| Literature DB >> 15639092 |
Takashi Koyanagi1, Takane Katayama, Hideyuki Suzuki, Hidetsugu Nakazawa, Kenzo Yokozeki, Hidehiko Kumagai.
Abstract
The enzymatic production of 3,4-dihydroxyphenyl-L-alanine (L-DOPA) using Erwinia herbicola cells involves the action of tyrosine phenol-lyase (Tpl, EC 4.1.99.2). Since Tpl is only synthesized under L-tyrosine-induced conditions, the addition of L-tyrosine to the medium is unavoidable when preparing cells (the enzyme source), but severely impedes the pure preparation of the final product L-DOPA. We circumvented this problem by using recombinant E. herbicola cells carrying a mutant transcriptional regulator TyrR, which is capable of activating the tpl promoter in the absence of L-tyrosine.Entities:
Mesh:
Substances:
Year: 2005 PMID: 15639092 DOI: 10.1016/j.jbiotec.2004.08.016
Source DB: PubMed Journal: J Biotechnol ISSN: 0168-1656 Impact factor: 3.307