Kinetic study of the effect of histidines 240 and 164 on TEM-149 enzyme probed by β-lactam inhibitors

Antimicrob Agents Chemother. 2014 Oct;58(10):6294-6. doi: 10.1128/AAC.02950-14. Epub 2014 Aug 4.

Abstract

In the present study, we performed a detailed kinetic analysis of the enzymes TEM-149, TEM-149(H240), and TEM-149(H164-H240) versus a large panel of inhibitors/inactivators, including penicillins, penems, carbapenems, monobactams, cephamycin, and carbacephem. These compounds behaved as poor substrates versus TEM-149, TEM-149(H240), and TEM-149(H164-H240) β-lactamases, and the Ki (inhibition constant), K (dissociation constant of the Henri-Michaelis complex), k+2 and k+3 (first-order acylation and deacylation constants, respectively), and k+2/K values were calculated.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbapenems / pharmacology
  • Histidine / chemistry*
  • Kinetics
  • Penicillins / pharmacology
  • beta-Lactamases / chemistry*
  • beta-Lactamases / metabolism*
  • beta-Lactams / pharmacology*

Substances

  • Carbapenems
  • Penicillins
  • beta-Lactams
  • Histidine
  • beta-Lactamases