Physical and kinetic properties of a pyridoxal reductase purified from bakers' yeast.

@article{Guirard1988PhysicalAK,
  title={Physical and kinetic properties of a pyridoxal reductase purified from bakers' yeast.},
  author={B M Guirard and Esmond E. Snell},
  journal={BioFactors},
  year={1988},
  volume={1 2},
  pages={187-92}
}
Pyridoxine dehydrogenase (1.1.1.65) (pyridoxal reductase), purified to homogeneity from baker's yeast, is a monomer of Mr approximately 33,000. It catalyzes the reversible oxidation of pyridoxine by NADP to yield pyridoxal and NADPH; equilibrium lies far in the direction of pyridoxine formation (Keq approximately 1.4 X 10(11) l/mol at 25 degrees C). Reduction of pyridoxal occurs most rapidly at pH 6.0-7.0; oxidation of pyridoxine is optimal at pH 8.6. NAD and NADH do not replace NADP and NADPH… CONTINUE READING

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