Kinetic mechanism of vanillyl-alcohol oxidase with short-chain 4-alkylphenols.

@article{Fraaije1998KineticMO,
  title={Kinetic mechanism of vanillyl-alcohol oxidase with short-chain 4-alkylphenols.},
  author={Marco W Fraaije and Robert van den Heuvel and Jules C A A Roelofs and Willem J H van Berkel},
  journal={European journal of biochemistry},
  year={1998},
  volume={253 3},
  pages={712-9}
}
The kinetic mechanism of vanillyl-alcohol oxidase with 4-methylphenol, 4-ethylphenol, 4-propylphenol and their C alpha-deuterated analogs has been studied at pH 7.5 and 25 degrees C. Conversion of 4-methylphenol is extremely slow (0.005 s(-1)) while the enzyme is largely in the reduced form during turnover. 4-Ethylphenol and 4-propylphenol are readily converted while the enzyme is mainly in the oxidized form during turnover. The deuterium kinetic isotope effect for overall catalysis ranges… CONTINUE READING

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