Insertion of 4-Demethylwyosine in tRNAPhe Catalyzed by the Radical S-Adenosyl-l-methionine Enzyme TYW1 Entails Oxidative Cleavage of Pyruvate to Form CO2
Author:
Affiliation:
1. Department of Chemistry, University of Utah, Salt Lake City, Utah 84112, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.2c00519
Reference21 articles.
1. Atlas of the Radical SAM Superfamily: Divergent Evolution of Function Using a “Plug and Play” Domain
2. Radical S-Adenosylmethionine Enzymes
3. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods
4. Electron-Nuclear Double Resonance Spectroscopic Evidence That S-Adenosylmethionine Binds in Contact with the Catalytically Active [4Fe−4S]+ Cluster of Pyruvate Formate-Lyase Activating Enzyme
5. Coordination and Mechanism of Reversible Cleavage of S-Adenosylmethionine by the [4Fe-4S] Center in Lysine 2,3-Aminomutase
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