6l86
The structure of SfaAThe structure of SfaA
Structural highlights
FunctionPublication Abstract from PubMedN-alkylisonitrile, a precursor to isonitrile-containing lipopeptides, is biosynthesized via decarboxylation-assisted -N identical withC group (isonitrile) formation by using N-alkylglycine as the substrate. This reaction is catalyzed by iron(II) and 2-oxoglutarate (Fe/2OG) dependent enzymes. Distinct from typical oxygenation or halogenation reactions catalyzed by this class of enzymes, installation of the isonitrile group represents a novel reaction type for Fe/2OG enzymes that involves a four-electron oxidative process. Here we report the plausible mechanism of three Fe/2OG enzymes, Sav607, ScoE and SfaA, catalyzed isonitrile formation. The X-ray structures of iron loaded ScoE in complex with its substrate and the intermediate, along with biochemical and biophysical data reveal that -N identical withC bond formation involves two cycles of Fe/2OG enzyme catalysis. The reaction starts with an Fe(IV)-oxo catalyzed hydroxylation. It is likely followed by decarboxylation-assisted desaturation to complete isonitrile installation. Pathway from N-alkylglycine to alkylisonitrile catalyzed by iron(II) and 2-oxoglutarate dependent oxygenases.,Chang WC, Chen TY, Chen J, Tang Y, Zhou J, Guo Y Angew Chem Int Ed Engl. 2020 Feb 19. doi: 10.1002/anie.201914896. PMID:32074393[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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