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

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...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2016-01, Vol.52 (9), p.1945-1948
Hauptverfasser: Goncharenko, Kristina V, Seebeck, Florian P
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/c5cc07772a