Kinetic study of monophenol and o-diphenol binding to oxytyrosinase

• Published in: Journal of molecular catalysis. B, Enzymatic Vol. 32; no. 5; pp. 185 - 192
• Main Authors: García-Molina, F., Peñalver, M.J., Fenoll, L.G., Rodríguez-López, J.N., Varón, R., García-Cánovas, F., Tudela, J.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01.03.2005; Elsevier Science
• Subjects: Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; Dead-end complex; Fundamental and applied biological sciences. Psychology; Methods. Procedures. Technologies; Monophenol and o-diphenol; Oxytyrosinase; Dead-end complex; Monophenol and o-diphenol; Oxytyrosinase; Phenols; Kinetics; Substrate enzyme complex

The complex reaction mechanism of tyrosinase involves three enzymatic forms, two overlapping catalytic cycles and a dead-end complex. The deoxytyrosinase form binds oxygen with a high degree of affinity, K s O 2 = 46.6 ± 2.4 μM. The mettyrosinase and oxytyrosinase forms bind monophenols and o-diphen...