A rapid-kinetic study of the class C beta-lactamase of Enterobacter cloacae 908R

FEBS Lett. 1992 Jul 20;306(2-3):108-12. doi: 10.1016/0014-5793(92)80979-q.

Abstract

The individual rate constants for acylation and deacylation (k2 and k3, respectively) of the class C beta-lactamase of Enterobacter cloacae 908R by ampicillin and carbenicillin have been determined. For several other beta-lactams, the value of k2 was too high to be determined and the k2/k3 ratio could be larger than 10,000. Branched pathways were also shown to occur with several penicillins and cephalosporins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enterobacter cloacae / enzymology*
  • Kinetics
  • Substrate Specificity
  • beta-Lactamase Inhibitors
  • beta-Lactamases / metabolism*

Substances

  • beta-Lactamase Inhibitors
  • beta-Lactamases