title: Novel carbenicillin-hydrolyzing beta-lactamase (CARB-5) from Acinetobacter calcoaceticus var. anitratus.
abstract: 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.
authors: CHU Cochin, Service de Bactériologie, Paris, France.
authors: G
authors: G
authors: Paul
authors: M L
authors: ML
authors: Joly-Guillou
authors: E
authors: E
authors: Bergogne-Berezin
authors: P
authors: P
authors: Névot
authors: A
authors: A
authors: Philippon
mesh_terms: D000150:Acinetobacter / Q000187:drug effects / Q000201:enzymology*; D002228:Carbenicillin / Q000378:metabolism*; D006868:Hydrolysis; D008826:Microbial Sensitivity Tests; D001618:beta-Lactamases / Q000032:analysis* / Q000276:immunology
chemical_list: D001618:beta-Lactamases; D002228:Carbenicillin