Component

5-Formiminotetrahydrofolate

Folate intermediate between the FT and CD reactions of FTCD.

4 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

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.

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.

Recorded relationships

What acts on it

  1. The formiminotransferase domain of FTCD transfers the formimino group from FIGLU to THF, producing 5-formimino-THF and glutamate.

    Human formimidoyltransferase cyclodeaminase / FTCD → 5-Formiminotetrahydrofolate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Established reaction in the pathway map of a primary human cancer-cell study; genetic perturbation and metabolomics investigate pathway flux rather than purified kinetics of every individual enzyme.
    limitations
    The existing rat FTCD biochemical claim remains a separate species-specific record. Correction record: A 2022 author correction is indexed (PMID 35017686). The publisher-accessible record identifies corrected Fig. 1f, Extended Data Fig. 11, Supplementary Fig. 3 and source data for Figs. 1/2, including an erroneous doxorubicin replicate. Complete correction narrative was not accessible; its full impact is not independently cleared. The original study remains flagged corrected, and no comprehensive safety claim is made. https://www.nature.com/articles/s41586-021-03487-2
    nutrient_topic
    L-Histidine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Histidine
    plain_language
    Folate accepts a group from a histidine-derived intermediate.
    primary_references
    Histidine catabolism is a major determinant of methotrexate sensitivity. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29995852/ · DOI 10.1038/s41586-018-0316-7

    L-Histidine: supply, catabolism, histamine, receptors and cross-nutrient mechanisms (2026-09-19) · lines 130–136

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Established reaction in the pathway map of a primary human cancer-cell study; genetic perturbation and metabolomics investigate pathway flux rather than purified kinetics of every individual enzyme. · source_derived_draft · unverified_draft

    ## histidine-ftcd-transfer Folate accepts a group from a histidine-derived intermediate. The formiminotransferase domain of FTCD transfers the formimino group from FIGLU to THF, producing 5-formimino-THF and glutamate. Model: Established reaction in the pathway map of a primary human cancer-cell study; genetic perturbation and metabolomics investigate pathway flux rather than purified kinetics of every individual enzyme. Limitations: The existing rat FTCD biochemical claim remains a separate species-specific record. Correction record: A 2022 author correction is indexed (PMID 35017686). The publisher-accessible record identifies corrected Fig. 1f, Extended Data Fig. 11, Supplementary Fig. 3 and source data for Figs. 1/2, including an erroneous doxorubicin replicate. Complete correction narrative was not accessible; its full impact is not independently cleared. The original study remains flagged corrected, and no comprehensive safety claim is made. https://www.nature.com/articles/s41586-021-03487-2 Evidence access: Primary full text Histidine catabolism is a major determinant of methotrexate sensitivity. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29995852/ · DOI 10.1038/s41586-018-0316-7
    Complete structured claim and evidence

  2. Rat FTCD cyclodeaminase converts 5-formimino-THF to 5,10-methenyl-THF with ammonia release.

    Rat formiminotransferase cyclodeaminase / FTCD → 5-Formiminotetrahydrofolate source_derived_draftungraded
    Experimental context and source evidence
    evidence_location
    Cyclodeaminase active-site results and enzyme assay methods.
    experimental_model
    Recombinant protein catalytic assay and mutagenesis
    exposure
    Recombinant rat FTCD and CD-site mutants.
    limitations
    Rat enzyme; human catalytic rates are not measured.
    nutrient_topic
    Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. · Folate (vitamin B9)
    organism
    Rattus norvegicus
    plain_language
    A second enzyme domain converts the transferred group into methenyl-folate.
    primary_references
    [mao-2004] Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer (2004). https://pubmed.ncbi.nlm.nih.gov/15272307/ DOI: 10.1038/sj.emboj.7600327
    tissue_or_cell_type
    Cell-free

    Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1308–1319

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant protein catalytic assay and mutagenesis · source_derived_draft · unverified_draft

    ### rat-ftcd-cyclodeamination Rat FTCD cyclodeaminase converts 5-formimino-THF to 5,10-methenyl-THF with ammonia release. 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 enzyme domain converts the transferred group into methenyl-folate. organism: Rattus norvegicus tissue_or_cell_type: Cell-free experimental_model: Recombinant protein catalytic assay and mutagenesis limitations: Rat enzyme; human catalytic rates are not measured. exposure: Recombinant rat FTCD and CD-site mutants. evidence_location: Cyclodeaminase active-site results and enzyme assay methods. [mao-2004] Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer (2004). https://pubmed.ncbi.nlm.nih.gov/15272307/ DOI: 10.1038/sj.emboj.7600327
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The cyclodeaminase domain of FTCD converts 5-formimino-THF to 5,10-methenyl-THF.

    Human formimidoyltransferase cyclodeaminase / FTCD → 5,10-Methenyltetrahydrofolate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Established reaction in the pathway map of a primary human cancer-cell study; genetic perturbation and metabolomics investigate pathway flux rather than purified kinetics of every individual enzyme.
    limitations
    Two catalytic activities are separately searchable; this does not establish folate depletion in a normally nourished person. Correction record: A 2022 author correction is indexed (PMID 35017686). The publisher-accessible record identifies corrected Fig. 1f, Extended Data Fig. 11, Supplementary Fig. 3 and source data for Figs. 1/2, including an erroneous doxorubicin replicate. Complete correction narrative was not accessible; its full impact is not independently cleared. The original study remains flagged corrected, and no comprehensive safety claim is made. https://www.nature.com/articles/s41586-021-03487-2
    nutrient_topic
    L-Histidine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Histidine
    plain_language
    A second activity of the same enzyme hands the group into one-carbon metabolism.
    primary_references
    Histidine catabolism is a major determinant of methotrexate sensitivity. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29995852/ · DOI 10.1038/s41586-018-0316-7

    L-Histidine: supply, catabolism, histamine, receptors and cross-nutrient mechanisms (2026-09-19) · lines 138–144

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Established reaction in the pathway map of a primary human cancer-cell study; genetic perturbation and metabolomics investigate pathway flux rather than purified kinetics of every individual enzyme. · source_derived_draft · unverified_draft

    ## histidine-ftcd-cyclodeamination A second activity of the same enzyme hands the group into one-carbon metabolism. The cyclodeaminase domain of FTCD converts 5-formimino-THF to 5,10-methenyl-THF. Model: Established reaction in the pathway map of a primary human cancer-cell study; genetic perturbation and metabolomics investigate pathway flux rather than purified kinetics of every individual enzyme. Limitations: Two catalytic activities are separately searchable; this does not establish folate depletion in a normally nourished person. Correction record: A 2022 author correction is indexed (PMID 35017686). The publisher-accessible record identifies corrected Fig. 1f, Extended Data Fig. 11, Supplementary Fig. 3 and source data for Figs. 1/2, including an erroneous doxorubicin replicate. Complete correction narrative was not accessible; its full impact is not independently cleared. The original study remains flagged corrected, and no comprehensive safety claim is made. https://www.nature.com/articles/s41586-021-03487-2 Evidence access: Primary full text Histidine catabolism is a major determinant of methotrexate sensitivity. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29995852/ · DOI 10.1038/s41586-018-0316-7
    Complete structured claim and evidence

  2. The FT activity of rat FTCD transfers the FIGLU formimino group to THF, yielding 5-formimino-THF and glutamate.

    Rat formiminotransferase cyclodeaminase / FTCD → N-Formimino-L-glutamate source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Histidine degradation supplies a folate-bound carbon group.
    evidence_location
    Introduction reaction definition; Figure 1 and FT-domain structural analysis.
    experimental_model
    Recombinant protein structure and functional analysis
    exposure
    Recombinant rat FTCD; FT-domain structural analysis.
    limitations
    Rat enzyme; no human histidine-loading response is inferred.
    nutrient_topic
    Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. · Folate (vitamin B9)
    organism
    Rattus norvegicus
    plain_language
    This step brings histidine-derived carbon into folate chemistry.
    primary_references
    [mao-2004] Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer (2004). https://pubmed.ncbi.nlm.nih.gov/15272307/ DOI: 10.1038/sj.emboj.7600327
    tissue_or_cell_type
    Cell-free

    Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1294–1306

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant protein structure and functional analysis · source_derived_draft · unverified_draft

    ### rat-ftcd-formimino-transfer The FT activity of rat FTCD transfers the FIGLU formimino group to THF, yielding 5-formimino-THF and glutamate. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: This step brings histidine-derived carbon into folate chemistry. organism: Rattus norvegicus tissue_or_cell_type: Cell-free experimental_model: Recombinant protein structure and functional analysis limitations: Rat enzyme; no human histidine-loading response is inferred. exposure: Recombinant rat FTCD; FT-domain structural analysis. cross_nutrient: Histidine degradation supplies a folate-bound carbon group. evidence_location: Introduction reaction definition; Figure 1 and FT-domain structural analysis. [mao-2004] Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer (2004). https://pubmed.ncbi.nlm.nih.gov/15272307/ DOI: 10.1038/sj.emboj.7600327
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards