Kinetic characterization of oxyresveratrol as a tyrosinase substrate.

作者: Carmen Vanessa Ortiz-Ruiz , Manuel Ballesta de los Santos , Jose Berna , Jose Fenoll , Pedro Antonio Garcia-Ruiz

DOI: 10.1002/IUB.1439

关键词: OxyresveratrolTyrosinaseStereochemistryHydroxylationSubstrate (chemistry)CatalysisKineticsFungal proteinChemistryMichaelis–Menten kinetics

摘要: Oxyresveratrol is a stilbenoid described as powerful inhibitor of tyrosinase and proposed skin-whitening anti-browning agent. However, the enzyme capable acting on it, considering it substrate, has been proved in case its analogous resveratrol. Tyrosinase hydroxylates oxyresveratrol to an o-diphenol oxidizes latter o-quinone, which finally isomerizes p-quinone. For these reactions take place presence Eox (oxy-tyrosinase) form necessary. The kinetic analysis mechanism allowed characterization this molecule substrate tyrosinase, affording catalytic constant 5.39 ± 0.21 sec(-1) Michaelis 8.65 ± 0.73 µM.

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