TABLE 2.
Kinetic and inhibition parameters of the OXA-24 β-lactamasea
Antibiotic | Km (μM) | Vmax (μmol/min/μl) | Relative Vmax/Kmb | Relative hydrolysis rateb | IC50 (μM)c |
---|---|---|---|---|---|
Benzylpenicillin | 65 | 370 | 100 | 100 | |
Cephaloridine | 395 | 200 | 9 | 64 | |
Oxacillin | NDd | ND | ND | <1 | |
Cloxacillin | ND | ND | ND | <1 | |
Methicillin | ND | ND | ND | <1 | |
Imipenem | 20 | 15 | 13 | 4 | |
Meropenem | 775 | 280 | 6 | 2 | |
Clavulanic acid | 50 | ||||
Sulbactam | 40 | ||||
Tazobactam | 0.5 |
Kinetic experiments were performed using a protein extract with a specific activity of 13.61 μmol of nitrocefin hydrolyzed/min/μg of protein.
Obtained by normalizing the value of each antibiotic to that for benzylpenicillin (taken as 100).
Nitrocefin was used as the substrate (25 μg/ml) following 10 min of preincubation of enzyme and inhibitor.
ND, hydrolysis not detected.