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Issue 69, 2016
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Mechanistic study of the radical SAM-dependent amine dehydrogenation reactions

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Abstract

The radical SAM enzyme NosL catalyzes the conversion of L-Trp to 3-methyl-2-indolic acid, and this reaction is initiated by the 5′-deoxyadenosyl (dAdo) radical-mediated hydrogen abstraction from the L-Trp amino group. We demonstrate here that when D-Trp was used in the NosL reaction, hydrogen abstraction occurs promiscuously at both the amino group and Cα of D-Trp. These results inspired us to establish the detailed mechanism of L-Trp amine dehydrogenation catalyzed by a NosL mutant, and to engineer a novel radical SAM-dependent L-Tyr amine dehydrogenase from the thiamine biosynthesis enzyme ThiH.

Graphical abstract: Mechanistic study of the radical SAM-dependent amine dehydrogenation reactions

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Publication details

The article was received on 09 Jul 2016, accepted on 27 Jul 2016 and first published on 29 Jul 2016


Article type: Communication
DOI: 10.1039/C6CC05661J
Citation: Chem. Commun., 2016,52, 10555-10558
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    Mechanistic study of the radical SAM-dependent amine dehydrogenation reactions

    X. Ji, W. Liu, S. Yuan, Y. Yin, W. Ding and Q. Zhang, Chem. Commun., 2016, 52, 10555
    DOI: 10.1039/C6CC05661J

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