Inhibition of Providencia stuartii cell envelope enzymes by chlorhexidine

J Antimicrob Chemother. 1987 Jun;19(6):743-51. doi: 10.1093/jac/19.6.743.

Abstract

The possibility that chlorhexidine is a specific inhibitor of membrane bound bacterial adenosine triphosphatase (ATPase) was addressed. The in-vitro susceptibilities of several Providencia stuartii cell envelope enzymes, including ATPase, to chlorhexidine were compared. The following concentrations of chlorhexidine were required to cause 50% inhibition of enzyme activity in preparations from chlorhexidine-sensitive strains (MIC 50 mg chlorhexidine/l): ATPase (160 mg/l), succinic dehydrogenase (greater than 300 mg/l), penicillin binding protein 7 (300 mg/l) and beta-lactamase (45 mg/l). Fifty per cent inhibition of the ATPase from a chlorhexidine-resistant strain (MIC 1600 mg/l) was achieved at an in-vitro concentration of 225 mg chlorhexidine/l. Our observations do not support the suggestion that bacterial membrane-bound ATPases are specific targets for chlorhexidine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / antagonists & inhibitors*
  • Cell Membrane / drug effects
  • Cell Membrane / enzymology
  • Chlorhexidine / pharmacology*
  • Proteus / drug effects*
  • Providencia / drug effects*
  • Providencia / enzymology

Substances

  • Adenosine Triphosphatases
  • Chlorhexidine