Component
Human trifunctional GART
Homo sapiens protein; gene perturbations are separate gene entities.
1 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 it acts on
The human GART transformylase domain binds a folate formyl donor and GAR-site acceptor in a ternary complex supporting GAR formylation to FGAR.
Experimental context and source evidence
- experimental_model
- X-ray crystallography
- exposure
- Assay conditions described in the linked primary study.
- limitations
- Structures used 10-formyl-dideazafolate and hydroxyacetamide ribonucleotide analogues.
- 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
- Folate donates one carbon early in purine-base construction.
- primary_references
- [dahms-2005] The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase (2005). https://pubmed.ncbi.nlm.nih.gov/16026156/ DOI: 10.1021/bi050307g
- tissue_or_cell_type
- Purified domain
Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 998–1008
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray crystallography · source_derived_draft · unverified_draft
### gart-formyl-transfer The human GART transformylase domain binds a folate formyl donor and GAR-site acceptor in a ternary complex supporting GAR formylation to FGAR. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: Folate donates one carbon early in purine-base construction. organism: Homo sapiens tissue_or_cell_type: Purified domain experimental_model: X-ray crystallography limitations: Structures used 10-formyl-dideazafolate and hydroxyacetamide ribonucleotide analogues. exposure: Assay conditions described in the linked primary study. [dahms-2005] The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase (2005). https://pubmed.ncbi.nlm.nih.gov/16026156/ DOI: 10.1021/bi050307g
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.