ArticleMedChemComm2019
FgaPT2, a biocatalytic tool for alkyl-diversification of indole natural products.
Article in MedChemComm, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Promiscuity of an Alcohol-Dependent Hemiterpene Pathway for the In Vivo Production of a Non-Natural Alkylated Tryptophan Derivative.ACS synthetic biology · 2025Article
- Substrate-Multiplexed Assessment of Aromatic Prenyltransferase Activity.Chembiochem : a European journal of chemical biology · 2025Article
- The utility of Streptococcus mutans undecaprenol kinase for the chemoenzymatic synthesis of diverse non-natural isoprenoids.Bioorganic chemistry · 2024Article
- Unlocking New Prenylation Modes: Azaindoles as a New Substrate Class for Indole Prenyltransferases.ChemCatChem · 2023Article
- Chemoenzymatic Late-Stage Modifications Enable Downstream Click-Mediated Fluorescent Tagging of Peptides.Angewandte Chemie (International ed. in English) · 2023Article
- Regioselective Biocatalytic C4-Prenylation of Unprotected Tryptophan Derivatives.Chembiochem : a European journal of chemical biology · 2022Article
- Article
- Novel Homologs of Isopentenyl Phosphate Kinase Reveal Class-Wide Substrate Flexibility.ChemCatChem · 2021Article
- Indole C6 Functionalization of Tryprostatin B Using Prenyltransferase CdpNPT.Catalysts (Basel, Switzerland) · 2020Article
- Synthetic biology, combinatorial biosynthesis, and chemo‑enzymatic synthesis of isoprenoids.Journal of industrial microbiology & biotechnology · 2020Review
- Chemoenzymatic synthesis of daptomycin analogs active against daptomycin-resistant strains.Applied microbiology and biotechnology · 2020Article
- Broadening the scope of biocatalytic C-C bond formation.Nature reviews. Chemistry · 2020Article
- Enzymatic studies on aromatic prenyltransferases.Journal of natural medicines · 2020Review
- Acceptor substrate determines donor specificity of an aromatic prenyltransferase: expanding the biocatalytic potential of NphB.Applied microbiology and biotechnology · 2020Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Aromatic prenyltransferases from natural product biosynthetic pathways display relaxed specificity for their aromatic substrates. While a growing body of evidence suggests aromatic prenyltransferases to be more tolerant towards their alkyl-donor substrates, most studies aimed at probing their donor-substrate specificity are limited to only a small set of alkyl pyrophosphate donors, restricting their broader utility as biocatalysts for synthetic applications. Here, we assess the donor substrate specificity of an l-tryptophan C4-prenyltransferase, also known as C4-dimethylallyltryptophan synthase, FgaPT2 from
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Registered trials
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