Oxygen Michaelis constants for tyrosinase.
The Michaelis constant of tyrosinase for oxygen in the presence of monophenols and o-diphenols, which generate a cyclizable o-quinone, has been studied. This constant depends on the nature of the monophenol and o-diphenol and is always lower in the presence of the former than of the latter. From the mechanism proposed for tyrosinase and from its kinetic analysis [RodrÃguez-López, J. N., Tudela, J., Varón, R., GarcÃa-Carmona, F. and GarcÃa-Cánovas, F. (1992) J. Biol. Chem. 267, 3801-3810] a quantitative ratio has been established between the Michaelis constants for oxygen in the presence of monophenols and their o-diphenols. This ratio is used for the determination of the Michaelis constant for oxygen with monophenols when its value cannot be calculated experimentally.[1]References
- Oxygen Michaelis constants for tyrosinase. Rodríguez-López, J.N., Ros, J.R., Varón, R., García-Cánovas, F. Biochem. J. (1993) [Pubmed]
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