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. 1995 Jul;39(7):1629–1631. doi: 10.1128/aac.39.7.1629

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

S Keynan 1, N M Hooper 1, A Felici 1, G Amicosante 1, A J Turner 1
PMCID: PMC162797  PMID: 7492120

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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Selected References

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