| Literature DB >> 8352753 |
J N Rodríguez-López1, J R Ros, R Varón, F García-Cánovas.
Abstract
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 [Rodríguez-López, J. N., Tudela, J., Varón, R., García-Carmona, F. and García-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.Entities:
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Year: 1993 PMID： 8352753 PMCID： PMC1134447 DOI： 10.1042/bj2930859
Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857