Park KH1, Lee JR, Hahn HS, Kim YH, Bae CD, Yang JM, Oh S, Bae YJ, Kim DE, Hahn MJ.
Chem Pharm Bull (Tokyo). 2006 Sep;54(9):1266-70.Tyrosinase requires two copper ions at the active site, in order to oxidize phenols to catechols. In this study, the inhibitory effect of the copper-chelating compound, ammonium tetrathiotungstate (ATTT), on the tyrosinase activity was investigated. ATTT was determined to inactivate the activity of mushroom tyrosinase, in a dose-dependent manner. The kinetic substrate reaction revealed that ATTT functions as a kinetically competitive inhibitor in vitro, and that the enzyme-ATTT complex subsequently undergoes a reversible conformational change, resulting in the inactivation of tyrosinase. Read More