Component

Sarcosine

N-methylglycine.

3 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 acts on it

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

    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

Where it participates (unsigned role)

  1. Rat DMGDH catalyzes oxidative demethylation of dimethylglycine to sarcosine.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/choline-research/24858690.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f", "start_char": 0, "end_char": 1506, "text_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f"}
    experimental_model
    Rat DMGDH crystallography and enzyme characterization
    exposure
    Dimethylglycine turnover and THF-bound structures
    limitations
    Species and assay context retained. The proposed intramolecular transfer route is not represented as a directly observed moving intermediate.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Rat recombinant enzyme
    plain_language
    After betaine donates one methyl group, another enzyme handles the remaining dimethylglycine.
    primary_references
    [choline-p24858690] Folate in demethylation: the crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate. (2014). https://pubmed.ncbi.nlm.nih.gov/24858690/ DOI: 10.1016/j.bbrc.2014.05.064
    tissue_or_cell_type
    Mitochondrial-enzyme preparation

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 659–670

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

    ### choline-dmgdh-sarcosine Rat DMGDH catalyzes oxidative demethylation of dimethylglycine to sarcosine. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: After betaine donates one methyl group, another enzyme handles the remaining dimethylglycine. organism: Rat recombinant enzyme tissue_or_cell_type: Mitochondrial-enzyme preparation experimental_model: Rat DMGDH crystallography and enzyme characterization limitations: Species and assay context retained. The proposed intramolecular transfer route is not represented as a directly observed moving intermediate. exposure: Dimethylglycine turnover and THF-bound structures evidence_span: {"source_cache": "artifacts/choline-research/24858690.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f", "start_char": 0, "end_char": 1506, "text_sha256": "e00bbb8f1c2c805e9d7261c286bace5758abd277bc95b3e0a830bd9cdb82a34f"} [choline-p24858690] Folate in demethylation: the crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate. (2014). https://pubmed.ncbi.nlm.nih.gov/24858690/ DOI: 10.1016/j.bbrc.2014.05.064
    Complete structured claim and evidence
  2. Rat GNMT structures located two folate-binding sites between subunits; occupancy restricts the N-terminal movements needed for substrate access.

    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

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