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Radical SAM-dependent adenosylation catalyzed by L-tyrosine lyases

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Abstract

The radical S-adenosylmethionine (SAM) superfamily is currently the largest known enzyme family. These enzymes reductively cleave SAM to produce a highly reactive 5′-deoxyadenosyl (dAdo) radical, which abstracts a hydrogen from the substrate and initiates diverse reactions. The canonic dAdo radical-mediated hydrogen abstraction can be changed to radical addition reactions by using olefin-containing substrate analogues, which result in adenosylation reactions. Here we report investigation of the adenosylation reactions catalyzed by four radical SAM L-Tyr lyases (RSTLs), including HydG, FbiC, and two ThiH enzymes from different organisms. We show RSTLs have diverse substrate specificity, and ThiH from E. coli exhibits the highest substrate tolerance toward the tested substrates. We also show ThiH from Clostridium berjerinckii does not act on 4-amino-L-phenylalanine, but catalyzes adenosylation of the corresponding olefin-containing analogue, suggesting adenosylation may occur more easily than the canonic radical SAM reactions. Our study highlights the remarkable catalytic promiscuity of radical SAM enzyme and the potential in using these enzymes for the synthesis of nucleotide-containing compounds.

Graphical abstract: Radical SAM-dependent adenosylation catalyzed by l-tyrosine lyases

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Publication details

The article was received on 21 Nov 2018, accepted on 01 Dec 2018 and first published on 06 Dec 2018


Article type: Communication
DOI: 10.1039/C8OB02906G
Citation: Org. Biomol. Chem., 2019, Advance Article
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    Radical SAM-dependent adenosylation catalyzed by L-tyrosine lyases

    Y. Wu, R. Wu, D. Mandalapu, X. Ji, T. Chen, W. Ding and Q. Zhang, Org. Biomol. Chem., 2019, Advance Article , DOI: 10.1039/C8OB02906G

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