The critical review describes the known dicopper systems mediating the aromatic
hydroxylation of monophenolic substrates. Such systems are of interest as structural and …

Tyrosinases are metalloenzymes belonging to the type‐3 copper protein family which
contain two copper ions in the active site. They are found in various prokaryotes as well as in …

Tyrosinase is responsible for the two initial enzymatic steps in the conversion of tyrosine to
melanin. Many tyrosinase mutations are the leading cause of albinism in humans, and it is a …

Tyrosinases are responsible for melanin formation in all life domains. Tyrosinase inhibitors
are used for the prevention of severe skin diseases, in skin-whitening creams and to avoid …

Tyrosinases and catechol oxidases belong to the family of polyphenol oxidases (PPOs).
Tyrosinases catalyze the o-hydroxylation and oxidation of phenolic compounds, whereas …

The ubiquitous type-3 copper enzyme polyphenol oxidase (PPO) has found itself the subject
of profound inhibitor research due to its role in fruit and vegetable browning and mammalian …

The structural difference between tyrosinase and catechol oxidase as the basis for their
catalytic activity is still a puzzle although several crystal structures of both enzymes exist. In …

Tyrosinase (EC 1.14. 18.1), a copper-containing monooxygenase, catalyzes the conversion
of phenol to the corresponding ortho-quinone. The Streptomyces tyrosinase is generated as …

Tyrosinase is a copper-binding enzyme involved in melanin biosynthesis. However, the
detailed structure of human tyrosinase has not yet been solved, along with the identification …

Tyrosinase, a widely spread enzyme in micro-organisms, animals, and plants, participates in
two rate-limiting steps in melanin formation pathway which is responsible for skin protection …