The current melanin biosynthesis pathway is described as the Raper-Mason pathway.
Images (1)
Raper-Mason-pathway
DefinitionThis section has been translated automatically.
General informationThis section has been translated automatically.
The current understanding of melanin is based on the generally accepted biosynthetic pathway for polymerization, the Raper-Mason pathway (RMP), which was first published in 1948. The pathway describes the stepwise evolution of melanin from the essential amino acid L-tyrosine via dopaquinone to dihydroxyindole (DHI) or dihydroxyindolecarboxylic acid (DHICA). These units are then oxidized to form indole-5,6-quinone-2-carboxylic acid (IQCA) or indole-5,6-quinone (IQ), the immediate precursors for polymerization. In addition to the various structural complexities, melanogenesis processes in vivo are regulated by a number of enzymes, including tyrosinases and decarboxylases, which link the oxidative and decarboxylative steps.
LiteratureThis section has been translated automatically.
- Casanola-Martin GM et al. (2014) Tyrosinase enzyme M. R. 1. An overview on a pharmacological target. Curr Top Med Chem 14:1494-1501.
- Mason HS (1948) The chemistry of melanin; mechanism of the oxidation of dihydroxyphenylalanine by tyrosinase. J Biol Chem 172:83-99.
Ni QZ et al. (2020) Chemoenzymatic elaboration of the Raper-Mason pathway unravels the structural diversity within eumelanin pigments. Chem Sci 11:7836-7841.
- Raper H S (1928) The Aerobic Oxidases. Physiol Rev 8:245-282.