Issue 9, 2016

Conversion of a non-heme iron-dependent sulfoxide synthase into a thiol dioxygenase by a single point mutation

Abstract

EgtB from Mycobacterium thermoresistibile catalyzes O2-dependent sulfur–carbon bond formation between the side chains of Nα-trimethyl histidine and γ-glutamyl cysteine as a central step in ergothioneine biosynthesis. A single point mutation converts this enzyme into a γ-glutamyl cysteine dioxygenase with an efficiency that rivals naturally evolved thiol dioxygenases.

Graphical abstract: Conversion of a non-heme iron-dependent sulfoxide synthase into a thiol dioxygenase by a single point mutation

Supplementary files

Article information

Article type
Communication
Submitted
16 Sep 2015
Accepted
02 Dec 2015
First published
14 Dec 2015
This article is Open Access
Creative Commons BY license

Chem. Commun., 2016,52, 1945-1948

Author version available

Conversion of a non-heme iron-dependent sulfoxide synthase into a thiol dioxygenase by a single point mutation

K. V. Goncharenko and F. P. Seebeck, Chem. Commun., 2016, 52, 1945 DOI: 10.1039/C5CC07772A

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