ArticleJournal of industrial microbiology & biotechnology2019
Integrating enzyme evolution and high-throughput screening for efficient biosynthesis of L-DOPA.
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 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Heterologous expression of hydroxylase coupled with pathway optimization enables highly efficient ʟ-DOPA production inSynthetic and systems biotechnology · 2026Article
- Efficient synthesis of l-DOPA inSynthetic and systems biotechnology · 2026Article
- Highly Sensitive Detection of Tyrosine and Neurotransmitters by Stereoselective Biosynthesis and Photochemically Induced Dynamic Nuclear Polarization.Journal of the American Chemical Society · 2025Article
- Microbial engineering for monocyclic aromatic compounds production.FEMS microbiology reviews · 2025Review
- A computational strategy to improve the activity of tyrosine phenol-lyase for the synthesis of L-DOPA.Scientific reports · 2024Article
- Rapid production of l-DOPA by Vibrio natriegens, an emerging next-generation whole-cell catalysis chassis.Microbial biotechnology · 2022Article
- Advances in engineering microbial biosynthesis of aromatic compounds and related compounds.Bioresources and bioprocessing · 2021Review
- Active tyrosine phenol-lyase aggregates induced by terminally attached functional peptides in Escherichia coli.Journal of industrial microbiology & biotechnology · 2020Article
- Toward fine-tuned metabolic networks in industrial microorganisms.Synthetic and systems biotechnology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
L-DOPA is a key pharmaceutical agent for treating Parkinson's, and market demand has exploded due to the aging population. There are several challenges associated with the chemical synthesis of L-DOPA, including complicated operation, harsh conditions, and serious pollution. A biocatalysis route for L-DOPA production is promising, especially via a route catalyzed by tyrosine phenol lyase (TPL). In this study, using TPL derived from Erwinia herbicola (Eh-TPL), a mutant Eh-TPL was obtained by integrating enzyme evolution and high-throughput screening methods. L-DOPA production using recombinant Escherichia coli BL21 (DE3) cells harbouring mutant Eh-TPL was enhanced by 36.5% in shake flasks, and the temperature range and alkali resistance of the Eh-TPL mutant were promoted. Sequence analysis revealed two mutated amino acids in the mutant (S20C and N161S), which reduced the length of a hydrogen bond and generated new hydrogen bonds. Using a fed-batch mode for whole-cell catalysis in a 5 L bioreactor, the titre of L-DOPA reached 69.1 g L
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Registered trials
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