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Inhibitory Effect of Ammonium Tetrathiotungstate on Tyrosinase and Its Kinetic Mechanism

Inhibitory Effect of Ammonium Tetrathiotungstate on Tyrosinase and Its Kinetic Mechanism

Kyung-Hee Park, Jae-Rin Lee, Hwa-Sun Hahn, Young-Hoon Kim, Chang-Dae Bae, Jun-Mo Yang, Sangtaek Oh, Yu-Jin Bae, Dong-Eun Kim, Myong-Joon Hahn

Chem Pharm Bull (Tokyo). 2006 Sep;54(9):1266-70.

PMID: 16946532

Abstract:

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. In human melanin-producing cells, ATTT evidenced a more profound tyrosinase-inhibitory effect than has been seen in the previously identified tyrosinase inhibitors, including kojic acid and hydroquinone. Our results may provide useful information for the development of whitening agent.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP13862787	Ammonium tetrathiotungstate		13862-78-7	Price

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