To produce dopamine from catechol, pyruvate, and ammonia, an enzymatic process consisting of a two-step reaction, catechol --> L-DOPA --> dopamine, was developed. For the first reaction step to synthesize L-DOPA, tyrosine phenol-lyase of Symbiobacterium sp. SC-1 was used successfully as a biocatalyst, resulting in the high conversion yield of 92%. Two aromatic amino acid decarboxylases, rat liver L-DOPA decarboxylase and Streptoccus faecalis tyrosine decarboxylase (TDC), were tested for the subsequent step to produce dopamine. In investigating the effect of L-DOPA concentration, a serious substrate inhibition of L-DOPA decarboxylase activity was observed at concentrations over 1 mM, while no inhibition was detected for TDC up to 40 mM L-DOPA. Therefore, the TDC of S. faecalis was selected as the biocatalyst for the second reaction step. Enzymatic conversion of L-DOPA to dopamine was carried out in a reactor controlling the reaction pH with an HCl solution containing pyridoxal 5＇-phosphate, to compensate for the loss of pyridoxal 5＇-phosphate by an enzyme-catalyzed side reaction, i.e, decarboxylation-dependent transamination. When the enzyme reactor was operated at 37 degrees C for 12 h, 100 mM of L-DOPA was converted to dopamine with the conversion yield of 100%. Simultaneous reactions of tyrosine phenol-lyase and TDC were tested for direct synthesis of dopamine, but the productivity was much lower than the separated two-step reactions.