Component

Saccharomyces cerevisiae alpha-glucosidase in the 2024 pigment assay

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 acts on it

  1. Docking proposed ankaflavin binding outside the catalytic center of the alpha-glucosidase model.

    Ankaflavin → Saccharomyces cerevisiae alpha-glucosidase in the 2024 pigment assay source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text PMC11120408
    experimental_model
    Computational analysis accompanying enzyme kinetics.
    limitations
    No ligand-bound crystal structure or direct human-enzyme result follows.
    nutrient_topic
    Red yeast rice collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Red yeast rice
    plain_language
    The proposed contact site remains a model.
    primary_references
    [38790873] Revealing the Hypoglycemic Effect of Red Yeast Rice: Perspectives from the Inhibition of α-Glucosidase and the Anti-Glycation Capability by Ankaflavin and Monascin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38790873/ · DOI 10.3390/foods13101573

    Red yeast rice: constituents, mevalonate, CoQ and product-specific interactions (2026-09-20) · lines 284–290

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Computational analysis accompanying enzyme kinetics. · source_derived_draft · unverified_draft

    ## red-yeast-rice-ankaflavin-docking The proposed contact site remains a model. Docking proposed ankaflavin binding outside the catalytic center of the alpha-glucosidase model. Model: Computational analysis accompanying enzyme kinetics. Limitations: No ligand-bound crystal structure or direct human-enzyme result follows. Evidence access: Primary full text PMC11120408 [38790873] Revealing the Hypoglycemic Effect of Red Yeast Rice: Perspectives from the Inhibition of α-Glucosidase and the Anti-Glycation Capability by Ankaflavin and Monascin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38790873/ · DOI 10.3390/foods13101573
    Complete structured claim and evidence

  2. Ankaflavin inhibited yeast alpha-glucosidase with an IC50 of 126.5 micromolar and mixed-type kinetics.

    Ankaflavin → Saccharomyces cerevisiae alpha-glucosidase in the 2024 pigment assay source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text PMC11120408
    experimental_model
    Saccharomyces cerevisiae enzyme, pNPG substrate, pH 6.8; one-hour preincubation and 30-minute reaction.
    limitations
    Yeast enzyme, not human intestinal maltase-glucoamylase or sucrase-isomaltase; potency is not clinical glucose lowering.
    nutrient_topic
    Red yeast rice collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Red yeast rice
    plain_language
    The isolated pigment inhibited a carbohydrate-cleaving enzyme preparation.
    primary_references
    [38790873] Revealing the Hypoglycemic Effect of Red Yeast Rice: Perspectives from the Inhibition of α-Glucosidase and the Anti-Glycation Capability by Ankaflavin and Monascin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38790873/ · DOI 10.3390/foods13101573

    Red yeast rice: constituents, mevalonate, CoQ and product-specific interactions (2026-09-20) · lines 276–282

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Saccharomyces cerevisiae enzyme, pNPG substrate, pH 6.8; one-hour preincubation and 30-minute reaction. · source_derived_draft · unverified_draft

    ## red-yeast-rice-ankaflavin-glucosidase The isolated pigment inhibited a carbohydrate-cleaving enzyme preparation. Ankaflavin inhibited yeast alpha-glucosidase with an IC50 of 126.5 micromolar and mixed-type kinetics. Model: Saccharomyces cerevisiae enzyme, pNPG substrate, pH 6.8; one-hour preincubation and 30-minute reaction. Limitations: Yeast enzyme, not human intestinal maltase-glucoamylase or sucrase-isomaltase; potency is not clinical glucose lowering. Evidence access: Primary full text PMC11120408 [38790873] Revealing the Hypoglycemic Effect of Red Yeast Rice: Perspectives from the Inhibition of α-Glucosidase and the Anti-Glycation Capability by Ankaflavin and Monascin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38790873/ · DOI 10.3390/foods13101573
    Complete structured claim and evidence

  3. Docking proposed monascin binding outside the catalytic center of the alpha-glucosidase model.

    Monascin → Saccharomyces cerevisiae alpha-glucosidase in the 2024 pigment assay source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text PMC11120408
    experimental_model
    Computational analysis accompanying enzyme kinetics.
    limitations
    No ligand-bound crystal structure or direct human-enzyme result follows.
    nutrient_topic
    Red yeast rice collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Red yeast rice
    plain_language
    The proposed contact site remains a model.
    primary_references
    [38790873] Revealing the Hypoglycemic Effect of Red Yeast Rice: Perspectives from the Inhibition of α-Glucosidase and the Anti-Glycation Capability by Ankaflavin and Monascin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38790873/ · DOI 10.3390/foods13101573

    Red yeast rice: constituents, mevalonate, CoQ and product-specific interactions (2026-09-20) · lines 300–306

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Computational analysis accompanying enzyme kinetics. · source_derived_draft · unverified_draft

    ## red-yeast-rice-monascin-docking The proposed contact site remains a model. Docking proposed monascin binding outside the catalytic center of the alpha-glucosidase model. Model: Computational analysis accompanying enzyme kinetics. Limitations: No ligand-bound crystal structure or direct human-enzyme result follows. Evidence access: Primary full text PMC11120408 [38790873] Revealing the Hypoglycemic Effect of Red Yeast Rice: Perspectives from the Inhibition of α-Glucosidase and the Anti-Glycation Capability by Ankaflavin and Monascin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38790873/ · DOI 10.3390/foods13101573
    Complete structured claim and evidence

  4. Monascin inhibited yeast alpha-glucosidase with an IC50 of 302.6 micromolar and mixed-type kinetics.

    Monascin → Saccharomyces cerevisiae alpha-glucosidase in the 2024 pigment assay source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text PMC11120408
    experimental_model
    Saccharomyces cerevisiae enzyme, pNPG substrate, pH 6.8; one-hour preincubation and 30-minute reaction.
    limitations
    Yeast enzyme, not human intestinal maltase-glucoamylase or sucrase-isomaltase; potency is not clinical glucose lowering.
    nutrient_topic
    Red yeast rice collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Red yeast rice
    plain_language
    The isolated pigment inhibited a carbohydrate-cleaving enzyme preparation.
    primary_references
    [38790873] Revealing the Hypoglycemic Effect of Red Yeast Rice: Perspectives from the Inhibition of α-Glucosidase and the Anti-Glycation Capability by Ankaflavin and Monascin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38790873/ · DOI 10.3390/foods13101573

    Red yeast rice: constituents, mevalonate, CoQ and product-specific interactions (2026-09-20) · lines 292–298

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Saccharomyces cerevisiae enzyme, pNPG substrate, pH 6.8; one-hour preincubation and 30-minute reaction. · source_derived_draft · unverified_draft

    ## red-yeast-rice-monascin-glucosidase The isolated pigment inhibited a carbohydrate-cleaving enzyme preparation. Monascin inhibited yeast alpha-glucosidase with an IC50 of 302.6 micromolar and mixed-type kinetics. Model: Saccharomyces cerevisiae enzyme, pNPG substrate, pH 6.8; one-hour preincubation and 30-minute reaction. Limitations: Yeast enzyme, not human intestinal maltase-glucoamylase or sucrase-isomaltase; potency is not clinical glucose lowering. Evidence access: Primary full text PMC11120408 [38790873] Revealing the Hypoglycemic Effect of Red Yeast Rice: Perspectives from the Inhibition of α-Glucosidase and the Anti-Glycation Capability by Ankaflavin and Monascin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38790873/ · DOI 10.3390/foods13101573
    Complete structured claim and evidence

  5. Lariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM.

    Lariciresinol, enantiomer unresolved → Saccharomyces cerevisiae alpha-glucosidase in the 2024 pigment assay source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not applicable
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    α-Glucosidase inhibitory assay with molecular docking
    exposure
    Lariciresinol
    limitations
    The enantiomer is not stated. The inhibition constant is about 150-fold below the inhibitory concentration, which is a large gap for a competitive inhibitor and depends on the substrate concentration used.
    organism
    α-Glucosidase inhibitory assay with molecular docking
    plain_language
    Lariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM.
    primary_references
    Lariciresinol Displays Anti-Diabetic Activity through Inhibition of α-Glucosidase and Activation and Enhancement of Insulin Signaling. (2022). https://pubmed.ncbi.nlm.nih.gov/35490401/ DOI: 10.1002/mnfr.202100910
    route
    In vitro
    tissue
    Carbohydrate-hydrolysing enzyme activity

    Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22) · lines 165–174

    Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft

    ## lariciresinol-inhibits-alpha-glucosidase Lariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM. Model/species: α-Glucosidase inhibitory assay with molecular docking Tissue/system: Carbohydrate-hydrolysing enzyme activity Exposure: Lariciresinol Route: In vitro Duration: Not applicable Limits: The enantiomer is not stated. The inhibition constant is about 150-fold below the inhibitory concentration, which is a large gap for a competitive inhibitor and depends on the substrate concentration used. Primary reference: Lariciresinol Displays Anti-Diabetic Activity through Inhibition of α-Glucosidase and Activation and Enhancement of Insulin Signaling. (2022). https://pubmed.ncbi.nlm.nih.gov/35490401/ DOI: 10.1002/mnfr.202100910 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    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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