Tyrosinase inhibition kinetics of anisic acid.
Anisic acid (p-methoxybenzoic acid) was characterized as a tyrosinase inhibitor from ani-seed, a common food spice. It inhibited the oxidation of L-3,4-dihydroxyphenylalanine (L-DOPA) catalyzed by tyrosinase with an IC50 of 0.60 mM. The inhibition of tyrosinase by anisic acid is a reversible reaction with residual enzyme activity. This phenolic acid was found to be a classical noncompetitive inhibitor and the inhibition constant K(I) was obtained as 0.603 mM. Anisic acid also inhibited the hydroxylation of L-tyrosine catalyzed by tyrosinase. The lag phase caused by the monophenolase activity was lengthened and the steady-state activity of the enzyme was decreased by anisic acid.
Kubo
Isao
I
Department of Environmental Science, Policy and Management, University of California, Berkeley, California 94720-3112, USA. ikubo@uclink4.berkeley.edu
Chen
Qing-Xi
QX
Nihei
Ken-Ichi
K
Calderón
José S
JS
Céspedes
Carlos L
CL
D000363:Agaricales / Q000201:enzymology; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D062425:Hydroxybenzoate Ethers; D062385:Hydroxybenzoates / Q000494:pharmacology*; D007700:Kinetics; D007980:Levodopa / Q000378:metabolism; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors*; D010101:Oxygen Consumption / Q000187:drug effects
D004791:Enzyme Inhibitors; D062425:Hydroxybenzoate Ethers; D062385:Hydroxybenzoates; D007980:Levodopa; C004520:4-anisic acid; D014442:Monophenol Monooxygenase