Component

Antiquitin / ALDH7A1

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

7 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 recombinant human ALDH7A1 metabolized betaine aldehyde.

    Antiquitin / ALDH7A1 → Betaine aldehyde source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/choline-research/20207735.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "510558afae2825079b269c8a4ee3f16114ab8d7f6c357c1a085ec14f1924e5e5", "start_char": 0, "end_char": 1582, "text_sha256": "510558afae2825079b269c8a4ee3f16114ab8d7f6c357c1a085ec14f1924e5e5"}
    experimental_model
    Purified recombinant human enzyme and CHO-cell expression
    exposure
    Betaine aldehyde substrate; increased extracellular sucrose or NaCl
    limitations
    ALDH7A1 accepts several aldehydes. Cell protection was not proved to be mediated exclusively by betaine or to predict benefit in pyridoxine-dependent epilepsy.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Human ALDH7A1; Chinese hamster ovary expression host
    plain_language
    The lysine-pathway enzyme already in the ledger also has activity on a choline-derived aldehyde.
    primary_references
    [choline-p20207735] Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress. (2010). https://pubmed.ncbi.nlm.nih.gov/20207735/ DOI: 10.1074/jbc.m109.077925
    tissue_or_cell_type
    Purified enzyme and osmotic-stress cell assays

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 633–644

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

    ### choline-aldh7-betaine Purified recombinant human ALDH7A1 metabolized betaine aldehyde. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: The lysine-pathway enzyme already in the ledger also has activity on a choline-derived aldehyde. organism: Human ALDH7A1; Chinese hamster ovary expression host tissue_or_cell_type: Purified enzyme and osmotic-stress cell assays experimental_model: Purified recombinant human enzyme and CHO-cell expression limitations: ALDH7A1 accepts several aldehydes. Cell protection was not proved to be mediated exclusively by betaine or to predict benefit in pyridoxine-dependent epilepsy. exposure: Betaine aldehyde substrate; increased extracellular sucrose or NaCl evidence_span: {"source_cache": "artifacts/choline-research/20207735.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "510558afae2825079b269c8a4ee3f16114ab8d7f6c357c1a085ec14f1924e5e5", "start_char": 0, "end_char": 1582, "text_sha256": "510558afae2825079b269c8a4ee3f16114ab8d7f6c357c1a085ec14f1924e5e5"} [choline-p20207735] Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress. (2010). https://pubmed.ncbi.nlm.nih.gov/20207735/ DOI: 10.1074/jbc.m109.077925
    Complete structured claim and evidence

  2. Human ALDH7A1 expression attenuated apoptosis caused by high extracellular sucrose or sodium chloride in CHO cells.

    Antiquitin / ALDH7A1 → Hyperosmotic apoptosis in CHO cells expressing human ALDH7A1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/choline-research/20207735.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "510558afae2825079b269c8a4ee3f16114ab8d7f6c357c1a085ec14f1924e5e5", "start_char": 0, "end_char": 1582, "text_sha256": "510558afae2825079b269c8a4ee3f16114ab8d7f6c357c1a085ec14f1924e5e5"}
    experimental_model
    Purified recombinant human enzyme and CHO-cell expression
    exposure
    Betaine aldehyde substrate; increased extracellular sucrose or NaCl
    limitations
    The enzyme also detoxifies other aldehydes; betaine is a proposed contributor, not an isolated mediator in this endpoint.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Human ALDH7A1; Chinese hamster ovary expression host
    plain_language
    The enzyme protected these cells during osmotic stress.
    primary_references
    [choline-p20207735] Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress. (2010). https://pubmed.ncbi.nlm.nih.gov/20207735/ DOI: 10.1074/jbc.m109.077925
    tissue_or_cell_type
    Purified enzyme and osmotic-stress cell assays

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 646–657

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

    ### choline-aldh7-osmotic Human ALDH7A1 expression attenuated apoptosis caused by high extracellular sucrose or sodium chloride in CHO cells. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme protected these cells during osmotic stress. organism: Human ALDH7A1; Chinese hamster ovary expression host tissue_or_cell_type: Purified enzyme and osmotic-stress cell assays experimental_model: Purified recombinant human enzyme and CHO-cell expression limitations: The enzyme also detoxifies other aldehydes; betaine is a proposed contributor, not an isolated mediator in this endpoint. exposure: Betaine aldehyde substrate; increased extracellular sucrose or NaCl evidence_span: {"source_cache": "artifacts/choline-research/20207735.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "510558afae2825079b269c8a4ee3f16114ab8d7f6c357c1a085ec14f1924e5e5", "start_char": 0, "end_char": 1582, "text_sha256": "510558afae2825079b269c8a4ee3f16114ab8d7f6c357c1a085ec14f1924e5e5"} [choline-p20207735] Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress. (2010). https://pubmed.ncbi.nlm.nih.gov/20207735/ DOI: 10.1074/jbc.m109.077925
    Complete structured claim and evidence

  3. ALDH7A1 deficiency reduces aldehyde clearance, increasing AASA and its equilibrium partner P6C.

    Antiquitin / ALDH7A1 → alpha-Aminoadipate semialdehyde source_derived_draftungraded
    Experimental context and source evidence
    affected_machinery
    ALDH7A1
    availability_state
    machinery_impairment Imported condition classification; unverified.
    deficiency_not_equivalent
    Dietary lysine deficiency
    experimental_model
    Human patient biochemical and genetic evidence
    limitations
    Inherited enzyme failure is distinct from inadequate lysine intake.
    organism
    Homo sapiens
    plain_language
    An enzyme block allows reactive lysine metabolites to accumulate.
    primary_references
    [mills2006] Mutations in antiquitin in individuals with pyridoxine-dependent seizures. (2006). https://pubmed.ncbi.nlm.nih.gov/16491085/ DOI: 10.1038/nm1366
    tissue_or_cell_type
    Affected tissues and body fluids
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 254–264

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human patient biochemical and genetic evidence · source_derived_draft · unverified_draft

    ### aldh7a1-metabolite-accumulation ALDH7A1 deficiency reduces aldehyde clearance, increasing AASA and its equilibrium partner P6C. Plain language: An enzyme block allows reactive lysine metabolites to accumulate. Condition category: machinery_impairment organism: Homo sapiens tissue_or_cell_type: Affected tissues and body fluids experimental_model: Human patient biochemical and genetic evidence limitations: Inherited enzyme failure is distinct from inadequate lysine intake. affected_machinery: ALDH7A1 deficiency_not_equivalent: Dietary lysine deficiency [mills2006] Mutations in antiquitin in individuals with pyridoxine-dependent seizures. (2006). https://pubmed.ncbi.nlm.nih.gov/16491085/ DOI: 10.1038/nm1366
    Complete structured claim and evidence

What acts on it

  1. ALDH7A1 variants identified in affected children abolished antiquitin activity in the reported functional assays.

    Biallelic ALDH7A1 disease genotypes studied by Mills 2006 → Antiquitin / ALDH7A1 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    Lysine catabolic machinery can impair intracellular B6 availability.
    experimental_model
    Affected children, expressed human ALDH7A1 variants and metabolite chemistry
    exposure
    Disease-variant functional expression.
    limitations
    Applies to the studied variants; not all possible ALDH7A1 alleles.
    nutrient_topic
    Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
    organism
    Homo sapiens
    plain_language
    The inherited defect blocks a lysine-breakdown enzyme.
    primary_references
    [mills-2006-aldh7a1] Mutations in antiquitin in individuals with pyridoxine-dependent seizures (2006). https://doi.org/10.1038/nm1366 DOI: 10.1038/nm1366
    tissue_or_cell_type
    Patient-linked expression experiments
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1145–1156

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Affected children, expressed human ALDH7A1 variants and metabolite chemistry · source_derived_draft · unverified_draft

    ### b6-neuro-aldh7a1-variants ALDH7A1 variants identified in affected children abolished antiquitin activity in the reported functional assays. Condition category: machinery_impairment nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The inherited defect blocks a lysine-breakdown enzyme. organism: Homo sapiens tissue_or_cell_type: Patient-linked expression experiments experimental_model: Affected children, expressed human ALDH7A1 variants and metabolite chemistry limitations: Applies to the studied variants; not all possible ALDH7A1 alleles. exposure: Disease-variant functional expression. cross_nutrient: Lysine catabolic machinery can impair intracellular B6 availability. [mills-2006-aldh7a1] Mutations in antiquitin in individuals with pyridoxine-dependent seizures (2006). https://doi.org/10.1038/nm1366 DOI: 10.1038/nm1366
    Complete structured claim and evidence

  2. Elevated AASA was observed in an 18-patient PDE cohort with ALDH7A1 investigation, including during pyridoxine treatment.

    alpha-Aminoadipate semialdehyde → Antiquitin / ALDH7A1 source_derived_draftungraded
    Experimental context and source evidence
    affected_machinery
    ALDH7A1 under investigation
    availability_state
    biomarker_context Imported condition classification; unverified.
    deficiency_not_equivalent
    Dietary lysine deficiency
    experimental_model
    Human clinical cohort; plasma and urine assays
    limitations
    A biomarker is not itself a diagnosis or proof of dietary lysine deficiency.
    organism
    Homo sapiens
    plain_language
    AASA measurement can reveal disturbed lysine breakdown.
    primary_references
    [plecko2007] Biochemical and molecular characterization of 18 patients with pyridoxine-dependent epilepsy and mutations of the antiquitin (ALDH7A1) gene (2007). https://pubmed.ncbi.nlm.nih.gov/17068770/ DOI: 10.1002/humu.20433
    tissue_or_cell_type
    Plasma and urine
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 324–334

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human clinical cohort; plasma and urine assays · source_derived_draft · unverified_draft

    ### aasa-pde-biomarker Elevated AASA was observed in an 18-patient PDE cohort with ALDH7A1 investigation, including during pyridoxine treatment. Plain language: AASA measurement can reveal disturbed lysine breakdown. Condition category: biomarker_context organism: Homo sapiens tissue_or_cell_type: Plasma and urine experimental_model: Human clinical cohort; plasma and urine assays limitations: A biomarker is not itself a diagnosis or proof of dietary lysine deficiency. affected_machinery: ALDH7A1 under investigation deficiency_not_equivalent: Dietary lysine deficiency [plecko2007] Biochemical and molecular characterization of 18 patients with pyridoxine-dependent epilepsy and mutations of the antiquitin (ALDH7A1) gene (2007). https://pubmed.ncbi.nlm.nih.gov/17068770/ DOI: 10.1002/humu.20433
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Children with pyridoxine-dependent seizures have mutations in the ALDH7A1 gene which encodes antiquitin, these mutations abolish the activity of antiquitin as a delta-1-piperideine-6-carboxylate to alpha-aminoadipic semialdehyde dehydrogenase, the accumulating delta-1-piperideine-6-carboxylate inactivates pyridoxal 5-phosphate by forming a Knoevenagel condensation product, and measurement of urinary alpha-aminoadipic semialdehyde provides a simple way of confirming the diagnosis.

    Delta-1-piperideine-6-carboxylate → PLP source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/gaba-research/16491085.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "da61b07cc71e16803fe09321738c7a6c8d2cbac0dff2b189b9f2586ce5950bfa", "start_char": 0, "end_char": 550, "text_sha256": "da61b07cc71e16803fe09321738c7a6c8d2cbac0dff2b189b9f2586ce5950bfa"}
    experimental_model
    Gene analysis and metabolite measurement in children with pyridoxine-dependent seizures
    exposure
    Naturally occurring ALDH7A1 mutations abolishing antiquitin dehydrogenase activity
    limitations
    Human genetics with a defined biochemical consequence. It establishes the chemistry of the cofactor loss; it does not measure brain GABA in the affected children.
    nutrient_topic
    GABA research collection; topical membership is not evidence of a direct clinical effect, and the sign of a GABA response depends on the chloride gradient of the cell it was measured in. · Gamma-aminobutyric acid
    organism
    Human
    plain_language
    A metabolite that piles up when one enzyme is missing chemically destroys the cofactor a different enzyme needs.
    primary_references
    [gb-p16491085] Mutations in antiquitin in individuals with pyridoxine-dependent seizures. (2006). https://pubmed.ncbi.nlm.nih.gov/16491085/ DOI: 10.1038/nm1366
    tissue_or_cell_type
    Whole body
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    GABA: a ligand with no sign of its own, the cofactor that limits its synthesis, the barrier that keeps it out of the brain, and the immune settings where the same molecule protects and harms (2026-09-22) · lines 118–129

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Gene analysis and metabolite measurement in children with pyridoxine-dependent seizures · source_derived_draft · unverified_draft

    ### gb-a-metabolite-destroys-the-cofactor Children with pyridoxine-dependent seizures have mutations in the ALDH7A1 gene which encodes antiquitin, these mutations abolish the activity of antiquitin as a delta-1-piperideine-6-carboxylate to alpha-aminoadipic semialdehyde dehydrogenase, the accumulating delta-1-piperideine-6-carboxylate inactivates pyridoxal 5-phosphate by forming a Knoevenagel condensation product, and measurement of urinary alpha-aminoadipic semialdehyde provides a simple way of confirming the diagnosis. Condition category: machinery_impairment nutrient_topic: GABA research collection; topical membership is not evidence of a direct clinical effect, and the sign of a GABA response depends on the chloride gradient of the cell it was measured in. plain_language: A metabolite that piles up when one enzyme is missing chemically destroys the cofactor a different enzyme needs. organism: Human tissue_or_cell_type: Whole body experimental_model: Gene analysis and metabolite measurement in children with pyridoxine-dependent seizures limitations: Human genetics with a defined biochemical consequence. It establishes the chemistry of the cofactor loss; it does not measure brain GABA in the affected children. exposure: Naturally occurring ALDH7A1 mutations abolishing antiquitin dehydrogenase activity evidence_span: {"source_cache": "artifacts/gaba-research/16491085.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "da61b07cc71e16803fe09321738c7a6c8d2cbac0dff2b189b9f2586ce5950bfa", "start_char": 0, "end_char": 550, "text_sha256": "da61b07cc71e16803fe09321738c7a6c8d2cbac0dff2b189b9f2586ce5950bfa"} [gb-p16491085] Mutations in antiquitin in individuals with pyridoxine-dependent seizures. (2006). https://pubmed.ncbi.nlm.nih.gov/16491085/ DOI: 10.1038/nm1366
    Complete structured claim and evidence

  2. ALDH7A1 oxidizes alpha-aminoadipate semialdehyde to alpha-aminoadipate using NAD+.

    alpha-Aminoadipate semialdehyde → L-alpha-Aminoadipate source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human ALDH7A1 biochemical and genetic study
    limitations
    Compartmental isoform distribution is not resolved by this claim.
    organism
    Homo sapiens
    plain_language
    Antiquitin clears the aldehyde intermediate.
    primary_references
    [luo2015] Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1 (2015). https://pubmed.ncbi.nlm.nih.gov/26260980/ DOI: 10.1021/acs.biochem.5b00754
    tissue_or_cell_type
    Lysine-catabolizing tissues

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 104–112

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human ALDH7A1 biochemical and genetic study · source_derived_draft · unverified_draft

    ### aldh7a1-oxidation ALDH7A1 oxidizes alpha-aminoadipate semialdehyde to alpha-aminoadipate using NAD+. Plain language: Antiquitin clears the aldehyde intermediate. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Lysine-catabolizing tissues experimental_model: Human ALDH7A1 biochemical and genetic study limitations: Compartmental isoform distribution is not resolved by this claim. [luo2015] Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1 (2015). https://pubmed.ncbi.nlm.nih.gov/26260980/ DOI: 10.1021/acs.biochem.5b00754
    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