Characteristics of phenol oxidase of Schistosoma mansoni and its functional implications in eggshell synthesis.

It is proposed that the phenol oxidase enzyme of schistosomes and other trematodes has a crucial role in the cross-linking of precursor proteins in the formation of the eggshell. However, to date there is no direct evidence to show that the enzyme catalyzes the reactions necessary for the posttranslational modification of eggshell precursor proteins. In this report we demonstrate that an eggshell precursor protein acts as a substrate for a schistosome fraction that catalyzed the 2 steps in the oxidation of tyrosine. This action of the phenol oxidase-containing worm fraction resulted in the tyrosine-dependent insolubilization and aggregation of the protein, suggesting a role for the enzyme in the posttranslational modification and cross-linking of schistosome eggshell proteins. The enzyme-rich fraction from Schistosoma mansoni catalyzed both steps of the reactions necessary for the conversion of tyrosine residues on putative eggshell precursor protein (p48) to quinones. The parasite fraction also catalyzed the hydroxylation of free L-tyrosine to DOPA (monophenol oxidase activity) and the oxidation of L-DOPA to dopaquinone (diphenol oxidase activity). Both activities of the enzyme are avidly bound to membranous structures, are susceptible to agents known to inhibit a functionally related enzyme, tyrosinase, and may reside on the same protein.