Changing Fates of the Substrate Radicals Generated in the Active Sites of the B12-Dependent Radical SAM Enzymes OxsB and AlsB
Author:
Affiliation:
1. Department of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States
2. Division of Chemical Biology & Medicinal Chemistry, College of Pharmacy, University of Texas at Austin, Austin, Texas 78712, United States
Funder
Welch Foundation
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.2c12953
Reference63 articles.
1. Radical SAM enzymes in the biosynthesis of sugar-containing natural products
2. Radical SAM enzymes involved in the biosynthesis of purine-based natural products
3. Radical SAM Enzymes in the Biosynthesis of Ribosomally Synthesized and Post-translationally Modified Peptides (RiPPs)
4. C–C bond forming radical SAM enzymes involved in the construction of carbon skeletons of cofactors and natural products
5. Cobalamin-dependent radicalS-adenosyl-l-methionine enzymes in natural product biosynthesis
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