Tyrosine erwinia herbicola

L-tyrosine phenol + pyruvic acid + NH P-tyrosinase Erwinia herbicola ... 

A further industrially important lyase for the production of L-amino acids is the tyrosine phenol lyase [39]. This biocatalyst is used by Ajinomoto in the production of the pharmaceutically important L-3,4-dihydroxyphenylalanine (L-dopa), 32, which is applied in the treatment of Parkinson s disease. The reaction concept is based on a one-pot three-component synthesis starting from catechol, 30, pyruvic acid, 31, and ammonia in the presence of suspended whole cells (strain Erwinia herbicola) containing the tyrosine phenol lyase biocatalyst (Fig. 16). A key feature of this process is the high volumetric productivity of 110 g/L of the desired L-dopa product. Notably, this reaction runs with an annual capacity of 250 tons. 

Synthesis of L-Dopa Catalyzed by Tyrosine Phenol Lyase from Erwinia herbicola (E.C. 4.1.99.2)1100-1031... 

Japanese workers have described a novel microbiological synthesis of L-tyrosine and L-dopa from sodium pyruvate, ammonia and phenol or catechol respectively, using cells of Erwinia herbicola. The reaction is catalysed by tyrosine phenol lyase and is the reverse of the normal a)3-elimination reaction catalysed by this enzyme. The L-tyrosine or L-dopa synthesised by this enzymatic method precipitates from the reaction media during incubation. The maximum amount of L-tyrosine synthesised by this method was 60.5 g per litre and of L-dopa 58.5 g per litre. The process is a variation on the analogous procedure reported by the same school which used d L-serine in place of sodium pyruvate. 

Shibasaki T, Mori H, Chiba S, Ozaki A (1999) Microbial proline 4-hydroxylase screening and gene cloning. Appl Environ Microbiol 65 4028-4031 Suzuki H, l tayama T, Yamamoto K, Kumagai H (1995) Transcriptional r ula-tion of tyrosine phenol-lyase gene of Erwinia herbicola AJ2985. Biosci Biotechnol Biochem 59 2028—2032... 

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