This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds (By similarity). Catalyzes the oxidation of o-diphenols (N-acetyldopamine, 4-methylcatechol and dopamine) (PubMed:12185078, PubMed:9085271, PubMed:16362048). Cannot oxidize monophenols and p-phenols (L-tyrosine, tyramine, gentisic acid and hydroquinone) (PubMed:9085271). Binds to the surface of hemocytes and is involved in hemocyte melanization (By similarity). Activation of the enzyme in response to bacterial lipopolysaccharides (LPS) suggests it may play a role in innate immunity (PubMed:9839951). Binds 2 copper ions per subunit. Optimum pH is 8.0. Optimum temperature is 35 degrees Celsius. 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 PPO2 activity (PubMed:16362048). Secreted in the hemolymph. Hemocytes. Expressed in larvae (at protein level). Precursor cleaved by PPAF1. Belongs to the tyrosinase family. The sequence was deposited erroneously as PPO1 (PubMed:12185078).