Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 73, Issue 5, Pages 1221-1223Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.90019
Keywords
3,4-dihydroxyphenyl-L-alanine (L-dopa); transcriptional regulator TyrR; tyrosine phenol-lyase
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [18780060]
- Ministry of Education, Culture, Sports, Science, and Technology
- Grants-in-Aid for Scientific Research [18780060] Funding Source: KAKEN
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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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