The Thiamine Biosynthetic Enzyme ThiC Catalyzes Multiple Turnovers and Is Inhibited by S-Adenosylmethionine (AdoMet) Metabolites
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference47 articles.
1. ThiC is an [Fe-S] cluster protein that requires AdoMet to generate the 4-amino-5-hydroxymethyl-2-methylpyrimidine moiety in thiamin synthesis;Martinez-Gomez;Biochemistry,2008
2. Reaction of AdoMet with ThiC generates a backbone free radical;Martinez-Gomez;Biochemistry,2009
3. Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily;Chatterjee;Nat. Chem. Biol,2008
4. A “radical dance” in thiamin biosynthesis. Mechanistic analysis of the bacterial hydroxymethylpyrimidine phosphate synthase;Chatterjee;Angew. Chem. Int. Ed. Engl,2010
5. Thiamin biosynthesis in prokaryotes;Begley;Arch. Microbiol,1999
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