Abstract
A tyrosinase, enzyme A, and a laccase, enzyme B, have been partially purified from larval cuticle of the flesh fly Sarcophaga bullata. Enzyme A (EC 1.10.3.1, o-diphenol: O2 oxidoreductase) oxidizes o-diphenols but not p-diphenols, is strongly inhibited by phenylthiourea, and has a pH optimum around pH 6.5–7.0. Assays on intact cuticle suggest that it becomes maximally activated at pH between 8 and 9. Enzyme B (EC 1.10.3.2, p-diphenol: O2 oxidoreductase) oxidizes both o-diphenols and p-diphenols, is not inhibited by phenylthiourea but is inhibited by concentrations of sodium azide that have little effect on enzyme A, and has a pH optimum near pH 4.5. Enzyme A was identified in extracts of cuticle from nine other species representing five orders. Enzyme B was much less readily extractable but was partially purified from larval cuticle of Phormia regina, Musca domestica, and Lucilia sericata. A summary of all species studied to date makes possible the test of a hypothesis about the distribution of these cuticular phenoloxidases within the Insecta.
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