Component

Human molybdenum cofactor synthesis protein MOCS1A

Human molybdenum cofactor synthesis protein MOCS1A. Species, exposure and limitations are retained in each linked claim.

5 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. MOCS1A contains a redox-active N-terminal [4Fe-4S] cluster coordinated by the conserved radical-SAM cysteine motif.

    Human molybdenum cofactor synthesis protein MOCS1A → S-Adenosyl-L-methionine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/15180982.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097", "start_char": 0, "end_char": 1828, "text_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097"}
    experimental_model
    Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods
    exposure
    Aerobic versus anaerobic purification; iron-sulfur reconstitution
    limitations
    The human protein study characterized clusters and essential cysteines; no human methylation-cycle depletion or clinical SAM requirement was measured.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Human protein expressed in Escherichia coli
    plain_language
    SAM participates in radical chemistry here; this is a different use from donating a methyl group to DNA.
    primary_references
    [mo-p15180982] Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. (2004). https://pubmed.ncbi.nlm.nih.gov/15180982/ DOI: 10.1074/jbc.m313398200
    tissue_or_cell_type
    Purified protein and bacterial complementation

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 326–337

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods · source_derived_draft · unverified_draft

    ### mo-mocs1a-radical-sam MOCS1A contains a redox-active N-terminal [4Fe-4S] cluster coordinated by the conserved radical-SAM cysteine motif. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: SAM participates in radical chemistry here; this is a different use from donating a methyl group to DNA. organism: Human protein expressed in Escherichia coli tissue_or_cell_type: Purified protein and bacterial complementation experimental_model: Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods limitations: The human protein study characterized clusters and essential cysteines; no human methylation-cycle depletion or clinical SAM requirement was measured. exposure: Aerobic versus anaerobic purification; iron-sulfur reconstitution evidence_span: {"source_cache": "artifacts/molybdenum-research/15180982.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097", "start_char": 0, "end_char": 1828, "text_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097"} [mo-p15180982] Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. (2004). https://pubmed.ncbi.nlm.nih.gov/15180982/ DOI: 10.1074/jbc.m313398200
    Complete structured claim and evidence

  2. Exon 1a targeted type I MOCS1A to the mitochondrial matrix, whereas exon 1b variants remained cytosolic.

    Human molybdenum cofactor synthesis protein MOCS1A → Human MOCS1A-MOCS1B cPMP synthesis system source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/31996372.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7", "start_char": 0, "end_char": 1846, "text_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7"}
    experimental_model
    Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins
    exposure
    Type I-III MOCS1 splice constructs
    limitations
    Localization and processing experiments; no dietary iron, SAM or molybdenum intervention.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Homo sapiens
    plain_language
    Splicing changes where the first assembly protein goes.
    primary_references
    [mo-p31996372] Alternative splicing of the bicistronic gene molybdenum cofactor synthesis 1 (MOCS1) uncovers a novel mitochondrial protein maturation mechanism. (2020). https://pubmed.ncbi.nlm.nih.gov/31996372/ DOI: 10.1074/jbc.ra119.010720
    tissue_or_cell_type
    Transfected human-cell localization and mitochondrial matrix

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 287–298

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins · source_derived_draft · unverified_draft

    ### mo-mocs1a-targeting Exon 1a targeted type I MOCS1A to the mitochondrial matrix, whereas exon 1b variants remained cytosolic. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Splicing changes where the first assembly protein goes. organism: Homo sapiens tissue_or_cell_type: Transfected human-cell localization and mitochondrial matrix experimental_model: Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins limitations: Localization and processing experiments; no dietary iron, SAM or molybdenum intervention. exposure: Type I-III MOCS1 splice constructs evidence_span: {"source_cache": "artifacts/molybdenum-research/31996372.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7", "start_char": 0, "end_char": 1846, "text_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7"} [mo-p31996372] Alternative splicing of the bicistronic gene molybdenum cofactor synthesis 1 (MOCS1) uncovers a novel mitochondrial protein maturation mechanism. (2020). https://pubmed.ncbi.nlm.nih.gov/31996372/ DOI: 10.1074/jbc.ra119.010720
    Complete structured claim and evidence

What acts on it

  1. Anaerobic reconstitution yielded human MOCS1A containing two [4Fe-4S] clusters.

    [4Fe-4S] iron-sulfur cluster → Human molybdenum cofactor synthesis protein MOCS1A source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/15180982.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097", "start_char": 0, "end_char": 1828, "text_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097"}
    experimental_model
    Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods
    exposure
    Aerobic versus anaerobic purification; iron-sulfur reconstitution
    limitations
    Cluster states depend on preparation and oxygen exposure; the paper does not demonstrate a dietary iron or methyl-donor threshold.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Human protein expressed in Escherichia coli
    plain_language
    Molybdenum-cofactor assembly itself requires iron-sulfur machinery.
    primary_references
    [mo-p15180982] Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. (2004). https://pubmed.ncbi.nlm.nih.gov/15180982/ DOI: 10.1074/jbc.m313398200
    tissue_or_cell_type
    Purified protein and bacterial complementation

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 313–324

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods · source_derived_draft · unverified_draft

    ### mo-mocs1a-fes Anaerobic reconstitution yielded human MOCS1A containing two [4Fe-4S] clusters. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Molybdenum-cofactor assembly itself requires iron-sulfur machinery. organism: Human protein expressed in Escherichia coli tissue_or_cell_type: Purified protein and bacterial complementation experimental_model: Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods limitations: Cluster states depend on preparation and oxygen exposure; the paper does not demonstrate a dietary iron or methyl-donor threshold. exposure: Aerobic versus anaerobic purification; iron-sulfur reconstitution evidence_span: {"source_cache": "artifacts/molybdenum-research/15180982.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097", "start_char": 0, "end_char": 1828, "text_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097"} [mo-p15180982] Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. (2004). https://pubmed.ncbi.nlm.nih.gov/15180982/ DOI: 10.1074/jbc.m313398200
    Complete structured claim and evidence

  2. Oxygen rapidly degraded both reconstituted MOCS1A [4Fe-4S] clusters, producing different semistable cluster intermediates.

    Molecular oxygen → Human molybdenum cofactor synthesis protein MOCS1A source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/15180982.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097", "start_char": 0, "end_char": 1828, "text_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097"}
    experimental_model
    Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods
    exposure
    Aerobic versus anaerobic purification; iron-sulfur reconstitution
    limitations
    Purified protein exposure; not evidence that normal breathing causes cofactor deficiency.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Human protein expressed in Escherichia coli
    plain_language
    The assembly protein contains oxygen-sensitive clusters.
    primary_references
    [mo-p15180982] Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. (2004). https://pubmed.ncbi.nlm.nih.gov/15180982/ DOI: 10.1074/jbc.m313398200
    tissue_or_cell_type
    Purified protein and bacterial complementation

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 339–350

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods · source_derived_draft · unverified_draft

    ### mo-mocs1a-oxygen Oxygen rapidly degraded both reconstituted MOCS1A [4Fe-4S] clusters, producing different semistable cluster intermediates. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The assembly protein contains oxygen-sensitive clusters. organism: Human protein expressed in Escherichia coli tissue_or_cell_type: Purified protein and bacterial complementation experimental_model: Recombinant human MOCS1A, cysteine mutagenesis and multiple spectroscopic methods limitations: Purified protein exposure; not evidence that normal breathing causes cofactor deficiency. exposure: Aerobic versus anaerobic purification; iron-sulfur reconstitution evidence_span: {"source_cache": "artifacts/molybdenum-research/15180982.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097", "start_char": 0, "end_char": 1828, "text_sha256": "722c11f1c29a720fb7105f37962af2652ce95b6734afdb59d675dee0b8302097"} [mo-p15180982] Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. (2004). https://pubmed.ncbi.nlm.nih.gov/15180982/ DOI: 10.1074/jbc.m313398200
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. MOCS1A and MOCS1B jointly support conversion of GTP to cPMP, the first intermediate of human Moco synthesis.

    Human MOCS1A-MOCS1B cPMP synthesis system → Cyclic pyranopterin monophosphate / cPMP source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/31996372.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7", "start_char": 0, "end_char": 1846, "text_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7"}
    experimental_model
    Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins
    exposure
    Type I-III MOCS1 splice constructs
    limitations
    Localization and processing experiments; no dietary iron, SAM or molybdenum intervention.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Homo sapiens
    plain_language
    The cofactor scaffold is built from GTP before molybdenum is inserted.
    primary_references
    [mo-p31996372] Alternative splicing of the bicistronic gene molybdenum cofactor synthesis 1 (MOCS1) uncovers a novel mitochondrial protein maturation mechanism. (2020). https://pubmed.ncbi.nlm.nih.gov/31996372/ DOI: 10.1074/jbc.ra119.010720
    tissue_or_cell_type
    Transfected human-cell localization and mitochondrial matrix

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 274–285

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins · source_derived_draft · unverified_draft

    ### mo-mocs1-cpmp MOCS1A and MOCS1B jointly support conversion of GTP to cPMP, the first intermediate of human Moco synthesis. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cofactor scaffold is built from GTP before molybdenum is inserted. organism: Homo sapiens tissue_or_cell_type: Transfected human-cell localization and mitochondrial matrix experimental_model: Alternative splicing, fluorescence microscopy, fractionation and mitochondrial targeting of human MOCS1 proteins limitations: Localization and processing experiments; no dietary iron, SAM or molybdenum intervention. exposure: Type I-III MOCS1 splice constructs evidence_span: {"source_cache": "artifacts/molybdenum-research/31996372.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7", "start_char": 0, "end_char": 1846, "text_sha256": "a88a2e2c4aae83293fa6f1860d10bb41b41c32d1ad79b0b04cd5dd3eb02865c7"} [mo-p31996372] Alternative splicing of the bicistronic gene molybdenum cofactor synthesis 1 (MOCS1) uncovers a novel mitochondrial protein maturation mechanism. (2020). https://pubmed.ncbi.nlm.nih.gov/31996372/ DOI: 10.1074/jbc.ra119.010720
    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