Catalytic mechanism of active-site serine beta-lactamases: role of the conserved hydroxy group of the Lys-Thr(Ser)-Gly triad.

@article{Dubus1994CatalyticMO,
  title={Catalytic mechanism of active-site serine beta-lactamases: role of the conserved hydroxy group of the Lys-Thr(Ser)-Gly triad.},
  author={Alain Dubus and J M Wilkin and Xavier Raquet and Staffan J. Normark and Jean Marie Fr{\`e}re},
  journal={The Biochemical journal},
  year={1994},
  volume={301 ( Pt 2)},
  pages={
          485-94
        }
}
The role of the conserved hydroxy group of the Lys-Thr(Ser)-Gly [KT(S)G] triad has been studied for a class A and a class C beta-lactamase by site-directed mutagenesis. Surprisingly, the disappearance of this functional group had little impact on the penicillinase activity of both enzymes. The cephalosporinase activity was much more affected for the class A S235A (Ser235-->Ala) and the class C T316V (Thr315-->Val) mutants, but the class C T316A mutant was less impaired. Studies were extended to… CONTINUE READING

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