Component

Glycine N-methyltransferase (Rattus norvegicus)

Rat GNMT in native liver and recombinant assays.

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 it acts on

  1. Rat GNMT activity assays measured SAM-dependent glycine methylation to sarcosine.

    Glycine N-methyltransferase (Rattus norvegicus) → Sarcosine source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Native rat liver and bacterially expressed rat GNMT.
    limitations
    Does not quantify whole-body methyl demand.
    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
    GNMT spends a SAM methyl group on glycine.
    primary_references
    [luka-2008] Acetylation of N-terminal valine of glycine N-methyltransferase affects enzyme inhibition by folate (2008). https://pubmed.ncbi.nlm.nih.gov/18501206/ DOI: 10.1016/j.bbapap.2008.04.016
    tissue_or_cell_type
    Native/recombinant rat enzyme

    Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 756–765

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Native rat liver and bacterially expressed rat GNMT. · source_derived_draft · unverified_draft

    ### folate-methyl-gnmt-methyl-use Rat GNMT activity assays measured SAM-dependent glycine methylation to sarcosine. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: GNMT spends a SAM methyl group on glycine. organism: Rattus norvegicus tissue_or_cell_type: Native/recombinant rat enzyme experimental_model: Native rat liver and bacterially expressed rat GNMT. limitations: Does not quantify whole-body methyl demand. [luka-2008] Acetylation of N-terminal valine of glycine N-methyltransferase affects enzyme inhibition by folate (2008). https://pubmed.ncbi.nlm.nih.gov/18501206/ DOI: 10.1016/j.bbapap.2008.04.016
    Complete structured claim and evidence

What acts on it

  1. Rat GNMT structures located two folate-binding sites between subunits; occupancy restricts the N-terminal movements needed for substrate access.

    5-Methyltetrahydrofolate → Glycine N-methyltransferase (Rattus norvegicus) source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat liver GNMT crystallography and binding experiments.
    limitations
    Rat enzyme and defined ligand conditions; not a demonstrated human supplement interaction.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Folate can regulate methyl-group disposal through glycine.
    primary_references
    5-methyltetrahydrofolate is bound in intersubunit areas of rat liver folate-binding protein glycine N-methyltransferase. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17158459/ · DOI 10.1074/jbc.M610384200

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 212–218

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat liver GNMT crystallography and binding experiments. · source_derived_draft · unverified_draft

    ## methionine-gnmt-folate-structure Folate can regulate methyl-group disposal through glycine. Rat GNMT structures located two folate-binding sites between subunits; occupancy restricts the N-terminal movements needed for substrate access. Model: Rat liver GNMT crystallography and binding experiments. Limitations: Rat enzyme and defined ligand conditions; not a demonstrated human supplement interaction. Evidence access: Primary abstract 5-methyltetrahydrofolate is bound in intersubunit areas of rat liver folate-binding protein glycine N-methyltransferase. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17158459/ · DOI 10.1074/jbc.M610384200
    Complete structured claim and evidence

  2. Non-acetylated recombinant GNMT required 590 micromolar folate pentaglutamate for 50% inhibition, versus 1.3 micromolar for native acetylated GNMT.

    5-Methyltetrahydrofolate pentaglutamate → Glycine N-methyltransferase (Rattus norvegicus) source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Native rat liver and bacterially expressed rat GNMT.
    limitations
    Recombinant potency cannot be directly transferred to liver.
    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
    Protein modification changed inhibitory sensitivity.
    primary_references
    [luka-2008] Acetylation of N-terminal valine of glycine N-methyltransferase affects enzyme inhibition by folate (2008). https://pubmed.ncbi.nlm.nih.gov/18501206/ DOI: 10.1016/j.bbapap.2008.04.016
    tissue_or_cell_type
    Native versus recombinant rat enzyme

    Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 778–787

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Native rat liver and bacterially expressed rat GNMT. · source_derived_draft · unverified_draft

    ### folate-methyl-gnmt-acetylation Non-acetylated recombinant GNMT required 590 micromolar folate pentaglutamate for 50% inhibition, versus 1.3 micromolar for native acetylated GNMT. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: Protein modification changed inhibitory sensitivity. organism: Rattus norvegicus tissue_or_cell_type: Native versus recombinant rat enzyme experimental_model: Native rat liver and bacterially expressed rat GNMT. limitations: Recombinant potency cannot be directly transferred to liver. [luka-2008] Acetylation of N-terminal valine of glycine N-methyltransferase affects enzyme inhibition by folate (2008). https://pubmed.ncbi.nlm.nih.gov/18501206/ DOI: 10.1016/j.bbapap.2008.04.016
    Complete structured claim and evidence

  3. Folate pentaglutamate produced 50% inhibition of native rat GNMT at 1.3 micromolar.

    5-Methyltetrahydrofolate pentaglutamate → Glycine N-methyltransferase (Rattus norvegicus) source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Native rat liver and bacterially expressed rat GNMT.
    limitations
    Not a human circulating threshold.
    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 folate form restrains SAM use by GNMT.
    primary_references
    [luka-2008] Acetylation of N-terminal valine of glycine N-methyltransferase affects enzyme inhibition by folate (2008). https://pubmed.ncbi.nlm.nih.gov/18501206/ DOI: 10.1016/j.bbapap.2008.04.016
    tissue_or_cell_type
    Purified liver enzyme

    Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 767–776

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Native rat liver and bacterially expressed rat GNMT. · source_derived_draft · unverified_draft

    ### folate-methyl-gnmt-folate-inhibition Folate pentaglutamate produced 50% inhibition of native rat GNMT at 1.3 micromolar. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: A folate form restrains SAM use by GNMT. organism: Rattus norvegicus tissue_or_cell_type: Purified liver enzyme experimental_model: Native rat liver and bacterially expressed rat GNMT. limitations: Not a human circulating threshold. [luka-2008] Acetylation of N-terminal valine of glycine N-methyltransferase affects enzyme inhibition by folate (2008). https://pubmed.ncbi.nlm.nih.gov/18501206/ DOI: 10.1016/j.bbapap.2008.04.016
    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