Citation

Muñoz-Muñoz JL, Acosta-Motos JR, García-Molina F, Varon R, Garcia-Ruíz PA, Tudela J, García-Cánovas F, Rodríguez-López JN. Biochim. Biophys. Acta 2010; 1804(7): 1467-1475.

Copyright

(Copyright © 2010, Elsevier Publishing)

DOI

10.1016/j.bbapap.2010.02.015

PMID

20215052

Abstract

Under aerobic or anaerobic conditions, tyrosinase undergoes a process of irreversible inactivation induced by its physiological substrate L-dopa. Under aerobic conditions, this inactivation occurs through a process of suicide inactivation involving the form oxy-tyrosinase. Under anaerobic conditions, both the met- and deoxy-tyrosinase forms undergo irreversible inactivation. Suicide inactivation in aerobic conditions is slower than the irreversible inactivation under anaerobic conditions. The enzyme has less affinity for the isomer D-dopa than for L-dopa but the velocity of inactivation is the same. We propose mechanisms to explain these processes.

Language: en

Keywords

Time Factors; Kinetics; Models, Biological; Oxygen; Catalysis; Magnetic Resonance Spectroscopy; Agaricales; Dihydroxyphenylalanine; Spectrophotometry; Catalytic Domain; Protein Binding; Models, Chemical; Monophenol Monooxygenase; Catechol Oxidase