Component

Terminal-sulfido molybdenum cofactor for XDH and AOX1

Terminal-sulfido molybdenum cofactor for XDH and AOX1. Species, exposure and limitations are retained in each linked claim.

2 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

Where it participates (unsigned role)

  1. MOCOS defects in type II xanthinuria support its role in supplying the terminal sulfur required by XDH and AOX1.

    Human molybdenum cofactor sulfurase / MOCOS → Human xanthine oxidoreductase / XDH source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/11302742.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3", "start_char": 0, "end_char": 1011, "text_sha256": "8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3"}
    experimental_model
    Gene identification in two type II xanthinuria patients and comparison subjects
    exposure
    MOCOS Arg419 stop mutation
    limitations
    Genetic evidence for terminal sulfuration; type II xanthinuria is different from loss of all Moco synthesis.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Homo sapiens
    plain_language
    Two molybdenum enzymes need an additional sulfur-activation step.
    primary_references
    [mo-p11302742] Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. (2001). https://pubmed.ncbi.nlm.nih.gov/11302742/ DOI: 10.1006/bbrc.2001.4719
    tissue_or_cell_type
    Liver cDNA and patient genetics

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 521–532

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Gene identification in two type II xanthinuria patients and comparison subjects · source_derived_draft · unverified_draft

    ### mo-mocos-sulfuration MOCOS defects in type II xanthinuria support its role in supplying the terminal sulfur required by XDH and AOX1. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Two molybdenum enzymes need an additional sulfur-activation step. organism: Homo sapiens tissue_or_cell_type: Liver cDNA and patient genetics experimental_model: Gene identification in two type II xanthinuria patients and comparison subjects limitations: Genetic evidence for terminal sulfuration; type II xanthinuria is different from loss of all Moco synthesis. exposure: MOCOS Arg419 stop mutation evidence_span: {"source_cache": "artifacts/molybdenum-research/11302742.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3", "start_char": 0, "end_char": 1011, "text_sha256": "8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3"} [mo-p11302742] Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. (2001). https://pubmed.ncbi.nlm.nih.gov/11302742/ DOI: 10.1006/bbrc.2001.4719
    Complete structured claim and evidence

  2. Recombinant human XDH/XOR catalyzed conversion of xanthine to urate.

    Human xanthine oxidoreductase / XDH → Xanthine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"}
    experimental_model
    Recombinant human XDH variants with urate, superoxide and NO assays
    exposure
    Xanthine, oxygen and inorganic nitrite assays
    limitations
    The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Homo sapiens protein
    plain_language
    The purine-breakdown pathway uses a molybdenum enzyme to make urate.
    primary_references
    [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
    tissue_or_cell_type
    Purified human enzyme

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 742–753

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human XDH variants with urate, superoxide and NO assays · source_derived_draft · unverified_draft

    ### mo-xdh-xanthine Recombinant human XDH/XOR catalyzed conversion of xanthine to urate. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The purine-breakdown pathway uses a molybdenum enzyme to make urate. organism: Homo sapiens protein tissue_or_cell_type: Purified human enzyme experimental_model: Recombinant human XDH variants with urate, superoxide and NO assays limitations: The 2023 Fig. 6E corrigendum corrects a displayed panel; authors state data and conclusions are unchanged. Enzyme activity is not a clinical benefit or dietary response. exposure: Xanthine, oxygen and inorganic nitrite assays evidence_span: {"source_cache": "artifacts/molybdenum-research/37713777.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9", "start_char": 0, "end_char": 1655, "text_sha256": "30e93ea24784120403bef1dfe72cf46411f1af88946b9cc1cba3d4c45a367bf9"} [mo-p37713777] Natural mutations of human XDH promote the nitrite (NO2-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health? (2023). https://pubmed.ncbi.nlm.nih.gov/37713777/ DOI: 10.1016/j.redox.2023.102864
    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