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Issue 9, 2016
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Conversion of a non-heme iron-dependent sulfoxide synthase into a thiol dioxygenase by a single point mutation

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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

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Publication details

The article was received on 16 Sep 2015, accepted on 02 Dec 2015 and first published on 14 Dec 2015


Article type: Communication
DOI: 10.1039/C5CC07772A
Citation: Chem. Commun., 2016,52, 1945-1948
  • Open access: Creative Commons BY license
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    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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