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 Dez 2018
First published
06 Dez 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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements