Component
Rat HMG-CoA reductase / Hmgcr
Context-specific entity; species, compartment and exposure are stated on each claim.
3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What acts on it
Monacolin K acid sodium salt competitively inhibited rat liver HMG-CoA reductase with respect to HMG-CoA; the reported Ki was 0.49 nM.
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
Where it participates (unsigned role)
Monacolin K inhibited lipid labeling from acetate or HMG-CoA, but did not inhibit incorporation from supplied mevalonate at concentrations up to 10 mM.
Experimental context and source evidence
- evidence_access
- Primary PDF, p335 visually inspected
- experimental_model
- Rat liver cell-free nonsaponifiable-lipid synthesis; lactone and acid preparations tested.
- limitations
- A biochemical bypass is not a clinical repletion strategy; the 10 mM figure applies to tested monacolin concentrations, not human exposure.
- nutrient_topic
- Red yeast rice collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Red yeast rice
- plain_language
- Supplying the downstream intermediate bypassed the inhibited step in this assay.
- 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 68–74
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat liver cell-free nonsaponifiable-lipid synthesis; lactone and acid preparations tested. · source_derived_draft · unverified_draft
## red-yeast-rice-mevalonate-bypass Supplying the downstream intermediate bypassed the inhibited step in this assay. Monacolin K inhibited lipid labeling from acetate or HMG-CoA, but did not inhibit incorporation from supplied mevalonate at concentrations up to 10 mM. Model: Rat liver cell-free nonsaponifiable-lipid synthesis; lactone and acid preparations tested. Limitations: A biochemical bypass is not a clinical repletion strategy; the 10 mM figure applies to tested monacolin concentrations, not human exposure. Evidence access: Primary PDF, p335 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 evidenceThe same monacolin K inhibition was noncompetitive with respect to NADPH.
Experimental context and source evidence
- evidence_access
- Primary PDF, p335 visually inspected
- experimental_model
- Rat liver reductase kinetics in the 1980 study.
- limitations
- Not evidence of NADPH depletion, niacin deficiency or reversal by niacin supplementation.
- nutrient_topic
- Red yeast rice collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Red yeast rice
- plain_language
- The reducing cofactor and the competing substrate have different roles.
- 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 60–66
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat liver reductase kinetics in the 1980 study. · source_derived_draft · unverified_draft
## red-yeast-rice-nadph-noncompetition The reducing cofactor and the competing substrate have different roles. The same monacolin K inhibition was noncompetitive with respect to NADPH. Model: Rat liver reductase kinetics in the 1980 study. Limitations: Not evidence of NADPH depletion, niacin deficiency or reversal by niacin supplementation. Evidence access: Primary PDF, p335 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
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.