Inactivation of the RTEM .beta.-lactamase from Escherichia coli. Interaction of penam sulfones with the enzyme
- 1 May 1981
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 20 (10) , 2726-2731
- https://doi.org/10.1021/bi00513a004
Abstract
The characteristics of the reaction of a number of mechanism-based inactivators of RTEM .beta.-lactamase from E. coli have suggested that a common mechanistic pathway may be followed by many of these compounds. These ideas were tested by the synthesis and evaluation of some penam sulfones as .beta.-lactamase inactivators. The sulfones of poor .beta.-lactamase substrates are, as predicted, potent inactivators of the enzyme. A unique serine residue (Ser-70) is labeled by quinacillin sulfone and it is likely that this serine acts nucleophilically in the normal hydrolytic reaction of the .beta.-lactamase to form an acyl-enzyme intermediate.This publication has 8 references indexed in Scilit:
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