Kinetics and thermodynamics of catalysis by the inorganic pyrophosphatase of Escherichia coli in both directions.

@article{Baykov1990KineticsAT,
  title={Kinetics and thermodynamics of catalysis by the inorganic pyrophosphatase of Escherichia coli in both directions.},
  author={Alexander A Baykov and Alexander S. Shestakov and Vladimir N Kasho and Alexander V. Vener and Anton Ivanov},
  journal={European journal of biochemistry},
  year={1990},
  volume={194 3},
  pages={879-87}
}
Combined evidence obtained from the measurements of pyrophosphate hydrolysis and synthesis, oxygen exchange between phosphate and water, enzyme-bound pyrophosphate formation and Mg2+ binding enabled us to deduce the overall scheme of catalysis by Escherichia coli inorganic pyrophosphatase in the presence of Mg2+. We determined the equilibrium constants for Mg2+ binding to various enzyme species and forward and reverse rate constants for the four steps of the catalytic reaction, namely, binding… CONTINUE READING

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