Considerations about the inhibition of monophenolase and diphenolase activities of tyrosinase. Characterization of the inhibitor concentration which generates 50 % of inhibition, type and inhibition constants. A review

Pablo García Molina; Adrian Saura-Sanmartin; Jose Berna; Jose Antonio Teruel; Jose Luis Muñoz Muñoz; Jose Neptuno Rodríguez López; Francisco García Cánovas; Francisco García Molina

doi:10.1016/j.ijbiomac.2024.131513

Considerations about the inhibition of monophenolase and diphenolase activities of tyrosinase. Characterization of the inhibitor concentration which generates 50 % of inhibition, type and inhibition constants. A review

Int J Biol Macromol. 2024 Apr 10;267(Pt 2):131513. doi: 10.1016/j.ijbiomac.2024.131513. Online ahead of print.

Authors

Pablo García Molina¹, Adrian Saura-Sanmartin², Jose Berna³, Jose Antonio Teruel⁴, Jose Luis Muñoz Muñoz⁵, Jose Neptuno Rodríguez López¹, Francisco García Cánovas¹, Francisco García Molina⁶

Affiliations

¹ GENZ-Group of Research on Enzymology, Department of Biochemistry and Molecular Biology-A, Regional Campus of International Excellence "Campus Mare Nostrum", University of Murcia, Espinardo, Murcia, Spain.
² Department of Organic Chemistry, Faculty of Chemistry, University of Murcia, E-30100 Espinardo, Murcia, Spain. Electronic address: adrian.saura@um.es.
³ Department of Organic Chemistry, Faculty of Chemistry, University of Murcia, E-30100 Espinardo, Murcia, Spain.
⁴ Department of Biochemistry and Molecular Biology-A, Regional Campus of International Excellence "Campus Mare Nostrum", University of Murcia, Espinardo, Murcia, Spain.
⁵ Microbial Enzymology Lab, Department of Applied Sciences, Ellison Building A, University of Northumbria, Newcastle Upon Tyne, UK.
⁶ Department of Anatomía Patológica, Hospital General Universitario Reina Sofía, Av. Intendente Jorge Palacios, 1, 30003 Murcia, Spain. Electronic address: pacogm@um.es.

PMID: 38608979
DOI: 10.1016/j.ijbiomac.2024.131513

Abstract

Tyrosinase is a copper oxidase enzyme which catalyzes the first two steps in the melanogenesis pathway, L-tyrosine to L-dopa conversion and, then, to o-dopaquinone and dopachrome. Hypopigmentation and, above all, hyperpigmentation issues can be originated depending on their activity. This enzyme also promotes the browning of fruits and vegetables. Therefore, control of their activity by regulators is research topic of great relevance. In this work, we consider the use of inhibitors of monophenolase and diphenolase activities of the enzyme in order to accomplish such control. An experimental design and data analysis which allow the accurate calculation of the degree of inhibition of monophenolase activity (i_M) and diphenolase activity (i_D) are proposed. The IC₅₀ values (amount of inhibitor that causes 50 % inhibition at a fixed substrate concentration) can be calculated for the two activities and from the values of IC₅₀^M (monophenolase) and IC₅₀^D(diphenolase). Additionally, the strength and type of inhibition can be deduced from these values. The data analysis from these IC₅₀^D values allows to obtain the values of [Formula: see text] or [Formula: see text] , or and [Formula: see text] from the values of IC₅₀^M. In all cases, the values of the different must satisfy their relationship with IC₅₀^M and IC₅₀^D.

Keywords: Degree of inhibition; Diphenolase activity; IC(50); Inhibition; Monophenolase activity; Tyrosinase.

Publication types

Review