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Puerol A ( 1 ) from Amorpha fruticosa showed highly potent inhibition against both monophenolase (IC 50 = 2.2 μM) and diphenolase (IC 50 = 3.8 μM) of tyrosinase. We tried to obtain a full story of enzyme inhibitory behavior for inhibitor 1 because the butenolide skeleton has never been reported as a tyrosinase inhibitor. Puerol A was proved as a reversible, competitive, simple slow-binding inhibitor, according to the respective parameters; k  3 = 0.0279 μM -1 min -1 and k  4 = 0.003 min -1 . A longer lag-phase and a reduced static-state activity of the enzyme explained that puerol A had a tight formation of the complex with E met . Dose-dependent inhibition was also confirmed by high-performance liquid chromatography (HPLC) analysis using N -acetyl-l-tyrosine as a substrate, which was completely inhibited at 20 μM. A high binding affinity of 1 to tyrosinase was confirmed by fluorescence quenching analysis. Moreover, puerol A decreased melanin content in the B16 melanoma cell dose-dependently with an IC 50 of 11.4 μM.

Tyrosinase Inhibition and Kinetic Details of Puerol A Having But-2-Enolide Structure from Amorpha fruticosa