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Kinetic characterization of oxyresveratrol as a tyrosinase substrate.
Ortiz-Ruiz, Carmen Vanessa; Ballesta de Los Santos, Manuel; Berna, Jose; Fenoll, Jose; Garcia-Ruiz, Pedro Antonio; Tudela, Jose; Garcia-Canovas, Francisco.
Affiliation
  • Ortiz-Ruiz CV; GENZ: Grupo De Investigación Enzimología, Departamento De Bioquímica Y Biología Molecular-A, Facultad De Biología, Campus De Excelencia Internacional "Mare Nostrum", Universidad De Murcia, Murcia, Spain.
  • Ballesta de Los Santos M; GENZ: Grupo De Investigación Enzimología, Departamento De Bioquímica Y Biología Molecular-A, Facultad De Biología, Campus De Excelencia Internacional "Mare Nostrum", Universidad De Murcia, Murcia, Spain.
  • Berna J; Grupo De Química Orgánica Sintética. Departamento De Química Orgánica. Facultad De Química, Campus De Excelencia Internacional "Mare Nostrum", Universidad De Murcia, Murcia, Spain.
  • Fenoll J; IMIDA: Instituto Murciano De Investigación Y Desarrollo Agrario Y Alimentario, Murcia, Spain.
  • Garcia-Ruiz PA; QCPAI: Grupo De Química De Carbohidratos, Polímeros Y Aditivos Industriales, Departamento De Química Orgánica. Facultad De Química, Campus De Excelencia Internacional "Mare Nostrum", Universidad De Murcia, Murcia, Spain.
  • Tudela J; GENZ: Grupo De Investigación Enzimología, Departamento De Bioquímica Y Biología Molecular-A, Facultad De Biología, Campus De Excelencia Internacional "Mare Nostrum", Universidad De Murcia, Murcia, Spain.
  • Garcia-Canovas F; GENZ: Grupo De Investigación Enzimología, Departamento De Bioquímica Y Biología Molecular-A, Facultad De Biología, Campus De Excelencia Internacional "Mare Nostrum", Universidad De Murcia, Murcia, Spain.
IUBMB Life ; 67(11): 828-36, 2015 Nov.
Article in En | MEDLINE | ID: mdl-26450473
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.
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Full text: 1 Database: MEDLINE Main subject: Stilbenes / Fungal Proteins / Plant Extracts / Monophenol Monooxygenase Language: En Journal: IUBMB Life Year: 2015 Type: Article Affiliation country: Spain

Full text: 1 Database: MEDLINE Main subject: Stilbenes / Fungal Proteins / Plant Extracts / Monophenol Monooxygenase Language: En Journal: IUBMB Life Year: 2015 Type: Article Affiliation country: Spain