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. 2000 Jun;44(6):1556–1561. doi: 10.1128/aac.44.6.1556-1561.2000

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
a

Kinetic experiments were performed using a protein extract with a specific activity of 13.61 μmol of nitrocefin hydrolyzed/min/μg of protein. 

b

Obtained by normalizing the value of each antibiotic to that for benzylpenicillin (taken as 100). 

c

Nitrocefin was used as the substrate (25 μg/ml) following 10 min of preincubation of enzyme and inhibitor. 

d

ND, hydrolysis not detected.