Effective production of 3,4-dihydroxyphenyl-L-alanine (L-DOPA) with Erwinia herbicola cells carrying a mutant transcriptional regulator TyrR

J Biotechnol. 2005 Feb 9;115(3):303-6. doi: 10.1016/j.jbiotec.2004.08.016.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Erwinia / genetics*
  • Erwinia / metabolism*
  • Escherichia coli Proteins / genetics*
  • Escherichia coli Proteins / metabolism*
  • Genetic Enhancement / methods*
  • Levodopa / biosynthesis*
  • Levodopa / genetics
  • Mutagenesis, Site-Directed
  • Protein Engineering / methods
  • Recombinant Proteins / metabolism
  • Repressor Proteins / genetics*
  • Repressor Proteins / metabolism*
  • Transcriptional Activation / genetics
  • Tyrosine Phenol-Lyase / genetics
  • Tyrosine Phenol-Lyase / metabolism*

Substances

  • Escherichia coli Proteins
  • Recombinant Proteins
  • Repressor Proteins
  • TyrR protein, E coli
  • Levodopa
  • Tyrosine Phenol-Lyase