Component

Human CoQ C-methyltransferase / COQ5

Human CoQ C-methyltransferase / COQ5. 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 it acts on

  1. Affected siblings with COQ5 duplications had low white-cell CoQ; the available muscle sample was also depleted.

    Human CoQ C-methyltransferase / COQ5 → Cellular coenzyme Q concentration source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/coq10-research/29044765.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "704d515eb76ce1074ae021346c10abee852de623057b33d287e4fad0b69d23b4", "start_char": 0, "end_char": 1271, "text_sha256": "704d515eb76ce1074ae021346c10abee852de623057b33d287e4fad0b69d23b4"}
    experimental_model
    Family sequencing and biochemical measurements
    exposure
    Biallelic COQ5 duplications; supplementation follow-up
    limitations
    Small uncontrolled genetic case series; clinical improvement cannot yield a general efficacy estimate.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    Three human siblings
    plain_language
    A low circulating-cell pool was linked to a defined synthesis defect.
    primary_references
    [coq10-p29044765] A novel inborn error of the coenzyme Q10 biosynthesis pathway: cerebellar ataxia and static encephalomyopathy due to COQ5 C-methyltransferase deficiency. (2018). https://pubmed.ncbi.nlm.nih.gov/29044765/ DOI: 10.1002/humu.23345
    tissue_or_cell_type
    Neurologic disease and CoQ measurements
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 1035–1046

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Family sequencing and biochemical measurements · source_derived_draft · unverified_draft

    ### coq10-coq5-deficiency Affected siblings with COQ5 duplications had low white-cell CoQ; the available muscle sample was also depleted. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A low circulating-cell pool was linked to a defined synthesis defect. organism: Three human siblings tissue_or_cell_type: Neurologic disease and CoQ measurements experimental_model: Family sequencing and biochemical measurements limitations: Small uncontrolled genetic case series; clinical improvement cannot yield a general efficacy estimate. exposure: Biallelic COQ5 duplications; supplementation follow-up evidence_span: {"source_cache": "artifacts/coq10-research/29044765.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "704d515eb76ce1074ae021346c10abee852de623057b33d287e4fad0b69d23b4", "start_char": 0, "end_char": 1271, "text_sha256": "704d515eb76ce1074ae021346c10abee852de623057b33d287e4fad0b69d23b4"} [coq10-p29044765] A novel inborn error of the coenzyme Q10 biosynthesis pathway: cerebellar ataxia and static encephalomyopathy due to COQ5 C-methyltransferase deficiency. (2018). https://pubmed.ncbi.nlm.nih.gov/29044765/ DOI: 10.1002/humu.23345
    Complete structured claim and evidence

  2. Human COQ5 retained C-methyltransferase function and restored CoQ production when the yeast synthome was stabilized.

    Human CoQ C-methyltransferase / COQ5 → Coenzyme Q precursor C-methylation source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coq10-research/25152161.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "84482b69f7e6e575614f1cae122298d4328a881a5eda65eb7e96ed4f11db17fe", "start_char": 0, "end_char": 1655, "text_sha256": "84482b69f7e6e575614f1cae122298d4328a881a5eda65eb7e96ed4f11db17fe"}
    experimental_model
    Localization and yeast complementation
    exposure
    COQ5 complementation with or without synthome stabilization
    limitations
    Human protein in yeast; an assembled biosynthesis complex was important for rescue.
    nutrient_topic
    Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
    organism
    Human COQ5 expressed in yeast
    plain_language
    A methylating enzyme also depends on the surrounding enzyme assembly.
    primary_references
    [coq10-p25152161] Molecular characterization of the human COQ5 C-methyltransferase in coenzyme Q10 biosynthesis. (2014). https://pubmed.ncbi.nlm.nih.gov/25152161/ DOI: 10.1016/j.bbalip.2014.08.007
    tissue_or_cell_type
    Mitochondrial matrix-facing biosynthetic complex

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 268–279

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Localization and yeast complementation · source_derived_draft · unverified_draft

    ### coq10-coq5-methylation Human COQ5 retained C-methyltransferase function and restored CoQ production when the yeast synthome was stabilized. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A methylating enzyme also depends on the surrounding enzyme assembly. organism: Human COQ5 expressed in yeast tissue_or_cell_type: Mitochondrial matrix-facing biosynthetic complex experimental_model: Localization and yeast complementation limitations: Human protein in yeast; an assembled biosynthesis complex was important for rescue. exposure: COQ5 complementation with or without synthome stabilization evidence_span: {"source_cache": "artifacts/coq10-research/25152161.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "84482b69f7e6e575614f1cae122298d4328a881a5eda65eb7e96ed4f11db17fe", "start_char": 0, "end_char": 1655, "text_sha256": "84482b69f7e6e575614f1cae122298d4328a881a5eda65eb7e96ed4f11db17fe"} [coq10-p25152161] Molecular characterization of the human COQ5 C-methyltransferase in coenzyme Q10 biosynthesis. (2014). https://pubmed.ncbi.nlm.nih.gov/25152161/ DOI: 10.1016/j.bbalip.2014.08.007
    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