Abstract
The pathways involved in tyrosine metabolism in insects are complex. Tyrosine serves as the precursor for melanin, sclerotin and the neuroactive catecholamines, dopamine and noradrenalin (see Fig. 1). Early workers (Ohnishi, 1954; Horowitz and Fling, 1955) demonstrated that fresh tissue extracts of Drosophila contained no measurable tyrosinase activity but following a time lag (during which the extract is maintained at O°C) tyrosinase activity develops. Horowitz and Fling (1955) noted that the kinetics of this activation process followed a sigmoid curve and suggested a modified autocata-lytic mechanism for activation. Electrophoretic analysis of the tyrosinase (phenol oxidase) system, (Mitchell and Weber, 1965) revealed the presence of three isozymes, A1, A2 and A3. These were present as proenzymes and required activation by a component, P, found in pupal extracts. A1 was predominantly a monophenol oxidase, reacting most strongly with tyrosinase whereas A2 and A3 showed diphenol oxidase activity reacting strongly with dopa and N-acetyldopamine. Mitchell et al. (1967) demonstrated that several discrete enzymes were involved in the activation process and Seybold et al. (1975) provided evidence that at least six structural genes are required for the production of phenol oxidase activity in Drosophila extracts.
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© 1982 Plenum Press, New York
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Burnell, A.M., Daly, B.A. (1982). Spontaneous Locomotor Activity and Dopamine Levels in Tyr-1 Mutants of Drosophila Melanogaster. In: Lakovaara, S. (eds) Advances in Genetics, Development, and Evolution of Drosophila. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-8321-9_32
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DOI: https://doi.org/10.1007/978-1-4615-8321-9_32
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