Kinetic characterization of oxyresveratrol as a tyrosinase substrate

IUBMB Life. 2015 Nov;67(11):828-36. doi: 10.1002/iub.1439. Epub 2015 Oct 8.

Abstract

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

Keywords: alternative substrate; hydrogen peroxide; kinetic characterization; oxyresveratrol; tyrosinase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Fungal Proteins / antagonists & inhibitors
  • Fungal Proteins / chemistry*
  • Hydrogen Peroxide / chemistry
  • Hydroxylation
  • Kinetics
  • Levodopa / chemistry
  • Monophenol Monooxygenase / antagonists & inhibitors
  • Monophenol Monooxygenase / chemistry*
  • Plant Extracts / chemistry*
  • Resveratrol
  • Stilbenes / chemistry*
  • Substrate Specificity
  • Tyrosine / chemistry

Substances

  • Fungal Proteins
  • Plant Extracts
  • Stilbenes
  • Tyrosine
  • Levodopa
  • puag-haad
  • Hydrogen Peroxide
  • Monophenol Monooxygenase
  • Resveratrol