Production of L-dihydroxyphenylalanine in Escherichia coli with the tyrosine phenol-lyase gene cloned from Erwinia herbicola.
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.
Foor
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Merck Research Laboratories, Rahway, New Jersey 07065.
Morin
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Bostian
K A
KA
D000595:Amino Acid Sequence; D001483:Base Sequence; D001709:Biotechnology; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D004885:Erwinia / Q000201:enzymology* / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism*; D005798:Genes, Bacterial; D007763:Lac Operon; D007980:Levodopa / Q000378:metabolism*; D008969:Molecular Sequence Data; D014443:Tyrosine / Q000378:metabolism; D014447:Tyrosine Phenol-Lyase / Q000235:genetics*
D004269:DNA, Bacterial; D014443:Tyrosine; D007980:Levodopa; D014447:Tyrosine Phenol-Lyase