ArticleACS chemical biology2013
Tyrosine O-prenyltransferase SirD catalyzes S-, C-, and N-prenylations on tyrosine and tryptophan derivatives.
Article in ACS chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 44 citations in OpenAlex.
- Biosynthetic allene and alkyne formation by enzymatic prenyl demethylation.Nature chemical biology · 2026Article
- Biosynthetic allene and alkyne formation by enzymatic prenyl demethylation.bioRxiv : the preprint server for biology · 2026Article
- Artificial Gold Enzymes Using a Genetically Encoded Thiophenol-Based Noble-Metal-Binding Ligand.Angewandte Chemie (International ed. in English) · 2025Article
- Prenylation of aromatic amino acids and plant phenolics by an aromatic prenyltransferase from Rasamsonia emersonii.Applied microbiology and biotechnology · 2024Article
- Chemoenzymatic Late-Stage Modifications Enable Downstream Click-Mediated Fluorescent Tagging of Peptides.Angewandte Chemie (International ed. in English) · 2023Article
- Epipolythiodioxopiperazine-Based Natural Products: Building Blocks, Biosynthesis and Biological Activities.Chembiochem : a European journal of chemical biology · 2022Review
- Data Science-Driven Analysis of Substrate-Permissive Diketopiperazine Reverse Prenyltransferase NotF: Applications in Protein Engineering and Cascade Biocatalytic Synthesis of (-)-Eurotiumin A.Journal of the American Chemical Society · 2022Article
- Structural Basis of Substrate Promiscuity and Catalysis by the Reverse PrenyltransferaseBiochemistry · 2022Article
- Biosynthesis and trafficking of hemeCritical reviews in biochemistry and molecular biology · 2021Review
- Synthetic biology, combinatorial biosynthesis, and chemo‑enzymatic synthesis of isoprenoids.Journal of industrial microbiology & biotechnology · 2020Review
- 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
- Structure and specificity of a permissive bacterial C-prenyltransferase.Nature chemical biology · 2017Article
- Enzyme-Catalyzed Intramolecular Enantioselective Hydroalkoxylation.Journal of the American Chemical Society · 2017Article
- Insights into Thiol-Aromatic Interactions: A Stereoelectronic Basis for S-H/π Interactions.Journal of the American Chemical Society · 2017Article
- Sulfotyrosine dipeptide: Synthesis and evaluation as HIV-entry inhibitor.Bioorganic chemistry · 2016Article
- Site-directed mutagenesis switching a dimethylallyl tryptophan synthase to a specific tyrosine C3-prenylating enzyme.The Journal of biological chemistry · 2015Article
- Click chemistry in complex mixtures: bioorthogonal bioconjugation.Chemistry & biology · 2014Review
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2 authors at 1 institution in 1 country.
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Abstract
The tyrosine O-prenyltransferase SirD in Leptosphaeria maculans catalyzes normal prenylation of the hydroxyl group in tyrosine as the first committed step in the biosynthesis of the phytotoxin sirodesmin PL. SirD also catalyzes normal N-prenylation of 4-aminophenylalanine and normal C-prenylation at C7 of tryptophan. In this study, we found that 4-mercaptophenylalanine and several derivatives of tryptophan are also substrates for prenylation by dimethylallyl diphosphate. Incubation of SirD with 4-mercaptophenylalanine gave normal S-prenylated mercaptophenylalanine. We found that incubation of the enzyme with tryptophan gave reverse prenylation at N1 in addition to the previously reported normal prenylation at C7. 4-Methyltryptophan also gave normal prenylation at C7 and reverse prenylation at N1, whereas 4-methoxytryptophan gave normal and reverse prenylation at C7, and 7-methyltryptophan gave normal prenylation at C6 and reverse prenylation at N1. The ability of SirD to prenylate at three different sites on the indole nucleus, with normal and reverse prenylation at one of the sites, is similar to behavior seen for dimethylallyltryptophan synthase. The multiple products produced by SirD suggests it and dimethylallyltryptophan synthase use a dissociative electrophilic mechanism for alkylation of amino acid substrates.
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