2. Academic Validation
  3. The renal membrane dipeptidase (dehydropeptidase I) inhibitor, cilastatin, inhibits the bacterial metallo-beta-lactamase enzyme CphA

The renal membrane dipeptidase (dehydropeptidase I) inhibitor, cilastatin, inhibits the bacterial metallo-beta-lactamase enzyme CphA

  • Antimicrob Agents Chemother. 1995 Jul;39(7):1629-31. doi: 10.1128/AAC.39.7.1629.
S Keynan 1,  N M Hooper,  A Felici,  G Amicosante,  A J Turner
Affiliations

Affiliation

  • 1 Department of Biochemistry and Molecular Biology, University of Leeds, United Kingdom.
PMID: 7492120 DOI: 10.1128/AAC.39.7.1629
Abstract

The Aeromonas hydrophila AE036 chromosome contains a cphA gene encoding a metallo-beta-lactamase which is highly active against carbapenem Antibiotics such as imipenem. Here we show that the cphA gene product shares inhibitory similarities with a mammalian zinc peptidase, membrane dipeptidase (MDP; dehydropeptidase I). Both Enzymes are able to hydrolyze imipenem and are inhibited by cilastatin. The active site similarities of these Enzymes are not reflected in any significant primary sequence similarity.

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