ArticleJournal of industrial microbiology & biotechnology2019
Redox self-sufficient biocatalyst system for conversion of 3,4-Dihydroxyphenyl-L-alanine into (R)- or (S)-3,4-Dihydroxyphenyllactic acid.
Article in Journal of industrial microbiology & biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- Transaminases engineering and their cascade systems for natural product synthesis.Applied biochemistry and biotechnology · 2026Review
- Self-sufficient biocatalytic cascade for the continuous synthesis of danshensu in flow.Applied microbiology and biotechnology · 2025Article
- Multienzyme cascade for synthesis of hydroxytyrosol via engineered Escherichia coli.Scientific reports · 2025Article
- Efficient production of salvianic acid A from L-dihydroxyphenylalanine through a tri-enzyme cascade.Bioresources and bioprocessing · 2023Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
We developed an efficient multi-enzyme cascade reaction to produce (R)- or (S)-3,4-Dihydroxyphenyllactic acid [(R)- or (S)-Danshensu, (R)- or (S)-DSS] from 3,4-Dihydroxyphenyl-L-alanine (L-DOPA) in Escherichia coli by introducing tyrosine aminotransferase (tyrB), glutamate dehydrogenase (cdgdh) and D-aromatic lactate dehydrogenase (csldhD) or L-aromatic lactate dehydrogenase (tcldhL). First, the genes in the pathway were overexpressed and fine-tuned for (R)- or (S)-DSS production. The resulting strain, E. coli TGL 2.1 and E. coli TGL 2.2, which overexpressed tyrB with the stronger T7 promoter and cdgdh, csldhD or tcldhL with the weaker Trc promoter, E. coli TGL 2.1 yielded 57% increase in (R)-DSS production: 59.8 ± 2.9 mM. Meanwhile, E. coli TGL 2.2 yielded 54% increase in (S)-DSS production: 52.2 ± 2.4 mM. The optimal concentration of L-glutamate was found to be 20 mM for production of (R)- or (S)-DSS. Finally, L-DOPA were transformed into (R)- or (S)-DSS with an excellent enantiopure form (enantiomeric excess > 99.99%) and productivity of 6.61 mM/h and 4.48 mM/h, respectively.
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