pH studies to elucidate the chemical mechanism of penicillin acylase from Kluyvera citrophila.

@article{Martn1993pHST,
  title={pH studies to elucidate the chemical mechanism of penicillin acylase from Kluyvera citrophila.},
  author={J P Mart{\'i}n and Ignacio Pri{\'e}to and Jos{\'e} Miguel Manche{\~n}o and Jos{\'e} L. Barbero and Roberto Arche},
  journal={Biotechnology and applied biochemistry},
  year={1993},
  volume={17 3},
  pages={
          311-25
        }
}
The variation with pH of the kinetic parameters of penicillin acylase from Kluyvera citrophila has been used to gain information about the chemical mechanism of the reaction catalysed by the enzyme. The pH-dependence of log (V/Km) for penicillin G showed that a group with a pK value over 4.7 must be deprotonated and that a group with a pK value over 9.7 must be protonated in the free enzyme for activity. The solvent perturbation and temperature studies indicated that these groups are… CONTINUE READING

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