Component

(S)-3-Hydroxy-3-methylglutaryl-CoA

Context-specific entity; species, compartment and exposure are stated on each 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. Human HMGCL cleaves HMG-CoA to acetoacetate and acetyl-CoA.

    (S)-3-Hydroxy-3-methylglutaryl-CoA → Acetoacetate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and indexed full-text introduction, PMC2924059
    experimental_model
    Human HMGCL structural study; reaction in primary introduction.
    limitations
    Mitochondrial pathway; net flux is not inferred from structure alone.
    nutrient_topic
    Fasting physiological-state collection; human protocols, cellular deprivation and refeeding are distinguished. · Fasting / abstention from energy intake
    plain_language
    A second enzyme releases the first ketone body.
    primary_references
    Functional insights into human HMG-CoA lyase from structures of Acyl-CoA-containing ternary complexes. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20558737/ · DOI 10.1074/jbc.M110.139931

    Fasting: fuel switching, nutrient sensing, ketone signaling, nutrient dependencies and refeeding (2026-09-18) · lines 112–118

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human HMGCL structural study; reaction in primary introduction. · source_derived_draft · unverified_draft

    ## fast-hmgcl A second enzyme releases the first ketone body. Human HMGCL cleaves HMG-CoA to acetoacetate and acetyl-CoA. Model: Human HMGCL structural study; reaction in primary introduction. Limitations: Mitochondrial pathway; net flux is not inferred from structure alone. Evidence access: Primary abstract and indexed full-text introduction, PMC2924059 Functional insights into human HMG-CoA lyase from structures of Acyl-CoA-containing ternary complexes. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20558737/ · DOI 10.1074/jbc.M110.139931
    Complete structured claim and evidence

What acts on it

  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

Where it participates (unsigned role)

  1. Monacolin K acid sodium salt competitively inhibited rat liver HMG-CoA reductase with respect to HMG-CoA; the reported Ki was 0.49 nM.

    Monacolin K hydroxy-acid sodium salt → Rat HMG-CoA reductase / Hmgcr source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary PDF, p335 and Figure 3 visually inspected
    experimental_model
    Partially purified rat liver microsomal reductase; radiolabeled product assay.
    limitations
    Assay-specific inhibition constant, not a human plasma threshold or potency of an entire rice product.
    nutrient_topic
    Red yeast rice collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Red yeast rice
    plain_language
    The active preparation competed with the enzyme substrate.
    primary_references
    [7380744] Monacolin K, a new hypocholesterolemic agent that specifically inhibits 3-hydroxy-3-methylglutaryl coenzyme A reductase. · 1980 · https://pubmed.ncbi.nlm.nih.gov/7380744/ · DOI 10.7164/antibiotics.33.334

    Red yeast rice: constituents, mevalonate, CoQ and product-specific interactions (2026-09-20) · lines 52–58

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Partially purified rat liver microsomal reductase; radiolabeled product assay. · source_derived_draft · unverified_draft

    ## red-yeast-rice-hmgcr-binding The active preparation competed with the enzyme substrate. Monacolin K acid sodium salt competitively inhibited rat liver HMG-CoA reductase with respect to HMG-CoA; the reported Ki was 0.49 nM. Model: Partially purified rat liver microsomal reductase; radiolabeled product assay. Limitations: Assay-specific inhibition constant, not a human plasma threshold or potency of an entire rice product. Evidence access: Primary PDF, p335 and Figure 3 visually inspected [7380744] Monacolin K, a new hypocholesterolemic agent that specifically inhibits 3-hydroxy-3-methylglutaryl coenzyme A reductase. · 1980 · https://pubmed.ncbi.nlm.nih.gov/7380744/ · DOI 10.7164/antibiotics.33.334
    Complete structured claim and evidence

  2. Human HMG-CoA reductase catalyzes mevalonate formation; substrate/cofactor-bound structures locate HMG-CoA and the nicotinamide cofactor in the catalytic domain.

    HMG-CoA reductase (HMGCR) → Mevalonate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human recombinant catalytic-domain crystallography and biochemical background.
    limitations
    Shared human machinery; the source is not an experiment administering red yeast rice.
    nutrient_topic
    Red yeast rice collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Red yeast rice
    plain_language
    This enzyme supplies a shared precursor pathway.
    primary_references
    [10698924] Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10698924/ · DOI 10.1093/emboj/19.5.819

    Red yeast rice: constituents, mevalonate, CoQ and product-specific interactions (2026-09-20) · lines 76–82

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant catalytic-domain crystallography and biochemical background. · source_derived_draft · unverified_draft

    ## red-yeast-rice-human-mevalonate-machinery This enzyme supplies a shared precursor pathway. Human HMG-CoA reductase catalyzes mevalonate formation; substrate/cofactor-bound structures locate HMG-CoA and the nicotinamide cofactor in the catalytic domain. Model: Human recombinant catalytic-domain crystallography and biochemical background. Limitations: Shared human machinery; the source is not an experiment administering red yeast rice. Evidence access: Primary abstract [10698924] Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10698924/ · DOI 10.1093/emboj/19.5.819
    Complete structured claim and evidence

  3. In HMGCL ternary structures Mg2+ coordinates His233, His235, Asp42, water and substrate/inhibitor oxygen atoms.

    Mg2+ → Human HMG-CoA lyase / HMGCL source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human wild-type inhibitor complex and R41M substrate complex.
    limitations
    Structural dependence does not show that dietary magnesium limits ketosis in a replete person.
    nutrient_topic
    Fasting physiological-state collection; human protocols, cellular deprivation and refeeding are distinguished. · Fasting / abstention from energy intake
    plain_language
    Magnesium participates directly in this ketone-producing enzyme.
    primary_references
    Functional insights into human HMG-CoA lyase from structures of Acyl-CoA-containing ternary complexes. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20558737/ · DOI 10.1074/jbc.M110.139931

    Fasting: fuel switching, nutrient sensing, ketone signaling, nutrient dependencies and refeeding (2026-09-18) · lines 120–126

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human wild-type inhibitor complex and R41M substrate complex. · source_derived_draft · unverified_draft

    ## fast-hmgcl-magnesium Magnesium participates directly in this ketone-producing enzyme. In HMGCL ternary structures Mg2+ coordinates His233, His235, Asp42, water and substrate/inhibitor oxygen atoms. Model: Human wild-type inhibitor complex and R41M substrate complex. Limitations: Structural dependence does not show that dietary magnesium limits ketosis in a replete person. Evidence access: Primary abstract Functional insights into human HMG-CoA lyase from structures of Acyl-CoA-containing ternary complexes. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20558737/ · DOI 10.1074/jbc.M110.139931
    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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