Isonitrile Formation by a Non-heme Iron(II)-Dependent Oxidase/Decarboxylase
Name
nihms-990873.pdf
Description
Accepted version
Size
512.56 KB
Format
Adobe PDF
Checksum (MD5)
7ddede5aac84c42a36ea438899cfd44b
Author(s)
Born, David A.
Drennan, Catherine L
Date Issued
July 2018
Journal
Angewandte Chemie - International Edition
Publisher
Wiley
Citation
Harris, Nicholas C. et al. “Isonitrile Formation by a Non-heme Iron(II)-Dependent Oxidase/Decarboxylase.” Angewandte Chemie - International Edition, vol. 57, no. 31, 2018, pp. 9707-9710 © 2018 The Author(s)
Version
Author's final manuscript
Abstract
The 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 herein 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, of which several members are critical for the virulence of pathogenic mycobacteria.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
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Creative Commons Attribution-Noncommercial-Share Alike
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DOI of Published Version
https://doi.org/10.1002/ANIE.201804307
