The Thiamine Biosynthetic Enzyme ThiC Catalyzes Multiple Turnovers and Is Inhibited byS-Adenosylmethionine (AdoMet) Metabolites

Enzyme catalyzed formation of radicals from S-adenosylmethionine and inhibition of enzyme activity by the cleavage products

(2012) Martyn J. Hiscox et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Emerging themes in radical SAM chemistry

(2012) Krista A Shisler et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Analysis of ThiC Variants in the Context of the Metabolic Network of Salmonella enterica

(2012) L. D. Palmer et al.   JOURNAL OF BACTERIOLOGY

Treponema denticolaPurE Is a Bacterial AIR Carboxylase

(2011) Sylvain Tranchimand et al.   BIOCHEMISTRY

Quantitative liquid chromatography–tandem mass spectrometry profiling of activated methyl cycle metabolites involved in LuxS-dependent quorum sensing in Escherichia coli

(2010) N.M. Halliday et al.   ANALYTICAL BIOCHEMISTRY

A “Radical Dance” in Thiamin Biosynthesis: Mechanistic Analysis of the Bacterial Hydroxymethylpyrimidine Phosphate Synthase

(2010) Abhishek Chatterjee et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Biotin Synthase Exhibits Burst Kinetics and Multiple Turnovers in the Absence of Inhibition by Products and Product-Related Biomolecules

(2010) Christine E. Farrar et al.   BIOCHEMISTRY

Radicals from S-adenosylmethionine and their application to biosynthesis

(2010) Peter L Roach   CURRENT OPINION IN CHEMICAL BIOLOGY

Anaerobic functionalization of unactivated C–H bonds

(2009) Squire J Booker   CURRENT OPINION IN CHEMICAL BIOLOGY

Product inhibition in the radicalS-adenosylmethionine family

(2009) Martin R. Challand et al.   FEBS LETTERS

Catalytic Activity of the Anaerobic Tyrosine Lyase Required for Thiamine Biosynthesis in Escherichia coli

(2009) Martin R. Challand et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli

(2009) Bryson D Bennett et al.   Nature Chemical Biology

In Vitro Characterization of AtsB, a Radical SAM Formylglycine-Generating Enzyme That Contains Three [4Fe-4S] Clusters†

(2008) Tyler L. Grove et al.   BIOCHEMISTRY

ThiC Is an [Fe-S] Cluster Protein That Requires AdoMet To Generate the 4-Amino-5-hydroxymethyl-2-methylpyrimidine Moiety in Thiamin Synthesis†

(2008) N. Cecilia Martinez-Gomez et al.   BIOCHEMISTRY

Reaction of AdoMet with ThiC Generates a Backbone Free Radical†

(2008) N. Cecilia Martinez-Gomez et al.   BIOCHEMISTRY

Cofactor biosynthesis—still yielding fascinating new biological chemistry

(2008) Tadhg P Begley et al.   CURRENT OPINION IN CHEMICAL BIOLOGY

Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily

(2008) Abhishek Chatterjee et al.   Nature Chemical Biology