Component

Protein-derived topaquinone / TPQ cofactor

Protein-derived topaquinone / TPQ cofactor. 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

What acts on it

  1. Human AOC1 has one copper ion and a tyrosine-derived topaquinone in each of its two active sites.

    Human diamine oxidase / AOC1 / DAO → Protein-derived topaquinone / TPQ cofactor source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/copper-research/19764817.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9a01d0dba5caec8a33a77fdbe7190d7a05bdd6e691a570a890eb6b19d4c692b6", "start_char": 0, "end_char": 1343, "text_sha256": "9a01d0dba5caec8a33a77fdbe7190d7a05bdd6e691a570a890eb6b19d4c692b6"}
    experimental_model
    Crystallography of recombinant human diamine oxidase and inhibitor complexes
    exposure
    Native structure and inhibitor binding
    limitations
    Copper/TPQ dependence is molecular evidence, not a trial of copper for histamine intolerance; DAO activity can have multiple determinants.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Human AOC1 expressed in insect cells
    plain_language
    Histamine-processing machinery includes both a metal and a protein-derived cofactor.
    primary_references
    [copper-p19764817] Structure and inhibition of human diamine oxidase. (2009). https://pubmed.ncbi.nlm.nih.gov/19764817/ DOI: 10.1021/bi9014192
    tissue_or_cell_type
    Purified protein

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 1014–1025

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystallography of recombinant human diamine oxidase and inhibitor complexes · source_derived_draft · unverified_draft

    ### copper-aoc1-copper-tpq Human AOC1 has one copper ion and a tyrosine-derived topaquinone in each of its two active sites. Condition category: normal nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: Histamine-processing machinery includes both a metal and a protein-derived cofactor. organism: Human AOC1 expressed in insect cells tissue_or_cell_type: Purified protein experimental_model: Crystallography of recombinant human diamine oxidase and inhibitor complexes limitations: Copper/TPQ dependence is molecular evidence, not a trial of copper for histamine intolerance; DAO activity can have multiple determinants. exposure: Native structure and inhibitor binding evidence_span: {"source_cache": "artifacts/copper-research/19764817.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9a01d0dba5caec8a33a77fdbe7190d7a05bdd6e691a570a890eb6b19d4c692b6", "start_char": 0, "end_char": 1343, "text_sha256": "9a01d0dba5caec8a33a77fdbe7190d7a05bdd6e691a570a890eb6b19d4c692b6"} [copper-p19764817] Structure and inhibition of human diamine oxidase. (2009). https://pubmed.ncbi.nlm.nih.gov/19764817/ DOI: 10.1021/bi9014192
    Complete structured claim and evidence

  2. The human AOC3 structure contained an active-site copper ion and TPQ in its active off-copper conformation.

    Human copper amine oxidase AOC3 / vascular adhesion protein 1 / VAP-1 → Protein-derived topaquinone / TPQ cofactor source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/copper-research/16239734.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "24ea102446aeff31a53b9302d191c0bc572100f8ee82b6ccb1a665432151662b", "start_char": 0, "end_char": 1408, "text_sha256": "24ea102446aeff31a53b9302d191c0bc572100f8ee82b6ccb1a665432151662b"}
    experimental_model
    X-ray structures of soluble human VAP-1 and inhibitor complex
    exposure
    Native and inhibitor-bound structure
    limitations
    Soluble protein structure; proposed gate and adhesion-motif functions are not proven clinical effects of copper intake.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Human protein
    plain_language
    A separate copper amine oxidase has its own catalytic arrangement.
    primary_references
    [copper-p16239734] Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1. (2005). https://pubmed.ncbi.nlm.nih.gov/16239734/ DOI: 10.1107/s0907444905028805
    tissue_or_cell_type
    Purified truncated soluble AOC3

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 1040–1051

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray structures of soluble human VAP-1 and inhibitor complex · source_derived_draft · unverified_draft

    ### copper-aoc3-copper-tpq The human AOC3 structure contained an active-site copper ion and TPQ in its active off-copper conformation. Condition category: normal nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: A separate copper amine oxidase has its own catalytic arrangement. organism: Human protein tissue_or_cell_type: Purified truncated soluble AOC3 experimental_model: X-ray structures of soluble human VAP-1 and inhibitor complex limitations: Soluble protein structure; proposed gate and adhesion-motif functions are not proven clinical effects of copper intake. exposure: Native and inhibitor-bound structure evidence_span: {"source_cache": "artifacts/copper-research/16239734.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "24ea102446aeff31a53b9302d191c0bc572100f8ee82b6ccb1a665432151662b", "start_char": 0, "end_char": 1408, "text_sha256": "24ea102446aeff31a53b9302d191c0bc572100f8ee82b6ccb1a665432151662b"} [copper-p16239734] Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1. (2005). https://pubmed.ncbi.nlm.nih.gov/16239734/ DOI: 10.1107/s0907444905028805
    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