Sensitivity of Aeromonas hydrophila carbapenemase to delta3-cephems: comparative study with other metallo-beta-lactamases

A Felici; M Perilli; N Franceschini; G M Rossolini; M Galleni; J M Frere; A Oratore; G Amicosante

doi:10.1128/AAC.41.4.866

Sensitivity of Aeromonas hydrophila carbapenemase to delta3-cephems: comparative study with other metallo-beta-lactamases

Antimicrob Agents Chemother. 1997 Apr;41(4):866-8. doi: 10.1128/AAC.41.4.866.

Authors

A Felici¹, M Perilli, N Franceschini, G M Rossolini, M Galleni, J M Frere, A Oratore, G Amicosante

Affiliation

¹ Dipartimento di Scienze e Tecnologie Biomediche Cattedra di Chimica Biologica e di Enzimologia, Università degli Studi dell'Aquila, Coppito (L'Aquila), Italy.

Abstract

Ceftriaxone and ceftriaxone S-oxide behaved as inactivators against the metallo-beta-lactamase of Aeromonas hydrophila AE036 and as substrates for the zinc beta-lactamase produced by Bacillus cereus (569/H/9) and Stenotrophomonas maltophilia ULA 511. Moreover, RO 09-1428, a catechol-cephalosporin, was not recognized by the A. hydrophila enzyme. Panipenem, cephalosporin C, cephalosporin C-gamma-lactone, and loracarbef were substrates for the three studied beta-lactamases.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Aeromonas hydrophila / drug effects
Aeromonas hydrophila / enzymology*
Bacterial Proteins*
Cyclosporins / pharmacology*
Enzyme Inhibitors / pharmacology*
Hydrolysis
Kinetics
beta-Lactamase Inhibitors*
beta-Lactamases

Substances

Bacterial Proteins
Cyclosporins
Enzyme Inhibitors
beta-Lactamase Inhibitors
beta-Lactamases
carbapenemase