Development of an enzymatic system for the production of dopamine from catechol, pyruvate, and ammonia

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Title
Development of an enzymatic system for the production of dopamine from catechol, pyruvate, and ammonia
Author(s)
Seung Goo Lee; Seung Pyo Hong; Moon Hee Sung
Bibliographic Citation
Enzyme and Microbial Technology, vol. 25, pp. 298-302
Publication Year
1999
Abstract
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°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.
Keyword
DopamineTyrosine phenol-lyaseTyrosine decarboxylaseSymbiobacteriumStreptococcus faecalis
ISSN
0141-0229
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/S0141-0229(99)00071-X
Type
Article
Appears in Collections:
Synthetic Biology and Bioengineering Research Institute > 1. Journal Articles
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