Overview on tyrosinases: Genetics, molecular biology, phylogenetic relationship.

Abstract

Tyrosinases (TYRs) are enzymes found in various organisms that are crucial for melanin biosynthesis, coloration, and UV protection. They play vital roles in insect cuticle sclerotization, mollusk shell formation, fungal and bacterial pigmentation, biofilm formation, and virulence. Structurally, TYRs feature copper-binding sites that are essential for catalytic activity, facilitating substrate oxidation via interactions with conserved histidine residues. TYRs exhibit diversity across animals, plants, fungi, mollusks, and bacteria, reflecting their roles and function. Eukaryotic TYRs undergo post-translational modifications, such as glycosylation, which affect protein folding and activity. Bacterial TYRs are categorized into five types based on their structural variation, domain organization and enzymatic properties, showing versatility across bacterial species. Moreover, bacterial TYRs, akin to fungal TYRs, have been implicated in the synthesis of secondary metabolites with antimicrobial properties. TYRs share significant sequence homology with hemocyanins, oxygen-carrier proteins in mollusks and arthropods, highlighting their evolutionary relationships. The evolution of TYRs underscores the dynamic nature of these enzymes and reflects adaptive strategies across diverse taxa.