Issue 7, 2019

Radical SAM-dependent adenosylation catalyzed by l-tyrosine lyases

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

Supplementary files

Article information

Article type
Communication
Submitted
21 Nov 2018
Accepted
01 Dec 2018
First published
06 Dec 2018

Org. Biomol. Chem., 2019,17, 1809-1812

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, 17, 1809 DOI: 10.1039/C8OB02906G

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