Component

Human MTHFD2

Homo sapiens protein; gene perturbations are separate gene entities.

2 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 it acts on

  1. Purified human MTHFD2 oxidizes 5,10-methylene-THF using NAD+ to form methenyl-THF and NADH.

    Human MTHFD2 → 5,10-Methylenetetrahydrofolate source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Nicotinamide cofactors connect folate chemistry to redox metabolism.
    experimental_model
    Purified recombinant enzyme
    exposure
    Assay conditions described in the linked primary study.
    limitations
    Cellular cofactor partition is not quantified.
    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
    This mitochondrial enzyme extracts electrons from folate-bound carbon.
    primary_references
    [shin-2017] Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase (2017). https://pubmed.ncbi.nlm.nih.gov/29225823/ DOI: 10.1186/s40170-017-0173-0
    tissue_or_cell_type
    Cell-free

    Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 812–823

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant enzyme · source_derived_draft · unverified_draft

    ### mthfd2-nad-oxidation Purified human MTHFD2 oxidizes 5,10-methylene-THF using NAD+ to form methenyl-THF and NADH. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: This mitochondrial enzyme extracts electrons from folate-bound carbon. organism: Homo sapiens tissue_or_cell_type: Cell-free experimental_model: Purified recombinant enzyme limitations: Cellular cofactor partition is not quantified. exposure: Assay conditions described in the linked primary study. cross_nutrient: Nicotinamide cofactors connect folate chemistry to redox metabolism. [shin-2017] Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase (2017). https://pubmed.ncbi.nlm.nih.gov/29225823/ DOI: 10.1186/s40170-017-0173-0
    Complete structured claim and evidence

  2. Human MTHFD2 also uses NADP+ with methylene-THF pentaglutamate; NADP-linked activity increases relative to the monoglutamate assay.

    Human MTHFD2 → NADP+ source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Folate polyglutamylation changes nicotinamide-cofactor use.
    experimental_model
    Purified recombinant enzyme
    exposure
    Mono- versus pentaglutamate folate substrates; controlled NAD(P)+ assays.
    limitations
    Kinetics do not establish dominant in vivo NADPH production.
    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
    The folate tail affects which electron carrier the enzyme uses.
    primary_references
    [shin-2017] Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase (2017). https://pubmed.ncbi.nlm.nih.gov/29225823/ DOI: 10.1186/s40170-017-0173-0
    tissue_or_cell_type
    Cell-free

    Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 825–836

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant enzyme · source_derived_draft · unverified_draft

    ### mthfd2-nadp-polyglutamate Human MTHFD2 also uses NADP+ with methylene-THF pentaglutamate; NADP-linked activity increases relative to the monoglutamate assay. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The folate tail affects which electron carrier the enzyme uses. organism: Homo sapiens tissue_or_cell_type: Cell-free experimental_model: Purified recombinant enzyme limitations: Kinetics do not establish dominant in vivo NADPH production. exposure: Mono- versus pentaglutamate folate substrates; controlled NAD(P)+ assays. cross_nutrient: Folate polyglutamylation changes nicotinamide-cofactor use. [shin-2017] Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase (2017). https://pubmed.ncbi.nlm.nih.gov/29225823/ DOI: 10.1186/s40170-017-0173-0
    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