Competitive inhibition of mushroom tyrosinase by 4-substituted benzaldehydes.
A kinetic study of the inhibition of mushroom tyrosinase by 4-substituted benzaldehydes showed that these compounds behave as classical competitive inhibitors, inhibiting the oxidation of L-3,4-dihydroxyphenylalanine (L-DOPA) by mushroom tyrosinase (o-diphenolase activity). The kinetic parameter (K(I)) characterizing this inhibition was evaluated for all of the seven compounds assayed. Cuminaldehyde showed the most potent inhibitory activity (K(I) = 9 microM). It also inhibited the oxidation of L-tyrosine by mushroom tyrosinase (o-monophenolase activity) in a competitive manner. The corresponding kinetic parameter for this inhibition was evaluated (K(I) = 0.12 mM).
Jiménez
M
M
Departamento de Bioquímica y Biología Molecular A, Unidad Docente de Biología, Facultad de Veterinaria, Universidad de Murcia, E-30080, Murcia, Spain. mja@um.es
Chazarra
S
S
Escribano
J
J
Cabanes
J
J
García-Carmona
F
F
D000363:Agaricales / Q000201:enzymology*; D001547:Benzaldehydes / Q000494:pharmacology*; D007700:Kinetics; D010455:Peptides / Q000187:drug effects*
D001547:Benzaldehydes; D010455:Peptides; C032175:benzaldehyde