Steady-state and pre-steady-state kinetics of coenzyme A linked aldehyde dehydrogenase from Escherichia coli.

@article{Shone1981SteadystateAP,
  title={Steady-state and pre-steady-state kinetics of coenzyme A linked aldehyde dehydrogenase from Escherichia coli.},
  author={Clifford C. Shone and Herbert J. Fromm},
  journal={Biochemistry},
  year={1981},
  volume={20 26},
  pages={
          7494-501
        }
}
Coenzyme A linked aldehyde dehydrogenase from Escherichia coli strain B has been purified to a specific activity of 14 units/mg of protein, and initial rate and substrate analogue inhibition experiments have been performed. On the basis of these steady-state measurements, a bi-uni-uni-uni ping-pong mechanism is proposed in which NAD+ binds to the free enzyme followed by acetaldehyde. The product NADH is then released before coenzyme A (CoA) can bind, and acetyl-CoA is the final product released… CONTINUE READING

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