Component
5-Formamidoimidazole-4-carboxamide ribonucleotide
Chemically distinct folate-pathway or nucleotide intermediate; shared across species.
2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What acts on it
Human ATIC has a separable IMP cyclohydrolase domain that converts FAICAR to IMP.
Experimental context and source evidence
- experimental_model
- Truncation-domain activity mapping
- exposure
- Assay conditions described in the linked primary study.
- limitations
- This second step does not consume another folate molecule.
- nutrient_topic
- Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. · Folate (vitamin B9)
- organism
- Homo sapiens
- plain_language
- After the folate donation, ATIC closes the purine ring.
- primary_references
- [rayl-1996] The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping (1996). https://pubmed.ncbi.nlm.nih.gov/8567683/ DOI: 10.1074/jbc.271.4.2225
- tissue_or_cell_type
- Cell-free
Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1022–1032
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Truncation-domain activity mapping · source_derived_draft · unverified_draft
### atic-faicar-cyclization Human ATIC has a separable IMP cyclohydrolase domain that converts FAICAR to IMP. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: After the folate donation, ATIC closes the purine ring. organism: Homo sapiens tissue_or_cell_type: Cell-free experimental_model: Truncation-domain activity mapping limitations: This second step does not consume another folate molecule. exposure: Assay conditions described in the linked primary study. [rayl-1996] The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping (1996). https://pubmed.ncbi.nlm.nih.gov/8567683/ DOI: 10.1074/jbc.271.4.2225
Complete structured claim and evidence
Where it participates (unsigned role)
Purified human ATIC uses 10-formyl-THF for its AICAR formyltransferase reaction, yielding FAICAR.
Experimental context and source evidence
- experimental_model
- Recombinant enzyme kinetics
- exposure
- Assay conditions described in the linked primary study.
- limitations
- Reported folate kinetics used a 6R/6S mixture.
- nutrient_topic
- Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. · Folate (vitamin B9)
- organism
- Homo sapiens
- plain_language
- A second folate donation helps finish the purine ring.
- primary_references
- [rayl-1996] The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping (1996). https://pubmed.ncbi.nlm.nih.gov/8567683/ DOI: 10.1074/jbc.271.4.2225
- tissue_or_cell_type
- Cell-free
Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1010–1020
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant enzyme kinetics · source_derived_draft · unverified_draft
### atic-aicar-formylation Purified human ATIC uses 10-formyl-THF for its AICAR formyltransferase reaction, yielding FAICAR. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: A second folate donation helps finish the purine ring. organism: Homo sapiens tissue_or_cell_type: Cell-free experimental_model: Recombinant enzyme kinetics limitations: Reported folate kinetics used a 6R/6S mixture. exposure: Assay conditions described in the linked primary study. [rayl-1996] The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping (1996). https://pubmed.ncbi.nlm.nih.gov/8567683/ DOI: 10.1074/jbc.271.4.2225
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.