM-149, TEM-149H240, and TEM-149H164-H240β-lactamases, and theKi(inhibition constant),K(dissociation constant of the Henri-Michaelis complex),k+2andk+3(first-order acylation and deacylation constants, respectively), andk+2/Kvalues were calculated.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
Cited by
3 articles.
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