Component

MTHFR Glu429Ala protein

Protein substitution encoded by the historical A1298C variant.

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.

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. Glu429Ala MTHFR showed FAD-release behavior indistinguishable from wild type under the tested dilution conditions.

    MTHFR Glu429Ala protein → FAD source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Bounds extrapolation of B2-cofactor loss across MTHFR variants.
    evidence_location
    Results: FAD loss; Figs 1-3
    experimental_model
    Baculovirus-produced purified human wild-type, Ala222Val, Glu429Ala and double-mutant MTHFR; dilution/cofactor-release assays.
    exposure
    Purified-enzyme assay
    limitations
    Normal result under tested in-vitro conditions does not exclude all cellular effects of A1298C.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Homo sapiens
    plain_language
    The two common MTHFR variants did not share the same cofactor-retention phenotype.
    primary_references
    [yamada2001] Effects of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase. (2001). https://pubmed.ncbi.nlm.nih.gov/11742092/ DOI: 10.1073/pnas.261469998
    tissue_or_cell_type
    Purified recombinant enzyme; no intact tissue

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1080–1092

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Baculovirus-produced purified human wild-type, Ala222Val, Glu429Ala and double-mutant MTHFR; dilution/cofactor-release assays. · source_derived_draft · unverified_draft

    ### b2-mthfr-glu429ala-retention Glu429Ala MTHFR showed FAD-release behavior indistinguishable from wild type under the tested dilution conditions. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The two common MTHFR variants did not share the same cofactor-retention phenotype. organism: Homo sapiens tissue_or_cell_type: Purified recombinant enzyme; no intact tissue experimental_model: Baculovirus-produced purified human wild-type, Ala222Val, Glu429Ala and double-mutant MTHFR; dilution/cofactor-release assays. limitations: Normal result under tested in-vitro conditions does not exclude all cellular effects of A1298C. exposure: Purified-enzyme assay cross_nutrient: Bounds extrapolation of B2-cofactor loss across MTHFR variants. evidence_location: Results: FAD loss; Figs 1-3 [yamada2001] Effects of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase. (2001). https://pubmed.ncbi.nlm.nih.gov/11742092/ DOI: 10.1073/pnas.261469998
    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