Component

Human acetyl-CoA carboxylase 2 / ACACB

Human acetyl-CoA carboxylase 2 / ACACB. Species, exposure and limitations are retained in each linked claim.

5 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. Purified human ACC2 formed malonyl-CoA from acetyl-CoA in assays varying bicarbonate and ATP.

    Human acetyl-CoA carboxylase 2 / ACACB → Acetyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/19236960.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bedd791235b10ff5942ef7177b54bca5b2243883da02fb24572691aaf5975be5", "start_char": 0, "end_char": 896, "text_sha256": "bedd791235b10ff5942ef7177b54bca5b2243883da02fb24572691aaf5975be5"}
    experimental_model
    Steady-state kinetics of purified recombinant human ACC2; LC-MS/MS malonyl-CoA assay
    exposure
    Bicarbonate, ATP, acetyl-CoA and citrate concentration matrices
    limitations
    Kinetic constants are assay properties; they do not define a dietary biotin or B5 threshold.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    ACC2 makes the same carbon product as ACC1 but serves a distinct enzyme context.
    primary_references
    [b7-p19236960] Characterization of recombinant human acetyl-CoA carboxylase-2 steady-state kinetics. (2009). https://pubmed.ncbi.nlm.nih.gov/19236960/ DOI: 10.1016/j.bbapap.2009.02.004
    tissue_or_cell_type
    Purified human ACC2

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 676–687

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Steady-state kinetics of purified recombinant human ACC2; LC-MS/MS malonyl-CoA assay · source_derived_draft · unverified_draft

    ### b7-acc2-reaction Purified human ACC2 formed malonyl-CoA from acetyl-CoA in assays varying bicarbonate and ATP. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: ACC2 makes the same carbon product as ACC1 but serves a distinct enzyme context. organism: Homo sapiens tissue_or_cell_type: Purified human ACC2 experimental_model: Steady-state kinetics of purified recombinant human ACC2; LC-MS/MS malonyl-CoA assay limitations: Kinetic constants are assay properties; they do not define a dietary biotin or B5 threshold. exposure: Bicarbonate, ATP, acetyl-CoA and citrate concentration matrices evidence_span: {"source_cache": "artifacts/biotin-research/19236960.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bedd791235b10ff5942ef7177b54bca5b2243883da02fb24572691aaf5975be5", "start_char": 0, "end_char": 896, "text_sha256": "bedd791235b10ff5942ef7177b54bca5b2243883da02fb24572691aaf5975be5"} [b7-p19236960] Characterization of recombinant human acetyl-CoA carboxylase-2 steady-state kinetics. (2009). https://pubmed.ncbi.nlm.nih.gov/19236960/ DOI: 10.1016/j.bbapap.2009.02.004
    Complete structured claim and evidence

What acts on it

  1. In the studied human ACC2 domain, phosphorylated Ser222 occupied the putative dimer interface, disrupting polymerization and explaining AMPK-mediated inactivation.

    AMP-activated protein kinase complexes → Human acetyl-CoA carboxylase 2 / ACACB source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/19900410.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3d7161fb1a281c68bbe3b8d4738b26d5ed762ca2bea3d9621ee6c8946a7fa71c", "start_char": 0, "end_char": 870, "text_sha256": "3d7161fb1a281c68bbe3b8d4738b26d5ed762ca2bea3d9621ee6c8946a7fa71c"}
    experimental_model
    Crystal structures of the human ACC2 biotin-carboxylase domain after AMPK phosphorylation
    exposure
    Phosphorylation and soraphen A comparison
    limitations
    Domain structures explain a regulatory mechanism; the construct uses Ser222 numbering and must not be silently relabeled with another isoform numbering scheme.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    An energy-sensing kinase can switch ACC2 down even when biotin is available.
    primary_references
    [b7-p19900410] Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK. (2010). https://pubmed.ncbi.nlm.nih.gov/19900410/ DOI: 10.1016/j.bbrc.2009.11.029
    tissue_or_cell_type
    Purified ACC2 domain

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 702–713

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystal structures of the human ACC2 biotin-carboxylase domain after AMPK phosphorylation · source_derived_draft · unverified_draft

    ### b7-acc2-ampk In the studied human ACC2 domain, phosphorylated Ser222 occupied the putative dimer interface, disrupting polymerization and explaining AMPK-mediated inactivation. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: An energy-sensing kinase can switch ACC2 down even when biotin is available. organism: Homo sapiens tissue_or_cell_type: Purified ACC2 domain experimental_model: Crystal structures of the human ACC2 biotin-carboxylase domain after AMPK phosphorylation limitations: Domain structures explain a regulatory mechanism; the construct uses Ser222 numbering and must not be silently relabeled with another isoform numbering scheme. exposure: Phosphorylation and soraphen A comparison evidence_span: {"source_cache": "artifacts/biotin-research/19900410.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3d7161fb1a281c68bbe3b8d4738b26d5ed762ca2bea3d9621ee6c8946a7fa71c", "start_char": 0, "end_char": 870, "text_sha256": "3d7161fb1a281c68bbe3b8d4738b26d5ed762ca2bea3d9621ee6c8946a7fa71c"} [b7-p19900410] Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK. (2010). https://pubmed.ncbi.nlm.nih.gov/19900410/ DOI: 10.1016/j.bbrc.2009.11.029
    Complete structured claim and evidence

  2. Citrate increased recombinant human ACC2 kcat and kcat/Km for ATP and acetyl-CoA.

    Citrate → Human acetyl-CoA carboxylase 2 / ACACB source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/19236960.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bedd791235b10ff5942ef7177b54bca5b2243883da02fb24572691aaf5975be5", "start_char": 0, "end_char": 896, "text_sha256": "bedd791235b10ff5942ef7177b54bca5b2243883da02fb24572691aaf5975be5"}
    experimental_model
    Steady-state kinetics of purified recombinant human ACC2; LC-MS/MS malonyl-CoA assay
    exposure
    Bicarbonate, ATP, acetyl-CoA and citrate concentration matrices
    limitations
    Kinetic constants are assay properties; they do not define a dietary biotin or B5 threshold.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    Citrate affects both enzyme speed and effective substrate use.
    primary_references
    [b7-p19236960] Characterization of recombinant human acetyl-CoA carboxylase-2 steady-state kinetics. (2009). https://pubmed.ncbi.nlm.nih.gov/19236960/ DOI: 10.1016/j.bbapap.2009.02.004
    tissue_or_cell_type
    Purified human ACC2

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 689–700

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Steady-state kinetics of purified recombinant human ACC2; LC-MS/MS malonyl-CoA assay · source_derived_draft · unverified_draft

    ### b7-acc2-citrate Citrate increased recombinant human ACC2 kcat and kcat/Km for ATP and acetyl-CoA. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Citrate affects both enzyme speed and effective substrate use. organism: Homo sapiens tissue_or_cell_type: Purified human ACC2 experimental_model: Steady-state kinetics of purified recombinant human ACC2; LC-MS/MS malonyl-CoA assay limitations: Kinetic constants are assay properties; they do not define a dietary biotin or B5 threshold. exposure: Bicarbonate, ATP, acetyl-CoA and citrate concentration matrices evidence_span: {"source_cache": "artifacts/biotin-research/19236960.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bedd791235b10ff5942ef7177b54bca5b2243883da02fb24572691aaf5975be5", "start_char": 0, "end_char": 896, "text_sha256": "bedd791235b10ff5942ef7177b54bca5b2243883da02fb24572691aaf5975be5"} [b7-p19236960] Characterization of recombinant human acetyl-CoA carboxylase-2 steady-state kinetics. (2009). https://pubmed.ncbi.nlm.nih.gov/19236960/ DOI: 10.1016/j.bbapap.2009.02.004
    Complete structured claim and evidence

  3. HLCS biotinylation of the human ACACB acceptor fragment was relatively slow and depended hyperbolically on fragment concentration.

    Human holocarboxylase synthetase / HLCS → Human acetyl-CoA carboxylase 2 / ACACB 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
    The two acetyl-CoA carboxylases showed different attachment kinetics from the mitochondrial carboxylase fragments.
    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 442–453

    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-acacb-acceptor HLCS biotinylation of the human ACACB acceptor fragment was relatively slow and depended hyperbolically on fragment concentration. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The two acetyl-CoA carboxylases showed different attachment kinetics from the mitochondrial carboxylase fragments. 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. Ten weeks of metformin significantly increased skeletal-muscle AMPK alpha2 activity with increased Thr172 phosphorylation and decreased acetyl-CoA carboxylase-2 activity in people with type 2 diabetes.

    Metformin → Skeletal-muscle AMPK activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/metformin-research/12086935.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a7807ae8af1c0f438eeff1dd4106d0198681e72f0333f0556786b9151b0df680", "start_char": 0, "end_char": 1474, "text_sha256": "a7807ae8af1c0f438eeff1dd4106d0198681e72f0333f0556786b9151b0df680"}
    experimental_model
    Ten weeks of metformin in people with type 2 diabetes with muscle biopsies
    exposure
    Therapeutic metformin doses for 10 weeks
    limitations
    A human tissue measurement at therapeutic dose. It is an association within a treatment study, not a demonstration that AMPK causes the glucose disposal change.
    nutrient_topic
    Metformin research collection; topical membership is not evidence of a direct clinical effect, and pharmacological exposure is not dietary intake. · Metformin
    organism
    Human
    plain_language
    At the dose people take, the energy sensor is measurably more active in human muscle.
    primary_references
    [metformin-p12086935] Metformin increases AMP-activated protein kinase activity in skeletal muscle of subjects with type 2 diabetes. (2002). https://pubmed.ncbi.nlm.nih.gov/12086935/ DOI: 10.2337/diabetes.51.7.2074
    tissue_or_cell_type
    Skeletal muscle

    Metformin: transport, molecular targets, gut mechanisms and nutrient interactions (2026-09-19) · lines 736–747

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ten weeks of metformin in people with type 2 diabetes with muscle biopsies · source_derived_draft · unverified_draft

    ### metformin-human-muscle-ampk Ten weeks of metformin significantly increased skeletal-muscle AMPK alpha2 activity with increased Thr172 phosphorylation and decreased acetyl-CoA carboxylase-2 activity in people with type 2 diabetes. Condition category: normal nutrient_topic: Metformin research collection; topical membership is not evidence of a direct clinical effect, and pharmacological exposure is not dietary intake. plain_language: At the dose people take, the energy sensor is measurably more active in human muscle. organism: Human tissue_or_cell_type: Skeletal muscle experimental_model: Ten weeks of metformin in people with type 2 diabetes with muscle biopsies limitations: A human tissue measurement at therapeutic dose. It is an association within a treatment study, not a demonstration that AMPK causes the glucose disposal change. exposure: Therapeutic metformin doses for 10 weeks evidence_span: {"source_cache": "artifacts/metformin-research/12086935.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a7807ae8af1c0f438eeff1dd4106d0198681e72f0333f0556786b9151b0df680", "start_char": 0, "end_char": 1474, "text_sha256": "a7807ae8af1c0f438eeff1dd4106d0198681e72f0333f0556786b9151b0df680"} [metformin-p12086935] Metformin increases AMP-activated protein kinase activity in skeletal muscle of subjects with type 2 diabetes. (2002). https://pubmed.ncbi.nlm.nih.gov/12086935/ DOI: 10.2337/diabetes.51.7.2074
    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