ArticleChembiochem : a European journal of chemical biology2019
Facile in Vitro Biocatalytic Production of Diverse Tryptamines.
Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed.
- Promiscuity-Guided Enzyme Evolution via Substrate Multiplexed Screening.Angewandte Chemie (International ed. in English) · 2026Review
- Continuous evolution of a halogenase enzyme with improved solubility and activity for sustainable bioproduction.Nature communications · 2026Article
- Sequence-based generative AI design of versatile tryptophan synthases.Nature communications · 2026Article
- Theranostic Probiotic Engineered Living Materials That Dynamically Respond to Inflammation Markers.Advanced healthcare materials · 2026Article
- Active site diversification of a non-canonical amino acid decarboxylase by merging substrate multiplexed screening with computationally guided recombination.Protein science : a publication of the Protein Society · 2025Article
- Biosynthetic Origin of the Methoxy Group in Quinine and Related Alkaloids.Angewandte Chemie (International ed. in English) · 2025Article
- A modular and synthetic biosynthesis platform for de novo production of diverse halogenated tryptophan-derived molecules.Nature communications · 2024Article
- Biosynthesis of natural and halogenated plant monoterpene indole alkaloids in yeast.Nature chemical biology · 2023Article
- Article
- Biocatalytic Friedel-Crafts Reactions.ChemCatChem · 2022Review
- Substrate multiplexed protein engineering facilitates promiscuous biocatalytic synthesis.Nature communications · 2022Article
- Investigation of β-Substitution Activity of O-Acetylserine Sulfhydrolase from Citrullus vulgaris.Chembiochem : a European journal of chemical biology · 2022Article
- Aromatic L-amino acid decarboxylases: mechanistic features and microbial applications.Applied microbiology and biotechnology · 2022Review
- Functional characterization of a catalytically promiscuous tryptophan decarboxylase from camptothecin-producingFrontiers in plant science · 2022Article
- Biochemical characterization and synthetic application of aromatic L-amino acid decarboxylase from Bacillus atrophaeus.Applied microbiology and biotechnology · 2021Article
- Tryptophan Synthase: Biocatalyst Extraordinaire.Chembiochem : a European journal of chemical biology · 2021Review
- Deploying Microbial Synthesis for Halogenating and Diversifying Medicinal Alkaloid Scaffolds.Frontiers in bioengineering and biotechnology · 2020Review
- Overview on Multienzymatic Cascades for the Production of Non-canonical α-Amino Acids.Frontiers in bioengineering and biotechnology · 2020Review
- Evaluation of TrpM and PsiD substrate promiscuity reveals new biocatalytic capabilities.Biotechnology progressArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Tryptamines are a medicinally important class of small molecules that serve as precursors to more complex, clinically used indole alkaloid natural products. Typically, tryptamine analogues are prepared from indoles through multistep synthetic routes. In the natural world, the desirable tryptamine synthon is produced in a single step by l-tryptophan decarboxylases (TDCs). However, no TDCs are known to combine high activity and substrate promiscuity, which might enable a practical biocatalytic route to tryptamine analogues. We have now identified the TDC from Ruminococcus gnavus as the first highly active and promiscuous member of this enzyme family. RgnTDC performs up to 96 000 turnovers and readily accommodates tryptophan analogues with substituents at the 4, 5, 6, and 7 positions, as well as alternative heterocycles, thus enabling the facile biocatalytic synthesis of >20 tryptamine analogues. We demonstrate the utility of this enzyme in a two-step biocatalytic sequence with an engineered tryptophan synthase to afford an efficient, cost-effective route to tryptamines from commercially available indole starting materials.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.