Component

Human molybdenum cofactor sulfurase / MOCOS

Human molybdenum cofactor sulfurase / MOCOS. Species, exposure and limitations are retained in each linked claim.

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. 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

What acts on it

  1. The purified human MOCOS NifS-like domain bound PLP and exhibited cysteine desulfurase activity.

    PLP → Human molybdenum cofactor sulfurase / MOCOS source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/34356852.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8bf3a09c4f88994cf8adc50faf391e62ac27e7572e59e6606147f2c689212d07", "start_char": 41304, "end_char": 42029, "text_sha256": "b9b02aae5eb537bdffc178ceaa33177cef6448738c19cb1a8477ad543f4e970c"}
    experimental_model
    Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay
    exposure
    PLP quantification, cysteine desulfurase assays and Moco/MPT binding
    limitations
    Human XDH C150F was functionally modeled using Arabidopsis XDH1 C161S, not purified human C150F; MOCOS assays used isolated domains.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Human genetics and human MOCOS proteins; plant XDH variant experiment separately
    plain_language
    Vitamin B6 chemistry helps supply the sulfur used to activate these molybdenum enzymes.
    primary_references
    [mo-p34356852] Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects. (2021). https://pubmed.ncbi.nlm.nih.gov/34356852/ DOI: 10.3390/biomedicines9070788
    tissue_or_cell_type
    Patient samples and purified domains

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 534–545

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay · source_derived_draft · unverified_draft

    ### mo-mocos-plp The purified human MOCOS NifS-like domain bound PLP and exhibited cysteine desulfurase activity. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamin B6 chemistry helps supply the sulfur used to activate these molybdenum enzymes. organism: Human genetics and human MOCOS proteins; plant XDH variant experiment separately tissue_or_cell_type: Patient samples and purified domains experimental_model: Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay limitations: Human XDH C150F was functionally modeled using Arabidopsis XDH1 C161S, not purified human C150F; MOCOS assays used isolated domains. exposure: PLP quantification, cysteine desulfurase assays and Moco/MPT binding evidence_span: {"source_cache": "artifacts/molybdenum-research/34356852.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8bf3a09c4f88994cf8adc50faf391e62ac27e7572e59e6606147f2c689212d07", "start_char": 41304, "end_char": 42029, "text_sha256": "b9b02aae5eb537bdffc178ceaa33177cef6448738c19cb1a8477ad543f4e970c"} [mo-p34356852] Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects. (2021). https://pubmed.ncbi.nlm.nih.gov/34356852/ DOI: 10.3390/biomedicines9070788
    Complete structured claim and evidence

  2. The Thr349Ile MOCOS N-terminal domain had severely impaired cysteine desulfurase activity, including a preparation with measurable PLP binding.

    Human MOCOS p.Thr349Ile → Human molybdenum cofactor sulfurase / MOCOS source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/34356852.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8bf3a09c4f88994cf8adc50faf391e62ac27e7572e59e6606147f2c689212d07", "start_char": 41304, "end_char": 42029, "text_sha256": "b9b02aae5eb537bdffc178ceaa33177cef6448738c19cb1a8477ad543f4e970c"}
    experimental_model
    Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay
    exposure
    PLP quantification, cysteine desulfurase assays and Moco/MPT binding
    limitations
    Human XDH C150F was functionally modeled using Arabidopsis XDH1 C161S, not purified human C150F; MOCOS assays used isolated domains.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Human genetics and human MOCOS proteins; plant XDH variant experiment separately
    plain_language
    Having some B6 cofactor bound did not repair the defective enzyme.
    primary_references
    [mo-p34356852] Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects. (2021). https://pubmed.ncbi.nlm.nih.gov/34356852/ DOI: 10.3390/biomedicines9070788
    tissue_or_cell_type
    Patient samples and purified domains
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 547–558

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay · source_derived_draft · unverified_draft

    ### mo-mocos-t349i The Thr349Ile MOCOS N-terminal domain had severely impaired cysteine desulfurase activity, including a preparation with measurable PLP binding. Condition category: machinery_impairment nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Having some B6 cofactor bound did not repair the defective enzyme. organism: Human genetics and human MOCOS proteins; plant XDH variant experiment separately tissue_or_cell_type: Patient samples and purified domains experimental_model: Xanthinuria families with recombinant human MOCOS-domain assays and a plant XDH homolog assay limitations: Human XDH C150F was functionally modeled using Arabidopsis XDH1 C161S, not purified human C150F; MOCOS assays used isolated domains. exposure: PLP quantification, cysteine desulfurase assays and Moco/MPT binding evidence_span: {"source_cache": "artifacts/molybdenum-research/34356852.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8bf3a09c4f88994cf8adc50faf391e62ac27e7572e59e6606147f2c689212d07", "start_char": 41304, "end_char": 42029, "text_sha256": "b9b02aae5eb537bdffc178ceaa33177cef6448738c19cb1a8477ad543f4e970c"} [mo-p34356852] Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects. (2021). https://pubmed.ncbi.nlm.nih.gov/34356852/ DOI: 10.3390/biomedicines9070788
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Active mARC1 and mARC2 were reconstituted with Moco without the terminal sulfuration needed by the XOR enzyme family.

    Molybdenum cofactor / Moco → Human mitochondrial amidoxime-reducing component 1 / MTARC1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/20861021.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877", "start_char": 0, "end_char": 1557, "text_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877"}
    experimental_model
    Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution
    exposure
    N-hydroxylated substrates; cofactor reconstitution
    limitations
    The 2010 paper could not identify the Mo-ligating cysteine; later structural/mutagenesis work resolves that point. Its earlier inference is not imported as current fact.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Human proteins expressed in Escherichia coli
    plain_language
    mARC does not require the extra sulfur-activation step used by XDH and AOX1.
    primary_references
    [mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. (2010). https://pubmed.ncbi.nlm.nih.gov/20861021/ DOI: 10.1074/jbc.m110.169532
    tissue_or_cell_type
    Purified enzyme system

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 976–987

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution · source_derived_draft · unverified_draft

    ### mo-marc-no-terminal-sulfur Active mARC1 and mARC2 were reconstituted with Moco without the terminal sulfuration needed by the XOR enzyme family. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: mARC does not require the extra sulfur-activation step used by XDH and AOX1. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Purified enzyme system experimental_model: Recombinant human mARC1/mARC2 biochemical and spectroscopic reconstitution limitations: The 2010 paper could not identify the Mo-ligating cysteine; later structural/mutagenesis work resolves that point. Its earlier inference is not imported as current fact. exposure: N-hydroxylated substrates; cofactor reconstitution evidence_span: {"source_cache": "artifacts/molybdenum-research/20861021.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877", "start_char": 0, "end_char": 1557, "text_sha256": "0f430936dcc4701e5d57040edcab4b0418e3c49c59620e0f7d5f54aff41e7877"} [mo-p20861021] Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. (2010). https://pubmed.ncbi.nlm.nih.gov/20861021/ DOI: 10.1074/jbc.m110.169532
    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