Component

Human adenylyltransferase and sulfurtransferase / MOCS3

Human adenylyltransferase and sulfurtransferase / MOCS3. Species, exposure and limitations are retained in each linked claim.

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

    Human adenylyltransferase and sulfurtransferase / MOCS3 → Human molybdopterin synthase sulfur carrier / MOCS2A source_derived_draftungraded
    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. MOCS3 also activates URM1 by adenylation and sulfur transfer to its terminal glycine.

    Human adenylyltransferase and sulfurtransferase / MOCS3 → Human ubiquitin-related modifier / URM1 source_derived_draftungraded
    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
    The same sulfur-handling enzyme supplies a separate RNA-modification pathway.
    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 456–467

    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-urm1 MOCS3 also activates URM1 by adenylation and sulfur transfer to its terminal glycine. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same sulfur-handling enzyme supplies a separate RNA-modification pathway. 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

What acts on it

  1. Removing the terminal glycine from MOCS2A or URM1 abolished the measured interaction with MOCS3.

    Human molybdopterin synthase sulfur carrier / MOCS2A → Human adenylyltransferase and sulfurtransferase / MOCS3 source_derived_draftungraded
    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
    The sulfur handoff depends on the receiving protein having the right end.
    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 469–480

    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-terminal-glycine Removing the terminal glycine from MOCS2A or URM1 abolished the measured interaction with MOCS3. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The sulfur handoff depends on the receiving protein having the right end. 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. FRET and split-EGFP supported an NFS1-MOCS3 interaction in the cytosol of human cells.

    Human cysteine desulfurase / NFS1 → Human adenylyltransferase and sulfurtransferase / MOCS3 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/23593335.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "de38fd3acf5b473459161bd9fc6bde8a7d13d8734336d445f36938684e50711b", "start_char": 0, "end_char": 1050, "text_sha256": "de38fd3acf5b473459161bd9fc6bde8a7d13d8734336d445f36938684e50711b"}
    experimental_model
    HeLa localization/FRET and split-EGFP; purified protein complementation
    exposure
    Cell fractionation, immunodetection and protein interaction
    limitations
    Cytosolic NFS1 is distinct from assuming all NFS1 sulfur transfer happens inside mitochondria.
    nutrient_topic
    Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
    organism
    Homo sapiens; separate Neurospora crassa complementation
    plain_language
    Sulfur delivery to the molybdenum pathway also occurs outside mitochondria.
    primary_references
    [mo-p23593335] The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans. (2013). https://pubmed.ncbi.nlm.nih.gov/23593335/ DOI: 10.1371/journal.pone.0060869
    tissue_or_cell_type
    Human cytosol and purified proteins

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 378–389

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · HeLa localization/FRET and split-EGFP; purified protein complementation · source_derived_draft · unverified_draft

    ### mo-nfs1-cytosol FRET and split-EGFP supported an NFS1-MOCS3 interaction in the cytosol of human cells. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Sulfur delivery to the molybdenum pathway also occurs outside mitochondria. organism: Homo sapiens; separate Neurospora crassa complementation tissue_or_cell_type: Human cytosol and purified proteins experimental_model: HeLa localization/FRET and split-EGFP; purified protein complementation limitations: Cytosolic NFS1 is distinct from assuming all NFS1 sulfur transfer happens inside mitochondria. exposure: Cell fractionation, immunodetection and protein interaction evidence_span: {"source_cache": "artifacts/molybdenum-research/23593335.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "de38fd3acf5b473459161bd9fc6bde8a7d13d8734336d445f36938684e50711b", "start_char": 0, "end_char": 1050, "text_sha256": "de38fd3acf5b473459161bd9fc6bde8a7d13d8734336d445f36938684e50711b"} [mo-p23593335] The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans. (2013). https://pubmed.ncbi.nlm.nih.gov/23593335/ DOI: 10.1371/journal.pone.0060869
    Complete structured claim and evidence

  3. Purified NFS1 interacted specifically with MOCS3-RLD and supported sulfur transfer to it.

    Human NFS1 sulfur-loaded persulfide state → Human adenylyltransferase and sulfurtransferase / MOCS3 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/18650437.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50", "start_char": 0, "end_char": 1547, "text_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50"}
    experimental_model
    Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays
    exposure
    L-cysteine sulfur-donor assays
    limitations
    Truncated and heterologously expressed proteins; cell localization was investigated independently in 2013.
    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
    The sulfur handoff uses identifiable proteins, not a free-floating mineral pool.
    primary_references
    [mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200
    tissue_or_cell_type
    Purified proteins

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 365–376

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays · source_derived_draft · unverified_draft

    ### mo-nfs1-mocs3-transfer Purified NFS1 interacted specifically with MOCS3-RLD and supported sulfur transfer to it. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The sulfur handoff uses identifiable proteins, not a free-floating mineral pool. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Purified proteins experimental_model: Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays limitations: Truncated and heterologously expressed proteins; cell localization was investigated independently in 2013. exposure: L-cysteine sulfur-donor assays evidence_span: {"source_cache": "artifacts/molybdenum-research/18650437.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50", "start_char": 0, "end_char": 1547, "text_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50"} [mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Human NFS1 transferred sulfur from L-cysteine through an NFS1-bound persulfide intermediate to the rhodanese-like domain of MOCS3.

    Human cysteine desulfurase / NFS1 → L-Cysteine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/molybdenum-research/18650437.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50", "start_char": 0, "end_char": 1547, "text_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50"}
    experimental_model
    Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays
    exposure
    L-cysteine sulfur-donor assays
    limitations
    Truncated and heterologously expressed proteins; cell localization was investigated independently in 2013.
    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
    Cysteine supplies sulfur that becomes part of the molybdenum cofactor.
    primary_references
    [mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200
    tissue_or_cell_type
    Purified proteins

    Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 352–363

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays · source_derived_draft · unverified_draft

    ### mo-nfs1-sulfur Human NFS1 transferred sulfur from L-cysteine through an NFS1-bound persulfide intermediate to the rhodanese-like domain of MOCS3. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Cysteine supplies sulfur that becomes part of the molybdenum cofactor. organism: Human proteins expressed in Escherichia coli tissue_or_cell_type: Purified proteins experimental_model: Purified human NFS1/ISD11 and MOCS3 rhodanese-domain interaction and sulfur-transfer assays limitations: Truncated and heterologously expressed proteins; cell localization was investigated independently in 2013. exposure: L-cysteine sulfur-donor assays evidence_span: {"source_cache": "artifacts/molybdenum-research/18650437.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50", "start_char": 0, "end_char": 1547, "text_sha256": "8180bd148722e8980ef5acbd4ae4c29a0d9d13da56bbccb91165a5eed4ab6f50"} [mo-p18650437] A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. (2008). https://pubmed.ncbi.nlm.nih.gov/18650437/ DOI: 10.1074/jbc.m804064200
    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