Inhibition of the RTEM beta-lactamase from Escherichia coli. Interaction of enzyme with derivatives of olivanic acid.

@article{Charnas1981InhibitionOT,
  title={Inhibition of the RTEM beta-lactamase from Escherichia coli. Interaction of enzyme with derivatives of olivanic acid.},
  author={R L Charnas and Jeremy Knowles},
  journal={Biochemistry},
  year={1981},
  volume={20 10},
  pages={
          2732-7
        }
}
The interaction of the RTEM beta-lactamase with two derivatives of olivanic acid has been studied. The compound MM22382 (1) behaves simply as a good substrate for the enzyme and is a relatively ineffective inhibitor. In contrast, the sulfate ester MM13902 (2) is a poor substrate and an excellent inhibitor of the enzyme. The inhibition derives from a branching of the normal hydrolytic pathway of the enzyme. At long times, all the catalytic activity of the enzyme returns. Free sulfate ion is not… CONTINUE READING

Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-10 OF 16 CITATIONS

Identification of peptide inhibitors of penicillinase using a phage display library.

VIEW 1 EXCERPT
CITES BACKGROUND

Avibactam is a covalent, reversible, non-β-lactam β-lactamase inhibitor.

Carbapenems: past, present, and future.

VIEW 2 EXCERPTS
CITES BACKGROUND