Component

Malonyl-CoA

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

7 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. Wild-type human CPT1B showed high-affinity malonyl-CoA binding and inhibition in recombinant mitochondrial assays.

    Malonyl-CoA → Human carnitine palmitoyltransferase 1B / CPT1B source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/10651636.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400", "start_char": 0, "end_char": 1542, "text_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400"}
    experimental_model
    Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria
    exposure
    Malonyl-CoA binding and activity assays
    limitations
    Expression host is yeast; these data concern human CPT1B, not every CPT1 isoform or a biotin supplementation outcome.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    Malonyl-CoA links the carboxylase pathway to the carnitine-dependent fat-entry step.
    primary_references
    [b7-p10651636] The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding. (2000). https://pubmed.ncbi.nlm.nih.gov/10651636/ DOI: 10.1021/bi9918700
    tissue_or_cell_type
    Recombinant human muscle/heart CPT1B

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 741–752

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria · source_derived_draft · unverified_draft

    ### b7-malonyl-cpt1b Wild-type human CPT1B showed high-affinity malonyl-CoA binding and inhibition in recombinant mitochondrial assays. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Malonyl-CoA links the carboxylase pathway to the carnitine-dependent fat-entry step. organism: Homo sapiens tissue_or_cell_type: Recombinant human muscle/heart CPT1B experimental_model: Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria limitations: Expression host is yeast; these data concern human CPT1B, not every CPT1 isoform or a biotin supplementation outcome. exposure: Malonyl-CoA binding and activity assays evidence_span: {"source_cache": "artifacts/biotin-research/10651636.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400", "start_char": 0, "end_char": 1542, "text_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400"} [b7-p10651636] The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding. (2000). https://pubmed.ncbi.nlm.nih.gov/10651636/ DOI: 10.1021/bi9918700
    Complete structured claim and evidence

What acts on it

  1. Deleting the first 28 residues of human CPT1B removed high-affinity malonyl-CoA binding and inhibition despite retained catalytic activity.

    Human CPT1B N-terminal 28-residue deletion → Malonyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/10651636.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400", "start_char": 0, "end_char": 1542, "text_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400"}
    experimental_model
    Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria
    exposure
    Malonyl-CoA binding and activity assays
    limitations
    Expression host is yeast; these data concern human CPT1B, not every CPT1 isoform or a biotin supplementation outcome.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    This engineered change separates the enzyme brake from its basic catalytic function.
    primary_references
    [b7-p10651636] The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding. (2000). https://pubmed.ncbi.nlm.nih.gov/10651636/ DOI: 10.1021/bi9918700
    tissue_or_cell_type
    Recombinant human muscle/heart CPT1B

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 754–765

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria · source_derived_draft · unverified_draft

    ### b7-cpt1b-delta28 Deleting the first 28 residues of human CPT1B removed high-affinity malonyl-CoA binding and inhibition despite retained catalytic activity. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: This engineered change separates the enzyme brake from its basic catalytic function. organism: Homo sapiens tissue_or_cell_type: Recombinant human muscle/heart CPT1B experimental_model: Human CPT1B wild type and N-terminal deletions expressed in yeast mitochondria limitations: Expression host is yeast; these data concern human CPT1B, not every CPT1 isoform or a biotin supplementation outcome. exposure: Malonyl-CoA binding and activity assays evidence_span: {"source_cache": "artifacts/biotin-research/10651636.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400", "start_char": 0, "end_char": 1542, "text_sha256": "e99728ef83700f17a810421385b71ea243576419df807dc4749b588beb01d400"} [b7-p10651636] The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding. (2000). https://pubmed.ncbi.nlm.nih.gov/10651636/ DOI: 10.1021/bi9918700
    Complete structured claim and evidence

  2. At 4 hours after feeding, liver malonyl-CoA, an allosteric inhibitor of carnitine palmitoyl-transferase, was significantly lower in the acetic acid group than in the control group, along with a lower serum lactate concentration and a lower ratio of insulin to glucagon, indicating the possibility of a transient enhancement of fatty acid oxidation in liver.

    Acetic acid → Malonyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/acetate-research/16277773.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "305aa81aca9908a350132a7c7dcc42c86be0b6030c70f51b5fe0c8971e75bcfe", "start_char": 0, "end_char": 1594, "text_sha256": "305aa81aca9908a350132a7c7dcc42c86be0b6030c70f51b5fe0c8971e75bcfe"}
    experimental_model
    Rats meal-fed once daily for 10 days, then sampled 4, 8 or 24 hours after feeding
    exposure
    0.7 g/kg-diet acetic acid in a 9 g meal, with sampling across the daily cycle
    limitations
    Adds the time dimension that single-timepoint studies miss. The effects were present at 4 hours and the authors explicitly rule out supercompensation.
    nutrient_topic
    Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. · Acetic acid
    organism
    Rat
    plain_language
    The brake on fat burning came off for a few hours.
    primary_references
    [acetate-p16277773] Effect of acetic acid feeding on the circadian changes in glycogen and metabolites of glucose and lipid in liver and skeletal muscle of rats. (2005). https://pubmed.ncbi.nlm.nih.gov/16277773/ DOI: 10.1079/bjn20051545
    tissue_or_cell_type
    Liver and skeletal muscle

    Acetic acid: the ingested acid, the receptors acetate binds, the acetyl-CoA it becomes, and the acetyl groups that reach histones (2026-09-21) · lines 472–483

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rats meal-fed once daily for 10 days, then sampled 4, 8 or 24 hours after feeding · source_derived_draft · unverified_draft

    ### acetate-malonyl-coa-fall At 4 hours after feeding, liver malonyl-CoA, an allosteric inhibitor of carnitine palmitoyl-transferase, was significantly lower in the acetic acid group than in the control group, along with a lower serum lactate concentration and a lower ratio of insulin to glucagon, indicating the possibility of a transient enhancement of fatty acid oxidation in liver. Condition category: normal nutrient_topic: Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. plain_language: The brake on fat burning came off for a few hours. organism: Rat tissue_or_cell_type: Liver and skeletal muscle experimental_model: Rats meal-fed once daily for 10 days, then sampled 4, 8 or 24 hours after feeding limitations: Adds the time dimension that single-timepoint studies miss. The effects were present at 4 hours and the authors explicitly rule out supercompensation. exposure: 0.7 g/kg-diet acetic acid in a 9 g meal, with sampling across the daily cycle evidence_span: {"source_cache": "artifacts/acetate-research/16277773.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "305aa81aca9908a350132a7c7dcc42c86be0b6030c70f51b5fe0c8971e75bcfe", "start_char": 0, "end_char": 1594, "text_sha256": "305aa81aca9908a350132a7c7dcc42c86be0b6030c70f51b5fe0c8971e75bcfe"} [acetate-p16277773] Effect of acetic acid feeding on the circadian changes in glycogen and metabolites of glucose and lipid in liver and skeletal muscle of rats. (2005). https://pubmed.ncbi.nlm.nih.gov/16277773/ DOI: 10.1079/bjn20051545
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Human ACC1 uses biotin-dependent carboxylation of acetyl-CoA to generate malonyl-CoA.

    Human acetyl-CoA carboxylase 1 / ACACA → Acetyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/39383219.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5f7d3cd6a5865a03b8dc9c510f60249ee2c9f6516773780e5d7b4aef0a9b2db8", "start_char": 0, "end_char": 309, "text_sha256": "b094342ce091c8f919d065311ecd04ddd0c6b9b2824ba8adedd5768424a81a71"}
    experimental_model
    Cryo-EM of endogenous and recombinant human ACC1 filaments
    exposure
    Inactive substrate-containing and dephosphorylated/citrate-treated states
    limitations
    Filament presence alone does not mean enzyme activation; the paper resolved both active and inactive arrangements.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    ACC1 makes a building block used in fatty-acid synthesis.
    primary_references
    [b7-p39383219] Filament structures unveil the dynamic organization of human acetyl-CoA carboxylase. (2024). https://pubmed.ncbi.nlm.nih.gov/39383219/ DOI: 10.1126/sciadv.ado4880
    tissue_or_cell_type
    Purified human ACC1

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 637–648

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM of endogenous and recombinant human ACC1 filaments · source_derived_draft · unverified_draft

    ### b7-acc1-reaction Human ACC1 uses biotin-dependent carboxylation of acetyl-CoA to generate malonyl-CoA. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: ACC1 makes a building block used in fatty-acid synthesis. organism: Homo sapiens tissue_or_cell_type: Purified human ACC1 experimental_model: Cryo-EM of endogenous and recombinant human ACC1 filaments limitations: Filament presence alone does not mean enzyme activation; the paper resolved both active and inactive arrangements. exposure: Inactive substrate-containing and dephosphorylated/citrate-treated states evidence_span: {"source_cache": "artifacts/biotin-research/39383219.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5f7d3cd6a5865a03b8dc9c510f60249ee2c9f6516773780e5d7b4aef0a9b2db8", "start_char": 0, "end_char": 309, "text_sha256": "b094342ce091c8f919d065311ecd04ddd0c6b9b2824ba8adedd5768424a81a71"} [b7-p39383219] Filament structures unveil the dynamic organization of human acetyl-CoA carboxylase. (2024). https://pubmed.ncbi.nlm.nih.gov/39383219/ DOI: 10.1126/sciadv.ado4880
    Complete structured claim and evidence

  2. Acacb-null mice had approximately 30-fold lower muscle malonyl-CoA and 10-fold lower heart malonyl-CoA than wild-type mice.

    Acacb-null mouse genotype → Mouse muscle malonyl-CoA concentration source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/biotin-research/11283375.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d8998a50f9e50b7528afe992760b547dcf705d04f873f0f4f11ed81e71b48249", "start_char": 0, "end_char": 894, "text_sha256": "d8998a50f9e50b7528afe992760b547dcf705d04f873f0f4f11ed81e71b48249"}
    experimental_model
    Acacb-knockout mice compared with wild type
    exposure
    Genetic deletion
    limitations
    Loss of one enzyme in mice is not dietary biotin deficiency, which can affect several enzymes; this is not evidence for inducing deficiency to change body weight.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Mus musculus
    plain_language
    Loss of ACC2 lowered the local metabolite that helps restrain fatty-acid entry.
    primary_references
    [b7-p11283375] Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2. (2001). https://pubmed.ncbi.nlm.nih.gov/11283375/ DOI: 10.1126/science.1056843
    tissue_or_cell_type
    Heart, skeletal muscle and adipose tissue
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 715–726

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Acacb-knockout mice compared with wild type · source_derived_draft · unverified_draft

    ### b7-acc2-null-malonyl Acacb-null mice had approximately 30-fold lower muscle malonyl-CoA and 10-fold lower heart malonyl-CoA than wild-type mice. Condition category: machinery_impairment nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Loss of ACC2 lowered the local metabolite that helps restrain fatty-acid entry. organism: Mus musculus tissue_or_cell_type: Heart, skeletal muscle and adipose tissue experimental_model: Acacb-knockout mice compared with wild type limitations: Loss of one enzyme in mice is not dietary biotin deficiency, which can affect several enzymes; this is not evidence for inducing deficiency to change body weight. exposure: Genetic deletion evidence_span: {"source_cache": "artifacts/biotin-research/11283375.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d8998a50f9e50b7528afe992760b547dcf705d04f873f0f4f11ed81e71b48249", "start_char": 0, "end_char": 894, "text_sha256": "d8998a50f9e50b7528afe992760b547dcf705d04f873f0f4f11ed81e71b48249"} [b7-p11283375] Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2. (2001). https://pubmed.ncbi.nlm.nih.gov/11283375/ DOI: 10.1126/science.1056843
    Complete structured claim and evidence

  3. Soleus fatty-acid oxidation was about 30% higher in Acacb-null mice than in wild-type mice.

    Acacb-null mouse genotype → Mouse muscle fatty-acid oxidation source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/biotin-research/11283375.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d8998a50f9e50b7528afe992760b547dcf705d04f873f0f4f11ed81e71b48249", "start_char": 0, "end_char": 894, "text_sha256": "d8998a50f9e50b7528afe992760b547dcf705d04f873f0f4f11ed81e71b48249"}
    experimental_model
    Acacb-knockout mice compared with wild type
    exposure
    Genetic deletion
    limitations
    Loss of one enzyme in mice is not dietary biotin deficiency, which can affect several enzymes; this is not evidence for inducing deficiency to change body weight.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Mus musculus
    plain_language
    The enzyme deletion changed fuel use in mouse muscle.
    primary_references
    [b7-p11283375] Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2. (2001). https://pubmed.ncbi.nlm.nih.gov/11283375/ DOI: 10.1126/science.1056843
    tissue_or_cell_type
    Heart, skeletal muscle and adipose tissue
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 728–739

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Acacb-knockout mice compared with wild type · source_derived_draft · unverified_draft

    ### b7-acc2-null-oxidation Soleus fatty-acid oxidation was about 30% higher in Acacb-null mice than in wild-type mice. Condition category: machinery_impairment nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme deletion changed fuel use in mouse muscle. organism: Mus musculus tissue_or_cell_type: Heart, skeletal muscle and adipose tissue experimental_model: Acacb-knockout mice compared with wild type limitations: Loss of one enzyme in mice is not dietary biotin deficiency, which can affect several enzymes; this is not evidence for inducing deficiency to change body weight. exposure: Genetic deletion evidence_span: {"source_cache": "artifacts/biotin-research/11283375.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d8998a50f9e50b7528afe992760b547dcf705d04f873f0f4f11ed81e71b48249", "start_char": 0, "end_char": 894, "text_sha256": "d8998a50f9e50b7528afe992760b547dcf705d04f873f0f4f11ed81e71b48249"} [b7-p11283375] Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2. (2001). https://pubmed.ncbi.nlm.nih.gov/11283375/ DOI: 10.1126/science.1056843
    Complete structured claim and evidence

  4. 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

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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