ArticleJournal of the American Chemical Society2025
Single-Enzyme Conversion of Tryptophan to Skatole and Cyanide Expands the Mechanistic Competence of Diiron Oxidases.
Article in Journal of the American Chemical Society, 2025. 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.
- Recent discoveries in mono- and dinuclear nonheme iron enzymes: Emerging mechanisms and catalytic strategies.Archives of biochemistry and biophysics · 2026Review
- Discovery of a Structurally Distinct Acetylenase in the Biosynthesis of Mangotoxin.Journal of the American Chemical Society · 2026Article
- Crystal structure of RohS, a heme-oxygenase-like N-oxygenase from azomycin biosynthesis.The Journal of biological chemistry · 2026Article
- Heme oxygenase-like dimetal oxidases and oxygenases.Biochemical Society transactions · 2026Review
- Microbial unusual gene clusters without prominent core enzymes: natural products, biosynthesis and genome mining.The Journal of antibiotics · 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
- 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
- Metagenomic Identification of Brominated Indole Biosynthetic Machinery from Cyanobacteria.Journal of natural products · 2025Article
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Authors and funding
5 authors.
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Abstract
Skatole is a pungent heterocyclic compound derived from the essential amino acid l-tryptophan by bacteria in the mammalian digestive tract. The four-step anaerobic conversion of tryptophan to skatole is well-established; though, to date, no aerobic counterpart has been reported. Herein, we report the discovery of the oxygen-dependent skatole synthase SktA that single-handedly converts 5-bromo-l-tryptophan to 5-bromoskatole, obviating the need for a multienzyme process. SktA is part of a three-gene biosynthetic gene cluster (BGC) in the cyanobacterium
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