6dch
From Proteopedia
Structure of isonitrile biosynthesis enzyme ScoE
Structural highlights
FunctionPublication Abstract from PubMedThe electron-rich isonitrile is an important functionality in bioactive natural products, but its biosynthesis has been restricted to the IsnA family of isonitrile synthases. We here provide the first structural and biochemical evidence of an alternative mechanism for isonitrile formation. ScoE, a putative non-heme iron(II)-dependent enzyme from Streptomyces coeruleorubidus, was shown to catalyze the conversion of (R)-3-((carboxymethyl)amino)butanoic acid to (R)-3-isocyanobutanoic acid through an oxidative decarboxylation mechanism. This work further provides a revised scheme for the biosynthesis of a unique class of isonitrile lipopeptides, members of which are critical for the virulence of pathogenic mycobacteria. Isonitrile Formation by a Non-heme Iron(II)-Dependent Oxidase/Decarboxylase.,Harris N, Born D, Cai W, Huang Y, Martin J, Khalaf R, Drennan C, Zhang W Angew Chem Int Ed Engl. 2018 Jun 15. doi: 10.1002/anie.201804307. PMID:29906336[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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