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A novel secreted aromatic amino acid decarboxylase-like molecule was identified in the excretory/secretory products of L3/L4 larvae as well as in an extract of adult  Dirofilaria immitis . The secretion of the enzyme was developmentally regulated. Peak enzyme activities were detected in the culture medium before and after the molting of L3 larvae  in vitro . The enzyme was purified from  D. immitis  adult extracts and the excretory/secretory products of L3/L4 larvae using different chromatographic methods followed by isoelectric focusing and SDS-PAGE. The enzyme has a molecular mass of 48 kDa and a pI of 5.6, and shows a specific enzymatic activity towards the aromatic amino acid substrates phenylalanine, tyrosine and tryptophan. The enzymes activity did not show an absolute requirement for exogenous pyridoxal-5-phosphate. However, addition of pyridoxal-5-phosphate at 5 μM in the reaction increased the enzyme activity greatly. The enzyme had the ability to catalyze the formation of dopamine from  L -dopa. Studies on the effects of inhibitors on the enzyme activity showed that the enzyme was sensitive to Pefabloc and  p -chloromercuribenzoic acid, but not to diisopropyl flurophosphate. The  K  m  values of the enzyme for H-Phe-AMC, H-Tyr-AMC and H-Trp-AMC were calculated to be 32.1 μM, 35.1 μM and 29.1 μM, respectively.

Identification and Characterization of an Aromatic Amino Acid Decarboxylase from the Filarial Nematode, Dirofilaria immitis