Novel carbenicillin-hydrolyzing beta-lactamase (CARB-5) from Acinetobacter calcoaceticus var. anitratus.
A strain of Acinetobacter calcoaceticus var. anitratus highly resistant to ticarcillin but susceptible to ticarcillin in combination with clavulanic acid (2 mg/l) was found to produce a constitutive beta-lactamase. This enzyme was periplasmic with a characteristic substrate profile of a carbenicillin-hydrolyzing enzyme. Enzyme inhibition was detected with antiserum (anti-CARB-3), pCMB, cloxacillin, clavulanic acid and sulbactam. This novel enzyme with a molecular mass of 28,000 resembles other plasmid-mediated carbenicillinases (CARB) but differs in its apparent isoelectric point estimated as 6.3 and has been designated CARB-5 on this basis.
Paul
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G
CHU Cochin, Service de Bactériologie, Paris, France.
Joly-Guillou
M L
ML
Bergogne-Berezin
E
E
Névot
P
P
Philippon
A
A
D000150:Acinetobacter / Q000187:drug effects / Q000201:enzymology*; D002228:Carbenicillin / Q000378:metabolism*; D006868:Hydrolysis; D008826:Microbial Sensitivity Tests; D001618:beta-Lactamases / Q000032:analysis* / Q000276:immunology
D001618:beta-Lactamases; D002228:Carbenicillin