Thiol-group binding of zinc to a beta-lactamase of Bacillus cereus: differential effects on enzyme activity with penicillin and cephalosporins as substrates.

@article{Sabath1968ThiolgroupBO,
  title={Thiol-group binding of zinc to a beta-lactamase of Bacillus cereus: differential effects on enzyme activity with penicillin and cephalosporins as substrates.},
  author={L. D. Sabath and Maxwell Finland},
  journal={Journal of bacteriology},
  year={1968},
  volume={95 5},
  pages={1513-9}
}
Zinc, which is required for the hydrolysis of cephalosporins by a crude enzyme from Bacillus cereus 569, also increased the stability of this activity during storage. A loss in activity of the zinc-activated enzyme which occurred on prolonged hydrolysis of cephalosporin C was not restored by further addition of zinc. The thiol reagents N-ethyl maleimide (NEM), iodoacetic acid (IAA), CdCl(2), and p-chloromercuribenzoate, all at 10(-3)m, and iodine at 1.6 x 10(-3)n prevent zinc activation of the… CONTINUE READING