Component

Acetoacetyl-CoA

Independent small molecule record; interpretation is limited by each linked claim and its study context.

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. Human mitochondrial acetoacetyl-CoA thiolase ACAT1/T2, a homotetramer, uses coenzyme A to cleave acetoacetyl-CoA into two acetyl-CoA molecules.

    Acetoacetyl-CoA → Acetyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified recombinant human ACAT1/T2 enzyme kinetics and crystal structures
    limitations
    Thiolase chemistry is reversible and shared with ketone metabolism. These experiments do not measure lysine-specific flux. ACAT1 here denotes acetyl-CoA acetyltransferase, not cholesterol acyltransferase SOAT1.
    organism
    Homo sapiens
    plain_language
    The four-carbon intermediate is split into two acetyl-CoA molecules.
    primary_references
    [haapalainen2007] Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function (2007). https://pubmed.ncbi.nlm.nih.gov/17371050/ DOI: 10.1021/bi6026192
    tissue_or_cell_type
    Mitochondrial matrix enzyme; recombinant protein study

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 377–385

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human ACAT1/T2 enzyme kinetics and crystal structures · source_derived_draft · unverified_draft

    ### acat1-acetoacetyl-coa-thiolysis Human mitochondrial acetoacetyl-CoA thiolase ACAT1/T2, a homotetramer, uses coenzyme A to cleave acetoacetyl-CoA into two acetyl-CoA molecules. Plain language: The four-carbon intermediate is split into two acetyl-CoA molecules. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Mitochondrial matrix enzyme; recombinant protein study experimental_model: Purified recombinant human ACAT1/T2 enzyme kinetics and crystal structures limitations: Thiolase chemistry is reversible and shared with ketone metabolism. These experiments do not measure lysine-specific flux. ACAT1 here denotes acetyl-CoA acetyltransferase, not cholesterol acyltransferase SOAT1. [haapalainen2007] Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function (2007). https://pubmed.ncbi.nlm.nih.gov/17371050/ DOI: 10.1021/bi6026192
    Complete structured claim and evidence

What acts on it

  1. The human HADH homodimer reversibly oxidizes (S)-3-hydroxybutyryl-CoA to acetoacetyl-CoA while reducing NAD+ to NADH.

    (S)-3-Hydroxybutyryl-CoA → Acetoacetyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified recombinant human HADH; substrate/product-cofactor crystal complexes
    limitations
    HADH is distinct from HADHA and HSD17B10. This shared reversible reaction supports the downstream route but does not quantify lysine-specific flux in people.
    organism
    Homo sapiens
    plain_language
    The four-carbon hydroxy intermediate is oxidized to a keto intermediate.
    primary_references
    [barycki2000] Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase (2000). https://pubmed.ncbi.nlm.nih.gov/10840044/ DOI: 10.1074/jbc.M004669200
    tissue_or_cell_type
    Mitochondrial short-chain hydroxyacyl-CoA metabolism; recombinant protein study

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 367–375

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human HADH; substrate/product-cofactor crystal complexes · source_derived_draft · unverified_draft

    ### hadh-hydroxybutyryl-coa-oxidation The human HADH homodimer reversibly oxidizes (S)-3-hydroxybutyryl-CoA to acetoacetyl-CoA while reducing NAD+ to NADH. Plain language: The four-carbon hydroxy intermediate is oxidized to a keto intermediate. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Mitochondrial short-chain hydroxyacyl-CoA metabolism; recombinant protein study experimental_model: Purified recombinant human HADH; substrate/product-cofactor crystal complexes limitations: HADH is distinct from HADHA and HSD17B10. This shared reversible reaction supports the downstream route but does not quantify lysine-specific flux in people. [barycki2000] Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase (2000). https://pubmed.ncbi.nlm.nih.gov/10840044/ DOI: 10.1074/jbc.M004669200
    Complete structured claim and evidence

  2. OXCT1 transfers CoA from succinyl-CoA to acetoacetate, yielding acetoacetyl-CoA and succinate.

    Acetoacetate → Acetoacetyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and indexed full-text introduction, PMC3825524
    experimental_model
    Human SCOT structure; described ketolysis reaction.
    limitations
    Production of ketones and ability to use them are different capacities.
    nutrient_topic
    Fasting physiological-state collection; human protocols, cellular deprivation and refeeding are distinguished. · Fasting / abstention from energy intake
    plain_language
    Using ketones requires a separate activation step.
    primary_references
    A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23420214/ · DOI 10.1007/s10545-013-9589-z

    Fasting: fuel switching, nutrient sensing, ketone signaling, nutrient dependencies and refeeding (2026-09-18) · lines 144–150

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human SCOT structure; described ketolysis reaction. · source_derived_draft · unverified_draft

    ## fast-scot Using ketones requires a separate activation step. OXCT1 transfers CoA from succinyl-CoA to acetoacetate, yielding acetoacetyl-CoA and succinate. Model: Human SCOT structure; described ketolysis reaction. Limitations: Production of ketones and ability to use them are different capacities. Evidence access: Primary abstract and indexed full-text introduction, PMC3825524 A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23420214/ · DOI 10.1007/s10545-013-9589-z
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Mitochondrial HMGCS2 catalyzes condensation of acetyl-CoA and acetoacetyl-CoA to form HMG-CoA.

    Acetyl-CoA → (S)-3-Hydroxy-3-methylglutaryl-CoA source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human HMGCS1/HMGCS2 structures and catalytic reaction description.
    limitations
    The mitochondrial isoform is distinct from cytosolic HMGCS1 in sterol synthesis.
    nutrient_topic
    Fasting physiological-state collection; human protocols, cellular deprivation and refeeding are distinguished. · Fasting / abstention from energy intake
    plain_language
    Two carbon-carrying molecules combine on the ketone-production route.
    primary_references
    Crystal structures of human HMG-CoA synthase isoforms provide insights into inherited ketogenesis disorders and inhibitor design. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20346956/ · DOI 10.1016/j.jmb.2010.03.034

    Fasting: fuel switching, nutrient sensing, ketone signaling, nutrient dependencies and refeeding (2026-09-18) · lines 104–110

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human HMGCS1/HMGCS2 structures and catalytic reaction description. · source_derived_draft · unverified_draft

    ## fast-hmgcs2 Two carbon-carrying molecules combine on the ketone-production route. Mitochondrial HMGCS2 catalyzes condensation of acetyl-CoA and acetoacetyl-CoA to form HMG-CoA. Model: Human HMGCS1/HMGCS2 structures and catalytic reaction description. Limitations: The mitochondrial isoform is distinct from cytosolic HMGCS1 in sterol synthesis. Evidence access: Primary abstract Crystal structures of human HMG-CoA synthase isoforms provide insights into inherited ketogenesis disorders and inhibitor design. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20346956/ · DOI 10.1016/j.jmb.2010.03.034
    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