PMID: 9161722May 1, 1997Paper

Kinetic study of the oxidation of 4-hydroxyanisole catalyzed by tyrosinase

Biochemistry and Molecular Biology International
J C EspínF García-Cánovas

Abstract

Despite the importance of the substrate 4-hydroxyanisole in melanoma therapy, the kinetics of its oxidation catalyzed by tyrosinase has never been properly characterized. This approach is reported here for the first time. The applicability to 4-hydroxyanisole of the reaction mechanism of tyrosinase previously proposed for other monophenols has been corroborated. The Michaelis constant for the oxidation of 4-hydroxyanisole catalyzed by mushroom tyrosinase was (62 +/- 1.5) microM at pH 7 and increased when the pH decreased, reaching a value of (195 +/- 5) microM at pH 5.5. However the maximum steady-state rate, whose value was (0.54 +/- 0.01) microM/min, did not change with the pH. The apparent catalytic constant was (184 +/- 5) s-1, around twenty three times higher than that previously described for L-tyrosine (8 s-1).

Citations

Mar 21, 2000·Biophysical Chemistry·L G FenollJ Tudela
Feb 26, 2000·European Journal of Biochemistry·J C EspínF García-Cánovas
Sep 21, 2000·European Journal of Biochemistry·L G FenollF García-Cánovas
Feb 21, 2008·The Journal of Pharmacy and Pharmacology·Dong-Seok KimKyoung-Chan Park
Nov 18, 2008·Biochimica Et Biophysica Acta·Jose Luis Munoz-MunozJose Neptuno Rodriguez-Lopez
Jul 5, 2018·Langmuir : the ACS Journal of Surfaces and Colloids·Camelia DraghiciCornelia G Palivan

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