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
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Research Support, Non-U.S. Gov't
MeSH terms
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Erwinia / genetics*
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Erwinia / metabolism*
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Escherichia coli Proteins / genetics*
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Escherichia coli Proteins / metabolism*
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Genetic Enhancement / methods*
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Levodopa / biosynthesis*
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Levodopa / genetics
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Mutagenesis, Site-Directed
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Protein Engineering / methods
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Recombinant Proteins / metabolism
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Repressor Proteins / genetics*
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Repressor Proteins / metabolism*
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Transcriptional Activation / genetics
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Tyrosine Phenol-Lyase / genetics
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Tyrosine Phenol-Lyase / metabolism*
Substances
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Escherichia coli Proteins
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Recombinant Proteins
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Repressor Proteins
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TyrR protein, E coli
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Levodopa
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Tyrosine Phenol-Lyase