ArticleNature communications2023
The structural and functional investigation into an unusual nitrile synthase.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed.
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- Discovery of a Structurally Distinct Acetylenase in the Biosynthesis of Mangotoxin.Journal of the American Chemical Society · 2026Article
- Heme oxygenase-like dimetal oxidases and oxygenases.Biochemical Society transactions · 2026Review
- A two-metalloenzyme cascade constructs the azetidine-containing pharmacophore.Nature chemistry · 2026Article
- Azetidine amino acid biosynthesis by non-haem iron-dependent enzymes.Nature chemistry · 2026Article
- Discovery and Mechanism of a Diiron Enzyme in Ethylidene Azetidine Formation.Journal of the American Chemical Society · 2025Article
- Structural basis of a 2-oxoglutarate-dependent heme-oxygenase-like enzyme HamA in fragin biosynthesis.RSC advances · 2025Article
- The Heme Oxygenase-Like Diiron Enzyme HrmI Reveals Altered Regulatory Mechanisms for Dioxygen Activation and Substrate N-Oxygenation.Journal of the American Chemical Society · 2025Article
- Mining for Halogenated Metabolites ofJournal of natural products · 2025Article
- Heme Oxygenase-Like Metalloenzymes.Annual review of biochemistry · 2025Review
- Biochemical characterization of the self-sacrificing p-aminobenzoate synthase from Nitrosomonas europaea reveals key residues involved in selecting a Fe/Fe or Mn/Fe cofactor.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Copper-chelating natural products.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- Mechanistic Perspective on C-N and C-S Bond Construction Catalyzed by Cytochrome P450 Enzymes.ACS bio & med chem Au · 2025Review
- A single diiron enzyme catalyses the oxidative rearrangement of tryptophan to indole nitrile.Nature chemistry · 2024Article
- Assembly of a Heterobimetallic Fe/Mn Cofactor in theBiochemistry · 2024Article
- Structural Basis for Methine Excision by a Heme Oxygenase-like Enzyme.ACS central science · 2024Article
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12 authors.
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Abstract
The biosynthesis of neurotoxin aetokthonotoxin (AETX) that features a unique structure of pentabrominated biindole nitrile involves a first-of-its-kind nitrile synthase termed AetD, an enzyme that shares very low sequence identity to known structures and catalyzes an unprecedented mechanism. In this study, we resolve the crystal structure of AetD in complex with the substrate 5,7-di-Br-L-Trp. AetD adopts the heme oxygenase like fold and forms a hydrophobic cavity within a helical bundle to accommodate the indole moiety. A diiron cluster comprising two irons that serves as a catalytic center binds to the carboxyl O and the amino N of the substrate. Notably, we demonstrate that the AetD-catalyzed reaction is independent of the bromination of the substrate and also solved crystal structures of AetD in complex with 5-Br-L-Trp and L-Trp. Altogether, the present study reveals the substrate-binding pattern and validates the diiron cluster-comprising active center of AetD, which should provide important basis to support the mechanistic investigations into this class of nitrile synthase.
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