This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the oxidation of o-diphenols (N-acetyldopamine, 4-methylcatechol and dopamine). Cannot oxidize monophenols and p-phenols (L-tyrosine, tyramine, gentisic acid and hydroquinone). Binds to the surface of hemocytes and is involved in hemocyte melanization. Activation of the enzyme in response to bacterial lipopolysaccharides (LPS) suggests it may play a role in innate immunity. Binds 2 copper ions per subunit. Dimer (PubMed:9085271). Might form a homodimer or a heterodimer with PPO1 (PubMed:9085271). Might interact with PPAF2 (via CLIP domain); the interaction might be required for PPO1 activity (PubMed:16362048). Secreted in the hemolymph. Hemocytes. Expressed in larvae (at protein level). Propeptide cleaved by PPAF1. Belongs to the tyrosinase family. The sequence was deposited erroneously as PPO2 (PubMed:12185078).