Component

4-Trimethylaminobutyraldehyde

Independent small molecule record; interpretation is limited by each linked claim and its study context.

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. Human ALDH9A1 oxidizes trimethylaminobutyraldehyde to gamma-butyrobetaine using NAD+.

    4-Trimethylaminobutyraldehyde → gamma-Butyrobetaine source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Rat enzyme purification and recombinant human ALDH9 comparison
    limitations
    ALDH9A1 has additional aldehyde substrates.
    organism
    Homo sapiens
    plain_language
    An aldehyde is converted into the immediate carnitine precursor.
    primary_references
    [vaz2000] Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis (2000). https://pubmed.ncbi.nlm.nih.gov/10702312/ DOI: 10.1074/jbc.275.10.7390
    tissue_or_cell_type
    Cytosolic carnitine-biosynthesis reaction

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 197–205

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat enzyme purification and recombinant human ALDH9 comparison · source_derived_draft · unverified_draft

    ### aldh9a1-tmaba-oxidation Human ALDH9A1 oxidizes trimethylaminobutyraldehyde to gamma-butyrobetaine using NAD+. Plain language: An aldehyde is converted into the immediate carnitine precursor. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Cytosolic carnitine-biosynthesis reaction experimental_model: Rat enzyme purification and recombinant human ALDH9 comparison limitations: ALDH9A1 has additional aldehyde substrates. [vaz2000] Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis (2000). https://pubmed.ncbi.nlm.nih.gov/10702312/ DOI: 10.1074/jbc.275.10.7390
    Complete structured claim and evidence

What acts on it

  1. Purified human SHMT1 cleaves hydroxytrimethyllysine into trimethylaminobutyraldehyde and glycine.

    (2S,3S)-3-Hydroxy-N-epsilon-trimethyllysine → 4-Trimethylaminobutyraldehyde source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified human enzyme; NMR and coupled activity assays
    limitations
    Whole-body flux contribution remains unquantified.
    organism
    Homo sapiens
    plain_language
    SHMT1 can perform the second carnitine-synthesis reaction.
    primary_references
    [osmes2024] One substrate many enzymes virtual screening uncovers missing genes of carnitine biosynthesis in human and mouse (2024). https://www.nature.com/articles/s41467-024-47466-3 DOI: 10.1038/s41467-024-47466-3
    tissue_or_cell_type
    Cytosolic enzyme tested in vitro

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 177–185

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

    ### shmt1-html-cleavage Purified human SHMT1 cleaves hydroxytrimethyllysine into trimethylaminobutyraldehyde and glycine. Plain language: SHMT1 can perform the second carnitine-synthesis reaction. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Cytosolic enzyme tested in vitro experimental_model: Purified human enzyme; NMR and coupled activity assays limitations: Whole-body flux contribution remains unquantified. [osmes2024] One substrate many enzymes virtual screening uncovers missing genes of carnitine biosynthesis in human and mouse (2024). https://www.nature.com/articles/s41467-024-47466-3 DOI: 10.1038/s41467-024-47466-3
    Complete structured claim and evidence

  2. Purified human SHMT2 also cleaves hydroxytrimethyllysine, with lower measured catalytic efficiency than SHMT1.

    (2S,3S)-3-Hydroxy-N-epsilon-trimethyllysine → 4-Trimethylaminobutyraldehyde source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified human enzyme kinetic assay
    limitations
    Mouse Tha1 specialization should not be assigned to a human THA1 enzyme.
    organism
    Homo sapiens
    plain_language
    SHMT2 provides another demonstrated aldolase activity.
    primary_references
    [osmes2024] One substrate many enzymes virtual screening uncovers missing genes of carnitine biosynthesis in human and mouse (2024). https://www.nature.com/articles/s41467-024-47466-3 DOI: 10.1038/s41467-024-47466-3
    tissue_or_cell_type
    Mitochondrial enzyme tested in vitro

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 187–195

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

    ### shmt2-html-cleavage Purified human SHMT2 also cleaves hydroxytrimethyllysine, with lower measured catalytic efficiency than SHMT1. Plain language: SHMT2 provides another demonstrated aldolase activity. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Mitochondrial enzyme tested in vitro experimental_model: Purified human enzyme kinetic assay limitations: Mouse Tha1 specialization should not be assigned to a human THA1 enzyme. [osmes2024] One substrate many enzymes virtual screening uncovers missing genes of carnitine biosynthesis in human and mouse (2024). https://www.nature.com/articles/s41467-024-47466-3 DOI: 10.1038/s41467-024-47466-3
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Expressing human ALDH9 in bacteria produced NAD+-dependent trimethylaminobutyraldehyde dehydrogenase activity, completing the aldehyde-to-gamma-butyrobetaine step.

    ALDH9A1 → gamma-Butyrobetaine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant human ALDH9 compared with purified and recombinant rat enzyme.
    limitations
    NAD+ dependence does not establish benefit from niacin supplementation.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    A niacin-derived coenzyme participates in making carnitine.
    primary_references
    Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10702312/ · DOI 10.1074/jbc.275.10.7390

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 18–24

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human ALDH9 compared with purified and recombinant rat enzyme. · source_derived_draft · unverified_draft

    ## l-carnitine-aldehyde-step A niacin-derived coenzyme participates in making carnitine. Expressing human ALDH9 in bacteria produced NAD+-dependent trimethylaminobutyraldehyde dehydrogenase activity, completing the aldehyde-to-gamma-butyrobetaine step. Model: Recombinant human ALDH9 compared with purified and recombinant rat enzyme. Limitations: NAD+ dependence does not establish benefit from niacin supplementation. Evidence access: Primary abstract Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10702312/ · DOI 10.1074/jbc.275.10.7390
    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