ArticleJournal of bacteriology2014
Amino-4-imidazolecarboxamide ribotide directly inhibits coenzyme A biosynthesis in Salmonella enterica.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Species-Level Reconfiguration and Retrospective Bridging Assessment of a Multiplex PCR Panel for Complicated and Recurrent Urinary Tract Infections.Current issues in molecular biology · 2026Article
- De novo or Salvage? Nucleotide Availability as a Driver of Bacterial Adaptation and Virulence.MicrobiologyOpen · 2026Review
- Activation of L-histidine biosynthesis as a new antibiotic strategy against Mycobacterium tuberculosis.Nature communications · 2026Article
- Tetrahydrofolate levels influence 2-aminoacrylate stress inJournal of bacteriology · 2024Article
- Bacillus subtilis FolE is sustained by the ZagA zinc metallochaperone and the alarmone ZTP under conditions of zinc deficiency.Molecular microbiology · 2019Article
- Evolutionary convergence in the biosyntheses of the imidazole moieties of histidine and purines.PloS one · 2018Article
- Untargeted metabolomics confirms and extends the understanding of the impact of aminoimidazole carboxamide ribotide (AICAR) in the metabolic network ofMicrobial cell (Graz, Austria) · 2017Article
- L-2,3-diaminopropionate generates diverse metabolic stresses in Salmonella enterica.Molecular microbiology · 2016Article
- Aminoimidazole Carboxamide Ribotide Exerts Opposing Effects on Thiamine Synthesis in Salmonella enterica.Journal of bacteriology · 2015Article
- From microbiology to cancer biology: the Rid protein family prevents cellular damage caused by endogenously generated reactive nitrogen species.Molecular microbiology · 2015Review
- Nutrient salvaging and metabolism by the intracellular pathogen Legionella pneumophila.Frontiers in cellular and infection microbiology · 2014Review
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Authors and funding
2 authors.
Funding
Abstract
Aminoimidazole carboxamide ribotide (AICAR) is a purine biosynthetic intermediate and a by-product of histidine biosynthesis. In bacteria, yeast, and humans, accumulation of AICAR has been shown to affect an array of cellular processes by both direct and indirect mechanisms. In purine biosynthesis, AICAR is the substrate of the bifunctional protein phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase (PurH, EC 2.1.2.3/3.5.4.10). Strains lacking PurH accumulate AICAR and have a defect in the synthesis of the 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) moiety of thiamine. The formation of HMP is also compromised in vivo when coenzyme A (CoA) levels are reduced. Our results show that the in vivo accumulation of AICAR decreased total CoA pools and, further, that AICAR inhibited the activity of pantoate β-alanine ligase in vitro (PanC, EC 6.3.2.1). These results demonstrated a mechanism of AICAR action and provide new insights into the metabolic consequences of disrupting purine metabolism.
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