Component

Lactoperoxidase compound I

Study-specific endpoint; inspect claim context for model and measurement.

4 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. H2O2 formed LPO compound I with second-order rate constant (1.1 ± 0.1) × 10^7 M−1 s−1.

    Hydrogen peroxide → Lactoperoxidase compound I source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract.
    exposure_category
    Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
    limitations
    Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues.
    nutrient_topic
    Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
    plain_language
    Peroxide activates the enzyme before iodide oxidation.
    primary_references
    Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x

    Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 184–190

    AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. · source_derived_draft · unverified_draft

    ## ki-lpo-activate Peroxide activates the enzyme before iodide oxidation. H2O2 formed LPO compound I with second-order rate constant (1.1 ± 0.1) × 10^7 M−1 s−1. Model: Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. Limitations: Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues. Evidence location: Primary abstract Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x
    Complete structured claim and evidence

  2. Chloride did not act as electron donor; bromide reacted much more slowly, at (4.1 ± 0.1) × 10^4 M−1 s−1.

    Chloride ion → Lactoperoxidase compound I source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract.
    exposure_category
    Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
    limitations
    Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues.
    nutrient_topic
    Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
    plain_language
    Abundant chloride cannot simply replace iodide in this enzyme reaction.
    primary_references
    Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x

    Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 208–214

    AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. · source_derived_draft · unverified_draft

    ## ki-lpo-halides Abundant chloride cannot simply replace iodide in this enzyme reaction. Chloride did not act as electron donor; bromide reacted much more slowly, at (4.1 ± 0.1) × 10^4 M−1 s−1. Model: Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. Limitations: Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues. Evidence location: Primary abstract Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x
    Complete structured claim and evidence

  3. Iodide reduced LPO compound I to native enzyme at (1.2 ± 0.04) × 10^8 M−1 s−1.

    Iodide ion → Lactoperoxidase compound I source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract.
    exposure_category
    Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
    limitations
    Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues.
    nutrient_topic
    Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
    plain_language
    Iodide supplies electrons to activated lactoperoxidase.
    primary_references
    Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x

    Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 192–198

    AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. · source_derived_draft · unverified_draft

    ## ki-lpo-iodide Iodide supplies electrons to activated lactoperoxidase. Iodide reduced LPO compound I to native enzyme at (1.2 ± 0.04) × 10^8 M−1 s−1. Model: Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. Limitations: Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues. Evidence location: Primary abstract Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x
    Complete structured claim and evidence

  4. Thiocyanate reacted with LPO compound I at 2.0 × 10^8 M−1 s−1.

    Thiocyanate ion → Lactoperoxidase compound I source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract.
    exposure_category
    Study-specific exposure, including pharmacological and in-vitro conditions; normal is the schema fallback outside the three availability categories.
    limitations
    Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues.
    nutrient_topic
    Potassium iodide research collection; shared-anion and comparator studies are not all KI interventions. · Potassium iodide
    plain_language
    Thiocyanate is another rapidly reacting substrate.
    primary_references
    Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x

    Potassium iodide: thyroid and non-thyroid mechanisms, interactions and discovery questions (2026-09-18) · lines 200–206

    AI-assisted research curation; primary-study references, chemical references and label statements individually identified. Not publisher full text. · supports · Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. · source_derived_draft · unverified_draft

    ## ki-lpo-scn Thiocyanate is another rapidly reacting substrate. Thiocyanate reacted with LPO compound I at 2.0 × 10^8 M−1 s−1. Model: Purified LPO transient kinetics; pH 7, 15 °C; preparation species unresolved in abstract. Limitations: Purified enzyme kinetics; concentrations, substrate competition and reaction order determine relevance in tissues. Evidence location: Primary abstract Reaction of lactoperoxidase compound I with halides and thiocyanate. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269834/ · DOI 10.1021/bi026326x
    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.

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