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

AUTOR(ES)

Keynan, S

RESUMO

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.

Documentos Relacionados

• Stability of New Carbapenem DA-1131 to Renal Dipeptidase (Dehydropeptidase I)
• A novel integron-like element carrying the metallo-beta-lactamase gene blaIMP.
• Biochemical properties and purification of metallo-beta-lactamase from Bacteroides fragilis.
• High specificity of cphA-encoded metallo-beta-lactamase from Aeromonas hydrophila AE036 for carbapenems and its contribution to beta-lactam resistance.
• Biochemical characterization of the metallo-beta-lactamase CcrA from Bacteroides fragilis TAL3636.