Ellagic acid inhibited tyrosinase activity in a reversible manner and was a mixed tyrosinase inhibitor. The value of the semi‐inhibitory rate (IC50) was 0.2 ± 0.05 mM. The results of enzyme kinetics indicated that ellagic acid could effectively inhibit tyrosinase activity. The activities of ellagic acid in inhibiting mushroom tyrosinase and cell proliferation were evaluated in this research. Our study suggests that oxymatrine is an important agent for various applications related to pigment formation. Knowledge of tyrosinase inhibition can provide medical, cosmetic, and agricultural applications. This strategy of predicting tyrosinase inhibition by simulation of docking coupling with kinetics may prove useful in screening for potential tyrosinase inhibitors. The results also suggested that oxymatrine interacts mostly with the residues of CYS83 and HIS263 in the active site of tyrosinase. We also conducted a docking simulation between tyrosinase and oxymatrine using two docking programs, Dock6.3 and AutoDock4.2 (binding energy was -118.81 kcal/mol for Dock6 and -8.04 kcal/mol for AutoDock4). Measurements of intrinsic and ANS-binding fluorescences showed that oxymatrine did not induce any conspicuous changes in the tertiary structure. Kinetic analysis showed that oxymatrine reversibly inhibited tyrosinase in a mixed-type manner. We found that oxymatrine significantly inhibited tyrosinase, and that this reaction was not accompanied by detectable conformational changes. A combination of enzymatic inhibition kinetics and computational prediction was employed to search for an effective inhibitor of tyrosinase.
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