Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor. an aralkylamine + H2O + 2 oxidized [azurin] = an aromatic aldehyde + 2 H(+) + NH4(+) + 2 reduced [azurin] Uses a protein-derived tryptophan tryptophylquinone (TTQ) cofactor. Irreversibly inhibited by phenylhydrazine, hydroxylamine, semicarbazide, hydrazine and aminoguanidine. Reversibly inhibited by isonicotinic acid hydrazide (isoniazid) and isonicotinic acid 2-isopropyl hydrazide (iproniazid). The above maximum is for the oxidized form. Shows a maximal peak at 330 nm in the reduced form. These absorption peaks are for the tryptophylquinone cofactor. The enzyme is substrate inhibited at high substrate concentrations (Ki=1.08 mM for tyramine). Heterotetramer of two light and two heavy chains. Binds two azurin molecules per heterotetramer. Tryptophan tryptophylquinone (TTQ) is formed by oxidation of the indole ring of a tryptophan to form tryptophylquinone followed by covalent cross-linking with another tryptophan residue. Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. Belongs to the aromatic amine dehydrogenase light chain family.