Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects.
The phenolic biopolymer eumelanin is an important skin pigment found throughout the animal kingdom. The enzyme, tyrosinase, initiates melanogenesis in mammals. The biogenesis is assisted by a number of mammalian protein factors including dopachrome tautomerase and 5,6-dihydroxyindole-2-carboxylate oxidase. Invertebrates, such as insects, employ phenoloxidase and dopachrome (decarboxylating) isomerase for melanin biosynthesis. Recently generated molecular biological and biochemical data indicate that tyrosinase and phenoloxidase are distinctly different enzymes in spite of possessing both monophenol monooxygenase activity as well as o-diphenoloxidase activity. Similarly, insect dopachrome isomerase also differs significantly from its mammalian counterpart in several of its properties including the nature of the enzymatic reaction. In addition, there are considerable differences in the eumelanogenic pathways of these two animal groups that include the utility of substrates, use of dihydroxyindoles and the nature of eumelanin pigment. Thus, the biochemistry and molecular biology of melanogenesis in mammals and insects are significantly different. The advantages of generating different eumelanin pigments and intermediates by the insects are discussed.
Sugumaran
Manickam
M
Department of Biology, University of Massachusetts, Boston, USA. manickam.sugumaran@umb.edu
D000595:Amino Acid Sequence; D000818:Animals; D007313:Insecta; D008543:Melanins / Q000096:biosynthesis* / Q000502:physiology*; D008969:Molecular Sequence Data; D014442:Monophenol Monooxygenase / Q000502:physiology*; D011498:Protein Precursors / Q000502:physiology
D008543:Melanins; D011498:Protein Precursors; C041877:eumelanin; D014442:Monophenol Monooxygenase