Novel carbenicillin-hydrolyzing beta-lactamase (CARB-5) from Acinetobacter calcoaceticus var. anitratus.

@article{Paul1989NovelCB,
  title={Novel carbenicillin-hydrolyzing beta-lactamase (CARB-5) from Acinetobacter calcoaceticus var. anitratus.},
  author={G{\'e}rard C. Paul and Marie-laure Joly-Guillou and Eug{\'e}nie Bergogne-B{\'e}r{\'e}zin and P A Nevot and Alain Philippon},
  journal={FEMS microbiology letters},
  year={1989},
  volume={50 1-2},
  pages={
          45-50
        }
}
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… CONTINUE READING

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