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Appl Environ Microbiol. 1993 September; 59(9): 3070-3075

Production of L-dihydroxyphenylalanine in Escherichia coli with the tyrosine phenol-lyase gene cloned from Erwinia herbicola.

F Foor, N Morin and K A Bostian

Merck Research Laboratories, Rahway, New Jersey 07065.

ABSTRACT

The gene (tutA) encoding tyrosine phenol-lyase from Erwinia herbicola was cloned into Escherichia coli, and fusions to the lac and tac promoters were constructed. The enzyme was expressed at high levels in E. coli in the presence of isopropyl-beta-D-thiogalactopyranoside or lactose as an inducer. L-Dihydroxyphenylalanine was synthesized in high yield from catechol, pyruvate, and ammonia by induced cells.

Appl Environ Microbiol. 1993 September; 59(9): 3070-3075




This article has been cited by other articles:

  • Katayama, T., Suzuki, H., Koyanagi, T., Kumagai, H. (2002). Functional Analysis of the Erwinia herbicola tutB Gene and Its Product. J. Bacteriol. 184: 3135-3141 [Abstract] [Full Text]  
  • Katayama, T., Suzuki, H., Koyanagi, T., Kumagai, H. (2000). Cloning and Random Mutagenesis of the Erwinia herbicola tyrR Gene for High-Level Expression of Tyrosine Phenol-Lyase. Appl. Environ. Microbiol. 66: 4764-4771 [Abstract] [Full Text]  
  • Bai, Q., Somerville, R. L. (1998). Integration Host Factor and Cyclic AMP Receptor Protein Are Required for TyrR-Mediated Activation of tpl in Citrobacter freundii. J. Bacteriol. 180: 6173-6186 [Abstract] [Full Text]  


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