Component

Human methylcrotonyl-CoA carboxylase alpha subunit / MCCC1

Human methylcrotonyl-CoA carboxylase alpha subunit / MCCC1. Species, exposure and limitations are retained in each linked claim.

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 it acts on

  1. Active recombinant human MCC contained alpha and beta subunits at a one-to-one ratio.

    Human methylcrotonyl-CoA carboxylase alpha subunit / MCCC1 → Human methylcrotonyl-CoA carboxylase beta subunit / MCCC2 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
    MCC needs both subunits; biotin cannot replace a missing protein partner.
    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 767–778

    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-complex Active recombinant human MCC contained alpha and beta subunits at a one-to-one ratio. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: MCC needs both subunits; biotin cannot replace a missing protein partner. 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

What acts on it

  1. HLCS rapidly biotinylated the biotin-acceptor fragment of human MCCC1, with transfer limited by enzyme-substrate association.

    Human holocarboxylase synthetase / HLCS → Human methylcrotonyl-CoA carboxylase alpha subunit / MCCC1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/22123817.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "559afe20b6f8601a2d055d42fb121c89eaf1ece76afaa5cc0817c20787893233", "start_char": 0, "end_char": 1502, "text_sha256": "559afe20b6f8601a2d055d42fb121c89eaf1ece76afaa5cc0817c20787893233"}
    experimental_model
    Single-turnover biotin transfer to minimal BCCP fragments from all five human carboxylases
    exposure
    Stopped-flow and quench-flow transfer kinetics
    limitations
    Fragment kinetics support differential recognition, not a universal nutrient-deficiency survival order in humans.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    This mitochondrial enzyme has a biotin attachment domain recognized by HLCS.
    primary_references
    [b7-p22123817] Selectivity in post-translational biotin addition to five human carboxylases. (2012). https://pubmed.ncbi.nlm.nih.gov/22123817/ DOI: 10.1074/jbc.m111.275982
    tissue_or_cell_type
    Purified HLCS and acceptor fragments

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 416–427

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Single-turnover biotin transfer to minimal BCCP fragments from all five human carboxylases · source_derived_draft · unverified_draft

    ### b7-hlcs-mcc-acceptor HLCS rapidly biotinylated the biotin-acceptor fragment of human MCCC1, with transfer limited by enzyme-substrate association. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: This mitochondrial enzyme has a biotin attachment domain recognized by HLCS. organism: Homo sapiens tissue_or_cell_type: Purified HLCS and acceptor fragments experimental_model: Single-turnover biotin transfer to minimal BCCP fragments from all five human carboxylases limitations: Fragment kinetics support differential recognition, not a universal nutrient-deficiency survival order in humans. exposure: Stopped-flow and quench-flow transfer kinetics evidence_span: {"source_cache": "artifacts/biotin-research/22123817.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "559afe20b6f8601a2d055d42fb121c89eaf1ece76afaa5cc0817c20787893233", "start_char": 0, "end_char": 1502, "text_sha256": "559afe20b6f8601a2d055d42fb121c89eaf1ece76afaa5cc0817c20787893233"} [b7-p22123817] Selectivity in post-translational biotin addition to five human carboxylases. (2012). https://pubmed.ncbi.nlm.nih.gov/22123817/ DOI: 10.1074/jbc.m111.275982
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. In the 88-person MCC-deficiency series, 57% were asymptomatic; 12 had acute metabolic decompensations, and genotype or biochemical phenotype did not reliably predict the course.

    Human 3-methylcrotonyl-CoA carboxylase complex → Clinical course of human isolated MCC deficiency source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/biotin-research/22642865.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f0c40118afe81e9b597d2d2cbe6a785c2b96a4dbd7f4dcb634230070c61865ee", "start_char": 0, "end_char": 1384, "text_sha256": "f0c40118afe81e9b597d2d2cbe6a785c2b96a4dbd7f4dcb634230070c61865ee"}
    experimental_model
    Retrospective clinical, biochemical and molecular study of 88 MCC-deficient individuals
    exposure
    MCCC1/MCCC2 defects; mixed newborn screening and clinical ascertainment
    limitations
    Ascertainment bias and incomplete penetrance limit predictions. This is an isolated inherited enzyme defect, not biotin intake deficiency.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    A striking biochemical marker does not determine how ill a person will be.
    primary_references
    [b7-p22642865] 3-methylcrotonyl-CoA carboxylase deficiency: clinical, biochemical, enzymatic and molecular studies in 88 individuals. (2012). https://pubmed.ncbi.nlm.nih.gov/22642865/ DOI: 10.1186/1750-1172-7-31
    tissue_or_cell_type
    Clinical and biochemical phenotype
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 1027–1038

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Retrospective clinical, biochemical and molecular study of 88 MCC-deficient individuals · source_derived_draft · unverified_draft

    ### b7-mcc-genetic-variability In the 88-person MCC-deficiency series, 57% were asymptomatic; 12 had acute metabolic decompensations, and genotype or biochemical phenotype did not reliably predict the course. Condition category: machinery_impairment nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: A striking biochemical marker does not determine how ill a person will be. organism: Homo sapiens tissue_or_cell_type: Clinical and biochemical phenotype experimental_model: Retrospective clinical, biochemical and molecular study of 88 MCC-deficient individuals limitations: Ascertainment bias and incomplete penetrance limit predictions. This is an isolated inherited enzyme defect, not biotin intake deficiency. exposure: MCCC1/MCCC2 defects; mixed newborn screening and clinical ascertainment evidence_span: {"source_cache": "artifacts/biotin-research/22642865.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f0c40118afe81e9b597d2d2cbe6a785c2b96a4dbd7f4dcb634230070c61865ee", "start_char": 0, "end_char": 1384, "text_sha256": "f0c40118afe81e9b597d2d2cbe6a785c2b96a4dbd7f4dcb634230070c61865ee"} [b7-p22642865] 3-methylcrotonyl-CoA carboxylase deficiency: clinical, biochemical, enzymatic and molecular studies in 88 individuals. (2012). https://pubmed.ncbi.nlm.nih.gov/22642865/ DOI: 10.1186/1750-1172-7-31
    Complete structured claim and evidence

  2. 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

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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