Use of electrospray mass spectrometry to directly observe an acyl enzyme intermediate in beta-lactamase catalysis

FEBS Lett. 1990 Dec 17;277(1-2):212-4. doi: 10.1016/0014-5793(90)80847-c.

Abstract

Electrospray mass spectrometry was used to directly observe intact acyl enzyme complexes formed between a class C beta-lactamase (from Enterobacter cloacae P99) and four poor substrates/inhibitors. In each case the molecular weight difference between the unreacted and the reacted beta-lactamase was consistent with the formation of an acyl enzyme.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acylation
  • Anti-Bacterial Agents / metabolism
  • Carbenicillin / chemistry
  • Enterobacter / enzymology
  • Mass Spectrometry / methods*
  • Molecular Weight
  • beta-Lactamases / chemistry
  • beta-Lactamases / metabolism*

Substances

  • Anti-Bacterial Agents
  • beta-Lactamases
  • Carbenicillin