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Tyrosinase is a copper-containing oxidase that serves as the rate-limiting enzyme in the biosynthesis of melanin, the pigment responsible for the color of skin, hair, and eyes [2, 8]. It catalyzes the hydroxylation of L-tyrosine to L-DOPA and the subsequent oxidation of L-DOPA to dopaquinone, which then polymerizes into eumelanin or pheomelanin [12, 15]. In mice, the tyrosinase gene (Tyr) is located at the albino locus, and mutations in this gene result in various forms of oculocutaneous albinism, such as the classic albino phenotype [4, 10]. Murine tyrosinase is a critical target in dermatological research for developing skin-lightening agents and in oncology as a tumor-associated antigen for melanoma immunotherapy [11, 14]. Because it is highly expressed in melanocytes and melanoma cells, it is used as a biomarker for disease progression and a target for enzyme-activated prodrugs [13, 16]. Therapeutic interventions include competitive inhibitors like hydroquinone and kojic acid to treat hyperpigmentation, as well as experimental vaccines designed to elicit an immune response against tyrosinase-expressing cancer cells [1, 6].
Competitive inhibition of the active site, suicide inactivation, or copper chelation to prevent the conversion of L-tyrosine and L-DOPA into melanin precursors [1, 3, 5].
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