Novel carbenicillin-hydrolyzing β-lactamase (CARB-5) from Acinetobacter calcoaceticus var. anitratus
| Autor: | M.L. Joly-Guillou, G. Paul, E. Bergogne-Berezin, Alain Philippon, Pierre Névot |
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| Rok vydání: | 1989 |
| Předmět: |
Microbial Sensitivity Tests
Microbiology beta-Lactamases Clavulanic acid polycyclic compounds Genetics medicine Molecular Biology chemistry.chemical_classification Acinetobacter biology Hydrolysis Sulbactam Periplasmic space biochemical phenomena metabolism and nutrition Carbenicillin biology.organism_classification Enzyme chemistry Biochemistry Ticarcillin bacteria Acinetobacter calcoaceticus medicine.drug |
| Zdroj: | FEMS Microbiology Letters. 59:45-50 |
| ISSN: | 1574-6968 0378-1097 |
| DOI: | 10.1111/j.1574-6968.1989.tb03080.x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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