Component

3-Methylcrotonyl-CoA

3-Methylcrotonyl-CoA. Species, exposure and limitations are retained in each linked claim.

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. Structural comparisons supported substrate-dependent, coordinated activation of human MCC.

    3-Methylcrotonyl-CoA → Human 3-methylcrotonyl-CoA carboxylase complex source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/39223421.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "221115ee36b8452b3915e000ae5f363f8f771705dcbb17570343b8f536b7c87a", "start_char": 0, "end_char": 1050, "text_sha256": "221115ee36b8452b3915e000ae5f363f8f771705dcbb17570343b8f536b7c87a"}
    experimental_model
    Structures of purified endogenous human MCC, PCC and PC; substrate-bound MCC conformations
    exposure
    Cryo-EM and substrate-bound structural analysis
    limitations
    Indexed abstract and publisher preview inspected; detailed residue-level claims require full-paper review. Published online 2024, journal issue 2025.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    Adding substrate reorganizes the working enzyme; the word synergy here refers to enzyme parts, not proven synergy between supplements.
    primary_references
    [b7-p39223421] Structural insight into synergistic activation of human 3-methylcrotonyl-CoA carboxylase. (2025). https://pubmed.ncbi.nlm.nih.gov/39223421/ DOI: 10.1038/s41594-024-01379-3
    tissue_or_cell_type
    Purified endogenous mitochondrial carboxylases

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 806–817

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Structures of purified endogenous human MCC, PCC and PC; substrate-bound MCC conformations · source_derived_draft · unverified_draft

    ### b7-mcc-substrate-conformations Structural comparisons supported substrate-dependent, coordinated activation of human MCC. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Adding substrate reorganizes the working enzyme; the word synergy here refers to enzyme parts, not proven synergy between supplements. organism: Homo sapiens tissue_or_cell_type: Purified endogenous mitochondrial carboxylases experimental_model: Structures of purified endogenous human MCC, PCC and PC; substrate-bound MCC conformations limitations: Indexed abstract and publisher preview inspected; detailed residue-level claims require full-paper review. Published online 2024, journal issue 2025. exposure: Cryo-EM and substrate-bound structural analysis evidence_span: {"source_cache": "artifacts/biotin-research/39223421.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "221115ee36b8452b3915e000ae5f363f8f771705dcbb17570343b8f536b7c87a", "start_char": 0, "end_char": 1050, "text_sha256": "221115ee36b8452b3915e000ae5f363f8f771705dcbb17570343b8f536b7c87a"} [b7-p39223421] Structural insight into synergistic activation of human 3-methylcrotonyl-CoA carboxylase. (2025). https://pubmed.ncbi.nlm.nih.gov/39223421/ DOI: 10.1038/s41594-024-01379-3
    Complete structured claim and evidence

What acts on it

  1. MCC converts 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA in the leucine breakdown pathway using biotin.

    Human 3-methylcrotonyl-CoA carboxylase complex → 3-Methylcrotonyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/21918059.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5cf1d7e25ae7bdfeb2ac3225cee8e4e660723d5197fc057f63327b3ad9eb3aaf", "start_char": 0, "end_char": 1723, "text_sha256": "5cf1d7e25ae7bdfeb2ac3225cee8e4e660723d5197fc057f63327b3ad9eb3aaf"}
    experimental_model
    Two human egg-white biotin-depletion cohorts with leucine challenges
    exposure
    28-day depletion in cohorts of 5 and 7 adults
    limitations
    Biomarker challenge study; the core MCC reaction is pathway background, not a new structural discovery.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    Biotin helps process a carbon intermediate produced while breaking down leucine.
    primary_references
    [b7-p21918059] Urinary excretion of 3-hydroxyisovaleric acid and 3-hydroxyisovaleryl carnitine increases in response to a leucine challenge in marginally biotin-deficient humans. (2011). https://pubmed.ncbi.nlm.nih.gov/21918059/ DOI: 10.3945/jn.111.146126
    tissue_or_cell_type
    Leucine metabolism and urine

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 793–804

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Two human egg-white biotin-depletion cohorts with leucine challenges · source_derived_draft · unverified_draft

    ### b7-mcc-reaction MCC converts 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA in the leucine breakdown pathway using biotin. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Biotin helps process a carbon intermediate produced while breaking down leucine. organism: Homo sapiens tissue_or_cell_type: Leucine metabolism and urine experimental_model: Two human egg-white biotin-depletion cohorts with leucine challenges limitations: Biomarker challenge study; the core MCC reaction is pathway background, not a new structural discovery. exposure: 28-day depletion in cohorts of 5 and 7 adults evidence_span: {"source_cache": "artifacts/biotin-research/21918059.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5cf1d7e25ae7bdfeb2ac3225cee8e4e660723d5197fc057f63327b3ad9eb3aaf", "start_char": 0, "end_char": 1723, "text_sha256": "5cf1d7e25ae7bdfeb2ac3225cee8e4e660723d5197fc057f63327b3ad9eb3aaf"} [b7-p21918059] Urinary excretion of 3-hydroxyisovaleric acid and 3-hydroxyisovaleryl carnitine increases in response to a leucine challenge in marginally biotin-deficient humans. (2011). https://pubmed.ncbi.nlm.nih.gov/21918059/ DOI: 10.3945/jn.111.146126
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Recombinant human MCC had an ATP Km of 45 ± 11 micromolar and a methylcrotonyl-CoA Km of 74 ± 7 micromolar.

    Human 3-methylcrotonyl-CoA carboxylase complex → ATP source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/17360195.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3ae046490d9657d005d5c39efb1f7439bc015d0cb2190834e3e868de70eaf985", "start_char": 0, "end_char": 1067, "text_sha256": "3ae046490d9657d005d5c39efb1f7439bc015d0cb2190834e3e868de70eaf985"}
    experimental_model
    Purified recombinant human MCC produced by baculovirus expression
    exposure
    ATP and methylcrotonyl-CoA kinetics
    limitations
    Recombinant-enzyme kinetics do not determine human dietary requirements.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    The biotin-dependent reaction also requires an energy substrate and the carbon substrate.
    primary_references
    [b7-p17360195] Expression, purification, characterization of human 3-methylcrotonyl-CoA carboxylase (MCCC). (2007). https://pubmed.ncbi.nlm.nih.gov/17360195/ DOI: 10.1016/j.pep.2007.01.012
    tissue_or_cell_type
    Purified human MCC complex

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 780–791

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human MCC produced by baculovirus expression · source_derived_draft · unverified_draft

    ### b7-mcc-atp Recombinant human MCC had an ATP Km of 45 ± 11 micromolar and a methylcrotonyl-CoA Km of 74 ± 7 micromolar. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The biotin-dependent reaction also requires an energy substrate and the carbon substrate. organism: Homo sapiens tissue_or_cell_type: Purified human MCC complex experimental_model: Purified recombinant human MCC produced by baculovirus expression limitations: Recombinant-enzyme kinetics do not determine human dietary requirements. exposure: ATP and methylcrotonyl-CoA kinetics evidence_span: {"source_cache": "artifacts/biotin-research/17360195.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3ae046490d9657d005d5c39efb1f7439bc015d0cb2190834e3e868de70eaf985", "start_char": 0, "end_char": 1067, "text_sha256": "3ae046490d9657d005d5c39efb1f7439bc015d0cb2190834e3e868de70eaf985"} [b7-p17360195] Expression, purification, characterization of human 3-methylcrotonyl-CoA carboxylase (MCCC). (2007). https://pubmed.ncbi.nlm.nih.gov/17360195/ DOI: 10.1016/j.pep.2007.01.012
    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