Tyrosinases: a family of copper-containing metalloenzymes

Abstract

Tyrosinases (TYRs) are a family of copper-containing metalloenzymes that are present in all domains of life. TYRs catalyze the reactions that start the biosynthesis of melanin, the main pigment of the animal kingdom, and are also involved in the formation of the bright colors seen on the caps of mushrooms and in the petals of flowers. TYRs catalyze the ortho-hydroxylation and oxidation of phenols and the oxidation of catechols to the respective o-quinones. They only need molecular oxygen to do that, and the products of TYRs—o-quinones—are highly reactive and will usually react with the next available nucleophile. This reactivity can be harnessed for pharmaceutical applications as well as in environmental and food biotechnology. The majority of both basic and applied research on TYRs utilizes “mushroom tyrosinase”, a crude enzyme preparation derived from button mushroom (Agaricus bisporus) fruiting bodies. Access to pure TYR preparations comes almost exclusively from the production of recombinant TYRs as the purification of these enzymes from the natural source is usually very laborious and plagued by low yields. In this text an introduction into the biochemistry of the enzyme TYR will be given, followed by an overview of available structural data of TYRs, the current model for the catalytic mechanism, a survey of reports on the recombinant production of this important metalloenzyme family, and a review of the applications of TYRs for the synthesis of catechols, as biosensors, in bioremediation, for the cross-linking of proteins and medical hydrogels as well as for melanoma treatment. Graphical Abstract