Hyperproduction of 3,4-dihydroxyphenyl-L-alanine (L-Dopa) using Erwinia herbicola cells carrying a mutant transcriptional regulator TyrR.
In the last few decades, enzymatic production of 3,4-dihydroxyphenyl-L-alanine (L-dopa) using tyrosine phenol-lyase (Tpl) has been industrialized. This method has an intrinsic problem of tyrosine contamination because Tpl is synthesized under tyrosine-induced conditions. Herein, we constructed a hyper-L-dopa-producing strain by exploiting a mutant TyrR, an activator of tpl. The highest productivity was obtained for the strain grown under non-induced conditions. It was 30-fold higher than that obtained for tyrosine-induced wild-type cells.
Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Ishikawa, Japan.
Takashi
T
Koyanagi
Takane
T
Katayama
Hideyuki
H
Suzuki
Akiko
A
Onishi
Kenzo
K
Yokozeki
Hidehiko
H
Kumagai
D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism*; D004885:Erwinia / Q000166:cytology* / Q000378:metabolism*; D007980:Levodopa / Q000096:biosynthesis*; D050505:Mutant Proteins / Q000235:genetics* / Q000378:metabolism*; D009154:Mutation
D001426:Bacterial Proteins; D050505:Mutant Proteins; D007980:Levodopa