| Literature DB >> 19420686 |
Takashi Koyanagi1, Takane Katayama, Hideyuki Suzuki, Akiko Onishi, Kenzo Yokozeki, Hidehiko Kumagai.
Abstract
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.Entities:
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Year: 2009 PMID: 19420686 DOI: 10.1271/bbb.90019
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN: 0916-8451 Impact factor: 2.043