The pH-dependence of class B and class C β-lactamases

Abstract
The classification by structure allots .beta.-lactamases to (at present) 3 classes, A, B and C. The pH-dependence of the kinetic parameters for class B and class C was determined. They differ from each other and from class A .beta.-lactamases. The class B enzyme was .beta.-lactamase II from Bacillus cereus 569/H/9. The plots of kcat against pH for the hydrolysis of benzylpenicillin by Zn(II)-requiring .beta.-lactamase II and Co(II)-requiring .beta.-lactamase II were not symmetrical, but those of kcat/Km were. A similar feature was observed for the hydrolysis of benzylpenicillin and cephalosporin C by a class C .beta.-lactamase from Pseudomonas aeruginosa. The results were interpreted by a scheme in which 2 ionic forms of an intermediate can give a product, but do so at differing rates.