ArticleJournal of bacteriology2012
Analysis of ThiC variants in the context of the metabolic network of Salmonella enterica.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 10 citations in OpenAlex.
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- Tetrahydrofolate levels influence 2-aminoacrylate stress inJournal of bacteriology · 2024Article
- Genetic Analysis Using Vitamin BJournal of bacteriology · 2022Article
- Perturbation of the metabolic network in Salmonella enterica reveals cross-talk between coenzyme A and thiamine pathways.PloS one · 2018Article
- The three-legged stool of understanding metabolism: integrating metabolomics with biochemical genetics and computational modeling.AIMS microbiology · 2018Article
- 2-Aminoacrylate Stress Induces a Context-Dependent Glycine Requirement in ridA Strains of Salmonella enterica.Journal of bacteriology · 2016Article
- Aminoimidazole Carboxamide Ribotide Exerts Opposing Effects on Thiamine Synthesis in Salmonella enterica.Journal of bacteriology · 2015Article
- Radical S-adenosylmethionine enzymes.Chemical reviews · 2014Review
- The thiamine biosynthetic enzyme ThiC catalyzes multiple turnovers and is inhibited by S-adenosylmethionine (AdoMet) metabolites.The Journal of biological chemistry · 2013Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In bacteria, the 4-amino-hydroxymethyl-2-methylpyrimidine (HMP) moiety of thiamine is synthesized from 5-aminoimidazole ribotide (AIR), a branch point metabolite of purine and thiamine biosynthesis. ThiC is a member of the radical S-adenosylmethionine (AdoMet) superfamily and catalyzes the complex chemical rearrangement of AIR to HMP-P. As reconstituted in vitro, the ThiC reaction requires AdoMet, AIR, and reductant. This study analyzed variants of ThiC in vivo and in vitro to probe the metabolic network surrounding AIR in Salmonella enterica. Several variants of ThiC that required metabolic perturbations to function in vivo were biochemically characterized in vitro. Results presented herein indicate that the subtleties of the metabolic network have not been captured in the current reconstitution of the ThiC reaction.
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Registered trials
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