A kinetic study of the suicide inactivation of an enzyme measured through coupling reactions. Application to the suicide inactivation of tyrosinase

Abstract

A systematic procedure for the kinetic study of reaction mechanisms with enzyme inactivation induced by a suicide substrate in the presence or in the absence of an auxiliary substrate, when the enzyme activity is measured through coupling reactions, enzymically catalysed or not, was developed and analysed by using the transient-phase approach. The methodology is established to determine the parameters and kinetic constants corresponding to the enzyme suicide inactivation and the coupling reactions. This approach is illustrated by a study of the suicide inactivation of tyrosinase by catechol in the presence of L-proline. Treatment of the experimental data was carried out by non-linear regression.

The Mechanism-based Inactivation of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase by Catecholic Substrates

“…For 3-chlorocatechol, DHB was used as a reporter substrate, and j 3E app was obtained using Equation 5 (48).…”

A General Progress Curve Method for the Kinetic Analysis of Suicide Enzyme Inhibitors

“…dium (21)(22)(23)(24). However, to our knowledge, the progress and are comparable to those defined by the dilution assay method of suicide inhibitors (see Appendix for curve kinetic analysis method for suicide inhibitors has not been applied to the most common case (most com-the definition of these parameters).…”

Stability, structural and suicide inactivation changes of Mushroom tyrosinase after acetylation by N-acetylimidazole

“…MT has been frequently studied with regard to its suicide substrate inactivation [21][22][23] and stability [24,25]. It was recently shown that the Tyr residues spatial arrangement plays a noticeable role in the efficiency of the MT activities [25].…”