Radical S-Adenosylmethionine Enzymes
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717, United States
Funder
National Institutes of Health
Basic Energy Sciences, Office of Science, U.S. Department of Energy
Publisher
American Chemical Society (ACS)
Subject
General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/cr4004709
Reference679 articles.
1. 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
2. Post-translational activation introduces a free radical into pyruvate formate-lyase.
3. Pyruvate Formate-Lyase Reaction in Escherichia coli. The Enzymatic System Converting and Inactive Form of the Lyase into the Catalytically Active Enzyme
4. The free radical in pyruvate formate-lyase is located on glycine-734.
5. Pyruvate Formate-Lyase Activating Enzyme Is an Iron−Sulfur Protein
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