MAMMALIAN TYROSINASE CATALYZES 3 REACTIONS IN THE BIOSYNTHESIS OF MELANIN
MAMMALIAN TYROSINASE CATALYZES 3 REACTIONS IN THE BIOSYNTHESIS OF MELANIN
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DOI:
10.1126/science.6810464
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发表时间:
1982-01-01
期刊:
影响因子:
56.9
通讯作者:
PAWELEK, J
中科院分区:
文献类型:
--
作者:
KORNER, A;PAWELEK, J
The biosynthesis of melanin is initiated by the catalytic oxidation of tyrosine to dopa by tyrosinase in a reaction that requires dopa as a cofactor. Tyrosinase then catalyzes the dehydrogenation of dopa to dopaquinone. The subsequent reactions can proceed spontaneously in vitro. Tyrosinase, purified from murine melanomas and the skins of brown mice, catalyzes a 3rd reaction in mammalian melanogenesis, i.e., the conversion of 5,6-dihydroxyindole to melanochrome. This reaction requires dopa as a cofactor and is inhibited by tyrosine. 5,6-Dihydroxyindole inhibits the oxidation of tyrosine to dopa, so that the relative concentrations of tyrosine and 5,6-dihydroxyindole within the mammalian pigment cell are capable of regulating melanogenesis in a previously unrecognized fashion. Tyrosinase has the unusual property of catalyzing 3 distinct reactions within a single biochemical pathway: the hydroxylation of a monophenol, the dehydrogenation of a catechol and the dehydrogenation of a dihydroxyindole. The 1st and 3rd of these reactions require dopa as a cofactor; in the 2nd reaction, dopa is a substrate.