Recent advances in HemN-like radical S-adenosyl-l-methionine enzyme-catalyzed reactions
Author:
Affiliation:
1. State Key Laboratory of Bio-organic and Natural Products Chemistry
2. Center for Excellence in Molecular Synthesis
3. Shanghai Institute of Organic Chemistry
4. University of Chinese Academy of Sciences
5. Chinese Academy of Sciences
Abstract
HemN-like radical S-adenosyl-l-methionine (SAM) enzymes have been recently disclosed to catalyze diverse chemically challenging reactions from primary to secondary metabolic pathways.
Funder
National Natural Science Foundation of China
Chinese Academy of Sciences
K. C. Wong Education Foundation
Publisher
Royal Society of Chemistry (RSC)
Subject
Organic Chemistry,Drug Discovery,Biochemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2020/NP/C9NP00032A
Reference73 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. An Anchoring Role for FeS Clusters: Chelation of the Amino Acid Moiety of S-Adenosylmethionine to the Unique Iron Site of the [4Fe−4S] Cluster of Pyruvate Formate-Lyase Activating Enzyme
3. New glycyl radical enzymes catalysing key metabolic steps in anaerobic bacteria
4. Radical-mediated enzymatic carbon chain fragmentation-recombination
5. The Radical S-Adenosyl-l-methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA Peptide
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