z-logo
Premium
Isonitrile Formation by a Non‐Heme Iron(II)‐Dependent Oxidase/Decarboxylase
Author(s) -
Harris Nicholas C.,
Born David A.,
Cai Wenlong,
Huang Yaobing,
Martin Joelle,
Khalaf Ryan,
Drennan Catherine L.,
Zhang Wenjun
Publication year - 2018
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201804307
Subject(s) - oxidative decarboxylation , chemistry , biosynthesis , decarboxylation , heme , enzyme , oxidase test , biochemistry , stereochemistry , amino acid , siderophore , streptomyces , catalysis , bacteria , gene , biology , genetics
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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here