Component

Human MOCS2A C-terminal thiocarboxylate

Human MOCS2A C-terminal thiocarboxylate. Species, exposure and limitations are retained in each linked claim.

3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

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. The sulfur used to form the MPT dithiolene group is supplied from the C-terminal thiocarboxylate of the small MPT-synthase subunit.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"}
    experimental_model
    Purified human MPT synthase and patient-derived point mutants
    exposure
    Precursor Z/cPMP conversion assays
    limitations
    In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy.
    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
    MOCS2A carries a chemically attached sulfur supply.
    primary_references
    [mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
    tissue_or_cell_type
    Reconstituted MOCS2A/MOCS2B tetramers

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 404–415

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human MPT synthase and patient-derived point mutants · source_derived_draft · unverified_draft

    ### mo-mocs2a-sulfur The sulfur used to form the MPT dithiolene group is supplied from the C-terminal thiocarboxylate of the small MPT-synthase subunit. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: MOCS2A carries a chemically attached sulfur supply. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Reconstituted MOCS2A/MOCS2B tetramers experimental_model: Purified human MPT synthase and patient-derived point mutants limitations: In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy. exposure: Precursor Z/cPMP conversion assays evidence_span: {"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"} [mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. MOCS3 activates MOCS2A by adenylation followed by sulfur transfer, forming its C-terminal thiocarboxylate.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/22453920.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64", "start_char": 0, "end_char": 1267, "text_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64"}
    experimental_model
    Human-cell interaction/localization and purified-protein adenylation/sulfuration
    exposure
    MOCS2A and URM1 terminal glycine variants
    limitations
    Shared enzyme does not prove competition for sulfur in ordinary nutrient deficiency.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Homo sapiens
    plain_language
    ATP-driven activation reloads the sulfur carrier.
    primary_references
    [mo-p22453920] Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans. (2012). https://pubmed.ncbi.nlm.nih.gov/22453920/ DOI: 10.1074/jbc.m112.351429
    tissue_or_cell_type
    Cytosolic sulfur-transfer pathways

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 443–454

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human-cell interaction/localization and purified-protein adenylation/sulfuration · source_derived_draft · unverified_draft

    ### mo-mocs3-activate MOCS3 activates MOCS2A by adenylation followed by sulfur transfer, forming its C-terminal thiocarboxylate. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: ATP-driven activation reloads the sulfur carrier. organism: Homo sapiens tissue_or_cell_type: Cytosolic sulfur-transfer pathways experimental_model: Human-cell interaction/localization and purified-protein adenylation/sulfuration limitations: Shared enzyme does not prove competition for sulfur in ordinary nutrient deficiency. exposure: MOCS2A and URM1 terminal glycine variants evidence_span: {"source_cache": "artifacts/molybdenum-research/22453920.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64", "start_char": 0, "end_char": 1267, "text_sha256": "700833295a22a72be9d0ee74144bfe9249d6266c7fcba7b48330a4b2f2bf9c64"} [mo-p22453920] Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans. (2012). https://pubmed.ncbi.nlm.nih.gov/22453920/ DOI: 10.1074/jbc.m112.351429
    Complete structured claim and evidence
  2. Human MOCS2A and MOCS2B assemble as active MPT synthase and convert cPMP to molybdopterin.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"}
    experimental_model
    Purified human MPT synthase and patient-derived point mutants
    exposure
    Precursor Z/cPMP conversion assays
    limitations
    In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy.
    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
    Two sulfur atoms create the part of the scaffold that will hold molybdenum.
    primary_references
    [mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
    tissue_or_cell_type
    Reconstituted MOCS2A/MOCS2B tetramers

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 391–402

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human MPT synthase and patient-derived point mutants · source_derived_draft · unverified_draft

    ### mo-mpt-synthase Human MOCS2A and MOCS2B assemble as active MPT synthase and convert cPMP to molybdopterin. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Two sulfur atoms create the part of the scaffold that will hold molybdenum. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Reconstituted MOCS2A/MOCS2B tetramers experimental_model: Purified human MPT synthase and patient-derived point mutants limitations: In-vitro assembly and kinetic defects; severity comparisons refer to specific patients, not a universal hierarchy. exposure: Precursor Z/cPMP conversion assays evidence_span: {"source_cache": "artifacts/molybdenum-research/12732628.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319", "start_char": 0, "end_char": 1322, "text_sha256": "154da4e4528674556bef92dfe50f098cfd9ae715c06ea01fc17d64c64b8aa319"} [mo-p12732628] Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. (2003). https://pubmed.ncbi.nlm.nih.gov/12732628/ DOI: 10.1074/jbc.m303092200
    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