Component

Human IYD lacking N-terminal membrane anchor

Experimental soluble human IYD construct, distinct from full-length IYD.

3 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. Purified soluble human IYD released radiolabeled iodide from diiodotyrosine during reductive enzyme assays.

    Human IYD lacking N-terminal membrane anchor → Iodide ion source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_span
    {"source_cache": "artifacts/iodine-synthesis-sources/25395621.txt", "start_char": 11103, "end_char": 12723, "text_sha256": "726c34262182d49a45a4741a29a49ef70bf6d529c79d75cfbb0e9ea59ffd256b", "text_characters": 1620, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}
    experimental_model
    Recombinant human IYD lacking residues 1–31; crystallography, radiotracer kinetics and redox titration
    exposure
    0–70 micromolar [125I]DIT; sodium dithionite supplies reducing equivalents.
    limitations
    Anchor-deleted enzyme and artificial reductant; does not identify the physiological electron donor.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens recombinant protein
    plain_language
    IYD recovers iodine from leftover iodinated tyrosine.
    primary_references
    [iodine-syn-iyd2015] A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. (2015). https://pubmed.ncbi.nlm.nih.gov/25395621/ DOI: 10.1074/jbc.m114.605964
    tissue_or_cell_type
    Purified soluble IYD

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 688–700

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human IYD lacking residues 1–31; crystallography, radiotracer kinetics and redox titration · source_derived_draft · unverified_draft

    ### iodine-syn-iyd-dit-salvage Purified soluble human IYD released radiolabeled iodide from diiodotyrosine during reductive enzyme assays. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: IYD recovers iodine from leftover iodinated tyrosine. organism: Homo sapiens recombinant protein tissue_or_cell_type: Purified soluble IYD experimental_model: Recombinant human IYD lacking residues 1–31; crystallography, radiotracer kinetics and redox titration limitations: Anchor-deleted enzyme and artificial reductant; does not identify the physiological electron donor. exposure: 0–70 micromolar [125I]DIT; sodium dithionite supplies reducing equivalents. cross_nutrient: true evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/25395621.txt", "start_char": 11103, "end_char": 12723, "text_sha256": "726c34262182d49a45a4741a29a49ef70bf6d529c79d75cfbb0e9ea59ffd256b", "text_characters": 1620, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-iyd2015] A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. (2015). https://pubmed.ncbi.nlm.nih.gov/25395621/ DOI: 10.1074/jbc.m114.605964
    Complete structured claim and evidence

  2. Human IYD crystal structures show one bound FMN per polypeptide, with iodotyrosine contacting its isoalloxazine ring in the substrate complex.

    Human IYD lacking N-terminal membrane anchor → Flavin mononucleotide source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_span
    {"source_cache": "artifacts/iodine-synthesis-sources/25395621.txt", "start_char": 14596, "end_char": 15366, "text_sha256": "5f3959109e358adaddae3ea78c716d16316c28f6fb4153ad5696bae7b1ed733e", "text_characters": 770, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}
    experimental_model
    Recombinant human IYD lacking residues 1–31; crystallography, radiotracer kinetics and redox titration
    exposure
    Human soluble IYD crystallized alone or with 3-iodo-L-tyrosine.
    limitations
    Cofactor structure; no riboflavin restriction or supplementation study.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens recombinant protein
    plain_language
    IYD uses the vitamin-B2-derived cofactor FMN to handle iodotyrosine.
    primary_references
    [iodine-syn-iyd2015] A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. (2015). https://pubmed.ncbi.nlm.nih.gov/25395621/ DOI: 10.1074/jbc.m114.605964
    tissue_or_cell_type
    Purified soluble IYD

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 702–714

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human IYD lacking residues 1–31; crystallography, radiotracer kinetics and redox titration · source_derived_draft · unverified_draft

    ### iodine-syn-iyd-fmn-binding Human IYD crystal structures show one bound FMN per polypeptide, with iodotyrosine contacting its isoalloxazine ring in the substrate complex. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: IYD uses the vitamin-B2-derived cofactor FMN to handle iodotyrosine. organism: Homo sapiens recombinant protein tissue_or_cell_type: Purified soluble IYD experimental_model: Recombinant human IYD lacking residues 1–31; crystallography, radiotracer kinetics and redox titration limitations: Cofactor structure; no riboflavin restriction or supplementation study. exposure: Human soluble IYD crystallized alone or with 3-iodo-L-tyrosine. cross_nutrient: true evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/25395621.txt", "start_char": 14596, "end_char": 15366, "text_sha256": "5f3959109e358adaddae3ea78c716d16316c28f6fb4153ad5696bae7b1ed733e", "text_characters": 770, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-iyd2015] A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. (2015). https://pubmed.ncbi.nlm.nih.gov/25395621/ DOI: 10.1074/jbc.m114.605964
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The substrate analog 3-fluoro-L-tyrosine stabilized a one-electron-reduced FMN semiquinone during reductive titration of soluble human IYD.

    3-Fluoro-L-tyrosine → FMN semiquinone source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_span
    {"source_cache": "artifacts/iodine-synthesis-sources/25395621.txt", "start_char": 4223, "end_char": 4943, "text_sha256": "5567eccc06be2559ce51e8a2640697678a8fd3c1216896997568a9341da5a73b", "text_characters": 720, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."}
    experimental_model
    Recombinant human IYD lacking residues 1–31; crystallography, radiotracer kinetics and redox titration
    exposure
    Reductive titration with versus without active-site ligand.
    limitations
    An inert fluorotyrosine probe demonstrates cofactor control, not physiological fluoride displacement.
    nutrient_topic
    Iodine research collection; topical membership is not evidence of a direct dietary effect. · Iodine
    organism
    Homo sapiens recombinant protein
    plain_language
    Substrate-like binding changes which FMN redox state the enzyme can stabilize.
    primary_references
    [iodine-syn-iyd2015] A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. (2015). https://pubmed.ncbi.nlm.nih.gov/25395621/ DOI: 10.1074/jbc.m114.605964
    tissue_or_cell_type
    Purified soluble IYD

    Iodine: thyroid hormone production, deficiency, excess and nutrient interactions (2026-09-17) · lines 716–728

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human IYD lacking residues 1–31; crystallography, radiotracer kinetics and redox titration · source_derived_draft · unverified_draft

    ### iodine-syn-iyd-redox-switch The substrate analog 3-fluoro-L-tyrosine stabilized a one-electron-reduced FMN semiquinone during reductive titration of soluble human IYD. Condition category: normal nutrient_topic: Iodine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Substrate-like binding changes which FMN redox state the enzyme can stabilize. organism: Homo sapiens recombinant protein tissue_or_cell_type: Purified soluble IYD experimental_model: Recombinant human IYD lacking residues 1–31; crystallography, radiotracer kinetics and redox titration limitations: An inert fluorotyrosine probe demonstrates cofactor control, not physiological fluoride displacement. exposure: Reductive titration with versus without active-site ligand. cross_nutrient: true evidence_span: {"source_cache": "artifacts/iodine-synthesis-sources/25395621.txt", "start_char": 4223, "end_char": 4943, "text_sha256": "5567eccc06be2559ce51e8a2640697678a8fd3c1216896997568a9341da5a73b", "text_characters": 720, "note": "Exact publisher passage retained in the cited local source cache; locator and digest supplied here."} [iodine-syn-iyd2015] A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. (2015). https://pubmed.ncbi.nlm.nih.gov/25395621/ DOI: 10.1074/jbc.m114.605964
    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