Inhibition of the metallo-beta-lactamase produced from Serratia marcescens by thiol compounds

Biol Pharm Bull. 1997 Nov;20(11):1136-40. doi: 10.1248/bpb.20.1136.


Low molecular weight thiol compounds have been found to be strong inhibitors of metallo-beta-lactamase (IMP-1) produced by Serratia marcescens TN9106, which was expressed by Echerichia coli JM109 cells. Mercaptoacetic acid and 2-mercaptopropionic acid strongly and competitively inhibited IMP-1 with Ki of 0.23 and 0.19 microM, respectively. 2-Mercaptoethanol reversibly inhibited IMP-1 but did not show simple competitive inhibition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Enzyme Inhibitors / pharmacology*
  • Escherichia coli / genetics
  • Kinetics
  • Recombinant Proteins / antagonists & inhibitors
  • Recombinant Proteins / genetics
  • Serratia marcescens / enzymology*
  • Sulfhydryl Compounds / pharmacology*
  • beta-Lactamase Inhibitors*
  • beta-Lactamases / genetics


  • Bacterial Proteins
  • Enzyme Inhibitors
  • Recombinant Proteins
  • Sulfhydryl Compounds
  • beta-Lactamase Inhibitors
  • beta-Lactamases