Hyperproduction of 3,4-Dihydroxyphenyl-L-alanine (L-Dopa) UsingErwinia herbicolaCells Carrying a Mutant Transcriptional Regulator TyrR | Zendy

Takashi Koyanagi | Zendy; Takane Katayama | Zendy; Hideyuki Suzuki | Zendy; Akiko Onishi | Zendy; Kenzo Yokozeki | Zendy; Hidehiko Kumagai | Zendy

Open Access

Hyperproduction of 3,4-Dihydroxyphenyl-L-alanine (L-Dopa) UsingErwinia herbicolaCells Carrying a Mutant Transcriptional Regulator TyrR

Author(s) -

Takashi Koyanagi,

Takane Katayama,

Hideyuki Suzuki,

Akiko Onishi,

Kenzo Yokozeki,

Hidehiko Kumagai

Publication year - 2009

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.90019

Subject(s) - mutant , tyrosine , regulator , activator (genetics) , biochemistry , enzyme , chemistry , protein tyrosine phosphatase , alanine , biology , microbiology and biotechnology , amino acid , gene

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.

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