Identification of p-hydroxybenzyl alcohol, tyrosol, phloretin and its derivate phloridzin as tyrosinase substrates

• Published in: Bioorganic & medicinal chemistry 2015-07, Vol.23 (13), p.3738-3746
• Main Authors: Ortiz-Ruiz, Carmen Vanessa, Berna, Jose, Garcia-Molina, Maria del Mar, Tudela, Jose, Tomas, Virginia, Garcia-Canovas, Francisco
• Format: Article
• Language: English
• Subjects: Alternative substrate; Benzyl Alcohols - chemistry; Enzyme Assays; Enzyme Inhibitors - chemistry; Fungal Proteins - antagonists & inhibitors; Fungal Proteins - chemistry; Kinetics; Levodopa - chemistry; Monophenol Monooxygenase - antagonists & inhibitors; Monophenol Monooxygenase - chemistry; p-Hydroxybenzyl alcohol; Phenylacetates - chemistry; Phenylethyl Alcohol - analogs & derivatives; Phenylethyl Alcohol - chemistry; Phloretin; Phloretin - chemistry; Phlorhizin - chemistry; Phloridzin; Substrate Specificity; Tyrosinase; Tyrosine - chemistry; Tyrosol
• ISSN: 0968-0896; 1464-3391
• DOI: 10.1016/j.bmc.2015.04.016

[Display omitted] In recent years, the hydroxyalkylphenols p-hydroxybenzyl alcohol and tyrosol, and the compound phloretin and its derivate phloridzin have been described as inhibitors of the enzyme tyrosinase. When the monophenolase and the diphenolase activities of tyrosinase on its physiological substrates l-dopa and/or l-tyrosine are measured in the presence of these compounds, the rate of action of the enzyme decreases. These findings led to the identification of these compounds as inhibitors. However, these molecules show an unusual behavior as inhibitors of the enzyme indeed, in this study, we demonstrate that they are not true inhibitors but alternative substrates of the enzyme.