Component

Human catechol O-methyltransferase / COMT

Human catechol O-methyltransferase / COMT. 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. The human COMT structure 3BWM includes bound magnesium alongside SAM and the catechol analog.

    Human catechol O-methyltransferase / COMT → Mg2+ source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/chlorogenic_acid-research/3BWM.cif", "source_url": "https://files.rcsb.org/download/3BWM.cif", "locator": "Primary deposited structure 3BWM chemical-component loop; zero-based end-exclusive Unicode offsets", "file_sha256": "debe2736e6c5affecce595281fac469cd424ab6e91a5d908ec89d9460f60e4f6", "start_char": 11428, "end_char": 13476, "text_sha256": "98319e36f43f3fe147a2b9a2444809c31b0e14ae68e789fe3c1a8303fd8da8bc"}
    experimental_model
    Human soluble COMT crystallography and deposited structure 3BWM
    exposure
    SAM and 3,5-dinitrocatechol-bound crystals; deposited Mg ion
    limitations
    Structural cofactor connection, not a CGA-magnesium supplementation trial. Human and rat COMT specificity differs; deposition includes an inhibitor analog rather than CGA.
    nutrient_topic
    Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect. · Chlorogenic acid / 5-O-caffeoylquinic acid
    organism
    Homo sapiens
    plain_language
    Magnesium is part of the measured enzyme complex; this does not prove that CGA depletes magnesium.
    primary_references
    [chlorogenic_acid-p18486144] Crystal structures of human 108V and 108M catechol O-methyltransferase. (2008). https://pubmed.ncbi.nlm.nih.gov/18486144/ DOI: 10.1016/j.jmb.2008.04.040
    tissue_or_cell_type
    Purified soluble COMT

    Chlorogenic acid: metabolism, signaling and nutrient connections (2026-09-17) · lines 854–865

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human soluble COMT crystallography and deposited structure 3BWM · source_derived_draft · unverified_draft

    ### chlorogenic_acid-human-comt-mg The human COMT structure 3BWM includes bound magnesium alongside SAM and the catechol analog. Condition category: normal nutrient_topic: Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: Magnesium is part of the measured enzyme complex; this does not prove that CGA depletes magnesium. organism: Homo sapiens tissue_or_cell_type: Purified soluble COMT experimental_model: Human soluble COMT crystallography and deposited structure 3BWM limitations: Structural cofactor connection, not a CGA-magnesium supplementation trial. Human and rat COMT specificity differs; deposition includes an inhibitor analog rather than CGA. exposure: SAM and 3,5-dinitrocatechol-bound crystals; deposited Mg ion evidence_span: {"source_cache": "artifacts/chlorogenic_acid-research/3BWM.cif", "source_url": "https://files.rcsb.org/download/3BWM.cif", "locator": "Primary deposited structure 3BWM chemical-component loop; zero-based end-exclusive Unicode offsets", "file_sha256": "debe2736e6c5affecce595281fac469cd424ab6e91a5d908ec89d9460f60e4f6", "start_char": 11428, "end_char": 13476, "text_sha256": "98319e36f43f3fe147a2b9a2444809c31b0e14ae68e789fe3c1a8303fd8da8bc"} [chlorogenic_acid-p18486144] Crystal structures of human 108V and 108M catechol O-methyltransferase. (2008). https://pubmed.ncbi.nlm.nih.gov/18486144/ DOI: 10.1016/j.jmb.2008.04.040
    Complete structured claim and evidence

  2. Human soluble COMT structures resolve bound SAM.

    Human catechol O-methyltransferase / COMT → S-Adenosyl-L-methionine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/chlorogenic_acid-research/18486144.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9cafbfc9353f49fab9919bc64608f21f445ace4b190771e44088a5a746e5a6e3", "start_char": 0, "end_char": 1961, "text_sha256": "9cafbfc9353f49fab9919bc64608f21f445ace4b190771e44088a5a746e5a6e3"}
    experimental_model
    Human soluble COMT crystallography and deposited structure 3BWM
    exposure
    SAM and 3,5-dinitrocatechol-bound crystals; deposited Mg ion
    limitations
    Structural cofactor connection, not a CGA-magnesium supplementation trial. Human and rat COMT specificity differs; deposition includes an inhibitor analog rather than CGA.
    nutrient_topic
    Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect. · Chlorogenic acid / 5-O-caffeoylquinic acid
    organism
    Homo sapiens
    plain_language
    The shared methyl donor links COMT to methionine-cycle metabolism.
    primary_references
    [chlorogenic_acid-p18486144] Crystal structures of human 108V and 108M catechol O-methyltransferase. (2008). https://pubmed.ncbi.nlm.nih.gov/18486144/ DOI: 10.1016/j.jmb.2008.04.040
    tissue_or_cell_type
    Purified soluble COMT

    Chlorogenic acid: metabolism, signaling and nutrient connections (2026-09-17) · lines 841–852

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human soluble COMT crystallography and deposited structure 3BWM · source_derived_draft · unverified_draft

    ### chlorogenic_acid-human-comt-sam Human soluble COMT structures resolve bound SAM. Condition category: normal nutrient_topic: Chlorogenic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The shared methyl donor links COMT to methionine-cycle metabolism. organism: Homo sapiens tissue_or_cell_type: Purified soluble COMT experimental_model: Human soluble COMT crystallography and deposited structure 3BWM limitations: Structural cofactor connection, not a CGA-magnesium supplementation trial. Human and rat COMT specificity differs; deposition includes an inhibitor analog rather than CGA. exposure: SAM and 3,5-dinitrocatechol-bound crystals; deposited Mg ion evidence_span: {"source_cache": "artifacts/chlorogenic_acid-research/18486144.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9cafbfc9353f49fab9919bc64608f21f445ace4b190771e44088a5a746e5a6e3", "start_char": 0, "end_char": 1961, "text_sha256": "9cafbfc9353f49fab9919bc64608f21f445ace4b190771e44088a5a746e5a6e3"} [chlorogenic_acid-p18486144] Crystal structures of human 108V and 108M catechol O-methyltransferase. (2008). https://pubmed.ncbi.nlm.nih.gov/18486144/ DOI: 10.1016/j.jmb.2008.04.040
    Complete structured claim and evidence

  3. Human recombinant COMT and liver S9 favored 4′- over 3′-O-methylation of luteolin.

    Human catechol O-methyltransferase / COMT → Diosmetin / 4′-O-methylluteolin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human enzyme and liver-S9 kinetics.
    limitations
    Product formation is not identical to accumulation after further metabolism.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    The enzyme initially favored the diosmetin branch.
    primary_references
    Luteolin is a rare substrate of human catechol-O-methyltransferase favoring a para-methylation. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23386290/ · DOI 10.1002/mnfr.201200584

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 92–98

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human enzyme and liver-S9 kinetics. · source_derived_draft · unverified_draft

    ## luteolin-comt-para The enzyme initially favored the diosmetin branch. Human recombinant COMT and liver S9 favored 4′- over 3′-O-methylation of luteolin. Model: Human enzyme and liver-S9 kinetics. Limitations: Product formation is not identical to accumulation after further metabolism. Evidence access: Primary abstract Luteolin is a rare substrate of human catechol-O-methyltransferase favoring a para-methylation. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23386290/ · DOI 10.1002/mnfr.201200584
    Complete structured claim and evidence

What acts on it

  1. EGCG inhibited human liver cytosolic COMT-mediated catechol-estrogen methylation, IC50 0.07 micromolar, with mixed inhibition.

    Epigallocatechin-3-gallate (EGCG) → Human catechol O-methyltransferase / COMT source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human liver cytosol and metabolite comparisons.
    limitations
    Assay potency does not establish brain, liver or whole-body inhibition after ingestion.
    nutrient_topic
    EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
    plain_language
    A liver preparation showed inhibition of a methyl-transfer enzyme.
    primary_references
    Inhibition of human liver catechol-O-methyltransferase by tea catechins and their metabolites: structure-activity relationship and molecular-modeling studies. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15857617/ · DOI 10.1016/j.bcp.2005.01.024

    EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 164–170

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human liver cytosol and metabolite comparisons. · source_derived_draft · unverified_draft

    ## egcg-comt-invitro A liver preparation showed inhibition of a methyl-transfer enzyme. EGCG inhibited human liver cytosolic COMT-mediated catechol-estrogen methylation, IC50 0.07 micromolar, with mixed inhibition. Model: Human liver cytosol and metabolite comparisons. Limitations: Assay potency does not establish brain, liver or whole-body inhibition after ingestion. Evidence access: primary abstract. Inhibition of human liver catechol-O-methyltransferase by tea catechins and their metabolites: structure-activity relationship and molecular-modeling studies. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15857617/ · DOI 10.1016/j.bcp.2005.01.024
    Complete structured claim and evidence

  2. 4″-O-methyl-EGCG retained COMT inhibitory activity, IC50 0.10 micromolar.

    4″-O-methyl-EGCG → Human catechol O-methyltransferase / COMT source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human liver cytosol; catechol-estrogen assay.
    limitations
    Do not assume metabolites have identical tissue exposure or activity to EGCG.
    nutrient_topic
    EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
    plain_language
    A methylated metabolite also affected the enzyme in vitro.
    primary_references
    Inhibition of human liver catechol-O-methyltransferase by tea catechins and their metabolites: structure-activity relationship and molecular-modeling studies. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15857617/ · DOI 10.1016/j.bcp.2005.01.024

    EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 172–178

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human liver cytosol; catechol-estrogen assay. · source_derived_draft · unverified_draft

    ## egcg-comt-metabolite A methylated metabolite also affected the enzyme in vitro. 4″-O-methyl-EGCG retained COMT inhibitory activity, IC50 0.10 micromolar. Model: Human liver cytosol; catechol-estrogen assay. Limitations: Do not assume metabolites have identical tissue exposure or activity to EGCG. Evidence access: primary abstract. Inhibition of human liver catechol-O-methyltransferase by tea catechins and their metabolites: structure-activity relationship and molecular-modeling studies. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15857617/ · DOI 10.1016/j.bcp.2005.01.024
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. After 750 mg EGCG in 24 volunteers, erythrocyte COMT activity increased by 24% at two hours rather than decreasing.

    Epigallocatechin-3-gallate (EGCG) → Human erythrocyte COMT activity source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Single exposure; 14 women and 10 men; COMT genotype assessment.
    limitations
    Red-cell activity at one time point is not a measurement of brain or liver COMT. No general catecholamine or fat-burning claim follows.
    nutrient_topic
    EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
    plain_language
    The measured human red-cell result did not match a simple inhibition prediction.
    primary_references
    The activity of catechol-O-methyltransferase (COMT) is not impaired by high doses of epigallocatechin-3-gallate (EGCG) in vivo. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24972245/ · DOI 10.1016/j.ejphar.2014.06.014

    EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 180–186

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Single exposure; 14 women and 10 men; COMT genotype assessment. · source_derived_draft · unverified_draft

    ## egcg-comt-human The measured human red-cell result did not match a simple inhibition prediction. After 750 mg EGCG in 24 volunteers, erythrocyte COMT activity increased by 24% at two hours rather than decreasing. Model: Single exposure; 14 women and 10 men; COMT genotype assessment. Limitations: Red-cell activity at one time point is not a measurement of brain or liver COMT. No general catecholamine or fat-burning claim follows. Evidence access: primary abstract. The activity of catechol-O-methyltransferase (COMT) is not impaired by high doses of epigallocatechin-3-gallate (EGCG) in vivo. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24972245/ · DOI 10.1016/j.ejphar.2014.06.014
    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