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A single diiron enzyme catalyses the oxidative rearrangement of tryptophan to indole nitrile
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A single diiron enzyme catalyses the oxidative rearrangement of tryptophan to indole nitrile
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Journal Article
A single diiron enzyme catalyses the oxidative rearrangement of tryptophan to indole nitrile
2024
Overview
Nitriles are uncommon in nature and are typically constructed from oximes through the oxidative decarboxylation of amino acid substrates or from the derivatization of carboxylic acids. Here we report a third nitrile biosynthesis strategy featuring the cyanobacterial nitrile synthase AetD. During the biosynthesis of the eagle-killing neurotoxin, aetokthonotoxin, AetD transforms the 2-aminopropionate portion of 5,7-dibromo-
l
-tryptophan to a nitrile. Employing a combination of structural, biochemical and biophysical techniques, we characterized AetD as a non-haem diiron enzyme that belongs to the emerging haem-oxygenase-like dimetal oxidase superfamily. High-resolution crystal structures of AetD together with the identification of catalytically relevant products provide mechanistic insights into how AetD affords this unique transformation, which we propose proceeds via an aziridine intermediate. Our work presents a unique template for nitrile biogenesis and portrays a substrate binding and metallocofactor assembly mechanism that may be shared among other haem-oxygenase-like dimetal oxidase enzymes.
Nitrile-containing molecules and their biosynthetic enzymes are uncommon in nature. Now, a nitrile-forming diiron enzyme involved in the biosynthesis of aetokthonotoxin—the ‘eagle-killing’ neurotoxin—has been characterized using biochemical, structural and biophysical methods. High-resolution protein crystal structures together with the identification of catalytically relevant tryptophan-based products provide mechanistic insights into this unusual nitrile-forming reaction.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
