Component

Aldehyde dehydrogenase 1A1 / ALDH1A1

Independent protein identity; organism and experimental state are specified on individual claims.

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 ALDH1A1 oxidized all-trans-retinaldehyde to retinoic acid in comparative enzyme assays.

    Aldehyde dehydrogenase 1A1 / ALDH1A1 → All-trans-retinoic acid source_derived_draftungraded
    Experimental context and source evidence
    evidence_location
    Abstract
    experimental_model
    Side-by-side recombinant human ALDH1A1, ALDH1A2 and ALDH1A3 kinetic assays.
    exposure
    Side-by-side retinaldehyde kinetic measurements by HPLC.
    limitations
    In vitro catalytic efficiency does not specify its contribution in a particular tissue.
    nutrient_topic
    Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Homo sapiens recombinant protein
    outcome
    Human ALDH1A1 oxidized all-trans-retinaldehyde to retinoic acid in comparative enzyme assays.
    plain_language
    This independently identified enzyme supplies the acid form used for signaling.
    primary_references
    [va-pequerul-2020] Structural and kinetic features of aldehyde dehydrogenase 1A (ALDH1A) subfamily members, cancer stem cell markers active in retinoic acid biosynthesis (2020). https://pubmed.ncbi.nlm.nih.gov/31923393/ DOI: 10.1016/j.abb.2020.108256
    tissue_or_cell_type
    Cell-free enzyme

    Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 559–571

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Side-by-side recombinant human ALDH1A1, ALDH1A2 and ALDH1A3 kinetic assays. · source_derived_draft · unverified_draft

    ### va-aldh1a1-retinal-oxidation Human ALDH1A1 oxidized all-trans-retinaldehyde to retinoic acid in comparative enzyme assays. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: This independently identified enzyme supplies the acid form used for signaling. organism: Homo sapiens recombinant protein tissue_or_cell_type: Cell-free enzyme experimental_model: Side-by-side recombinant human ALDH1A1, ALDH1A2 and ALDH1A3 kinetic assays. limitations: In vitro catalytic efficiency does not specify its contribution in a particular tissue. exposure: Side-by-side retinaldehyde kinetic measurements by HPLC. outcome: Human ALDH1A1 oxidized all-trans-retinaldehyde to retinoic acid in comparative enzyme assays. evidence_location: Abstract [va-pequerul-2020] Structural and kinetic features of aldehyde dehydrogenase 1A (ALDH1A) subfamily members, cancer stem cell markers active in retinoic acid biosynthesis (2020). https://pubmed.ncbi.nlm.nih.gov/31923393/ DOI: 10.1016/j.abb.2020.108256
    Complete structured claim and evidence

What acts on it

  1. In human liver S9, AOX inhibition reduced retinoic-acid formation by 20-50%, versus 50-80% with ALDH1A1 inhibition; AOX had lower affinity and higher capacity.

    Human aldehyde oxidase 1 / AOX1 → Aldehyde dehydrogenase 1A1 / ALDH1A1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/33355213.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2", "start_char": 0, "end_char": 2211, "text_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2"}
    experimental_model
    Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification
    exposure
    Retinaldehyde with/without NAD+; selective inhibitors
    limitations
    Ex-vivo contribution depends on substrate and NAD+ availability; no dietary molybdenum intervention or universal in-vivo percentage.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Homo sapiens
    plain_language
    Different enzymes share vitamin A processing, and their contributions depend on the conditions.
    primary_references
    [mo-p33355213] Aldehyde Oxidase Contributes to All-Trans-Retinoic Acid Biosynthesis in Human Liver. (2021). https://pubmed.ncbi.nlm.nih.gov/33355213/ DOI: 10.1124/dmd.120.000296
    tissue_or_cell_type
    Purified enzyme and liver S9 fractions

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 911–922

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification · source_derived_draft · unverified_draft

    ### mo-aox-aldh-partition In human liver S9, AOX inhibition reduced retinoic-acid formation by 20-50%, versus 50-80% with ALDH1A1 inhibition; AOX had lower affinity and higher capacity. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Different enzymes share vitamin A processing, and their contributions depend on the conditions. organism: Homo sapiens tissue_or_cell_type: Purified enzyme and liver S9 fractions experimental_model: Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification limitations: Ex-vivo contribution depends on substrate and NAD+ availability; no dietary molybdenum intervention or universal in-vivo percentage. exposure: Retinaldehyde with/without NAD+; selective inhibitors evidence_span: {"source_cache": "artifacts/molybdenum-research/33355213.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2", "start_char": 0, "end_char": 2211, "text_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2"} [mo-p33355213] Aldehyde Oxidase Contributes to All-Trans-Retinoic Acid Biosynthesis in Human Liver. (2021). https://pubmed.ncbi.nlm.nih.gov/33355213/ DOI: 10.1124/dmd.120.000296
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Conditional deletion of Aldh1a1, Aldh1a2 and Aldh1a3 did not prevent fetal ovarian meiotic progression despite strongly reduced RA.

    All-trans-retinoic-acid biosynthesis → Mouse fetal ovarian meiotic progression source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    false
    experimental_model
    Three conditional deletion strategies
    exposure
    Somatic or ubiquitous Aldh1a1-3 ablation; ovarian analyses around E13.5-E16.5.
    limitations
    Minor Stra8 delay occurred; analytically zero RA from every source was not demonstrated.
    nutrient_topic
    Vitamin A expansion research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
    organism
    Mus musculus
    plain_language
    Removing the main RA-synthesis enzymes did not stop fetal ovarian meiosis.
    primary_references
    [chassot2020] Retinoic acid synthesis by ALDH1A proteins is dispensable for meiosis initiation in the mouse fetal ovary. (2020). https://pubmed.ncbi.nlm.nih.gov/32494737/ DOI: 10.1126/sciadv.aaz1261
    tissue_or_cell_type
    fetal ovary
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vitamin A expansion: reproduction, light-driven vision and shared mechanisms (2026-09-17) · lines 291–302

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Three conditional deletion strategies · source_derived_draft · unverified_draft

    ### va-repro-aldh-loss-ovarian-meiosis Conditional deletion of Aldh1a1, Aldh1a2 and Aldh1a3 did not prevent fetal ovarian meiotic progression despite strongly reduced RA. Condition category: machinery_impairment nutrient_topic: Vitamin A expansion research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing the main RA-synthesis enzymes did not stop fetal ovarian meiosis. organism: Mus musculus tissue_or_cell_type: fetal ovary experimental_model: Three conditional deletion strategies limitations: Minor Stra8 delay occurred; analytically zero RA from every source was not demonstrated. exposure: Somatic or ubiquitous Aldh1a1-3 ablation; ovarian analyses around E13.5-E16.5. cross_nutrient: false [chassot2020] Retinoic acid synthesis by ALDH1A proteins is dispensable for meiosis initiation in the mouse fetal ovary. (2020). https://pubmed.ncbi.nlm.nih.gov/32494737/ DOI: 10.1126/sciadv.aaz1261
    Complete structured claim and evidence

  2. A separable aldehyde-oxidase fraction accounted for some NAD-independent retinaldehyde metabolism in human liver and kidney extracts.

    Human aldehyde oxidase 1 / AOX1 → Hepatic retinal oxidase activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/10559215.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238", "start_char": 0, "end_char": 1879, "text_sha256": "a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238"}
    experimental_model
    Biochemical fractionation of four human livers and three kidneys
    exposure
    Retinaldehyde and other aldehyde substrate assays
    limitations
    Biochemical enzyme-fraction identification predates modern isoform assays; does not establish AOX1 as the dominant human retinoic-acid source or mineral-responsive route.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Homo sapiens
    plain_language
    AOX1 intersects vitamin A chemistry, alongside other enzymes.
    primary_references
    [mo-p10559215] Metabolism of retinaldehyde and other aldehydes in soluble extracts of human liver and kidney. (1999). https://pubmed.ncbi.nlm.nih.gov/10559215/ DOI: 10.1074/jbc.274.47.33366
    tissue_or_cell_type
    Liver and kidney soluble extracts

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 885–896

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Biochemical fractionation of four human livers and three kidneys · source_derived_draft · unverified_draft

    ### mo-aox-retinal A separable aldehyde-oxidase fraction accounted for some NAD-independent retinaldehyde metabolism in human liver and kidney extracts. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: AOX1 intersects vitamin A chemistry, alongside other enzymes. organism: Homo sapiens tissue_or_cell_type: Liver and kidney soluble extracts experimental_model: Biochemical fractionation of four human livers and three kidneys limitations: Biochemical enzyme-fraction identification predates modern isoform assays; does not establish AOX1 as the dominant human retinoic-acid source or mineral-responsive route. exposure: Retinaldehyde and other aldehyde substrate assays evidence_span: {"source_cache": "artifacts/molybdenum-research/10559215.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238", "start_char": 0, "end_char": 1879, "text_sha256": "a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238"} [mo-p10559215] Metabolism of retinaldehyde and other aldehydes in soluble extracts of human liver and kidney. (1999). https://pubmed.ncbi.nlm.nih.gov/10559215/ DOI: 10.1074/jbc.274.47.33366
    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.

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