Inhibition of beta-lactamases by 6,6-bis(hydroxylmethyl)penicillanate

Bioorg Chem. 2001 Jun;29(3):140-5. doi: 10.1006/bioo.2001.1205.

Abstract

beta-Lactamases of classes A and C are the two most prevalent resistant determinants to beta-lactam antibiotics among bacterial pathogens. Both these enzymes pursue different mechanisms for their catalytic processes, highlighted by the fact that the hydrolytic water molecule in each approaches the ester of the intermediary acyl-enzyme species from the opposite ends. 6,6-Bis(hydroxylmethyl)penicillanate was designed as an inhibitor that would impair the approach of the hydrolytic water molecule in either of these enzymes upon formation of the acyl-enzyme species. The design, synthesis, and kinetic evaluation of this inhibitor are disclosed herein.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Enterobacter cloacae / enzymology
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / pharmacology*
  • Escherichia coli / enzymology
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Penicillanic Acid / analogs & derivatives
  • Penicillanic Acid / chemical synthesis*
  • Penicillanic Acid / pharmacology*
  • beta-Lactamase Inhibitors*

Substances

  • 6,6-bis(hydroxylmethyl)penicillanate
  • Enzyme Inhibitors
  • beta-Lactamase Inhibitors
  • Penicillanic Acid