Citation

Munoz-Munoz JL, García-Molina F, García-Ruiz PA, Varon R, Tudela J, García-Cánovas F, Rodriguez-Lopez JN. Biochim. Biophys. Acta 2009; 1794(2): 244-253.

Copyright

(Copyright © 2009, Elsevier Publishing)

DOI

10.1016/j.bbapap.2008.10.002

PMID

19010454

Abstract

A kinetic study of the inactivation of tyrosinase by L- and D-ascorbic acid isomers has been carried out. In aerobic conditions, a suicide inactivation mechanism operates, which was attributed to the enzymatic form oxytyrosinase. This suicide inactivation is stereospecific as regards the affinity of the enzyme for the substrate but not as regards the speed of the process, which is the same for both isomers, reflecting the influence of the chemical shift of the carbon C-2 (delta(2)) and C-3 (delta(3)) as seen by (13)C-NMR. The inactivation of deoxytyrosinase and mettyrosinase observed in anaerobic conditions, is irreversible and faster than the suicide inactivation process, underlining the fact that the presence of oxygen protects the enzyme against inactivation.

Language: en

Keywords

Ascorbic Acid; Kinetics; Magnetic Resonance Spectroscopy; Monophenol Monooxygenase; Oxygen; Stereoisomerism; Structure-Activity Relationship; Substrate Specificity