Component

Mouse branched-chain alpha-ketoacid dehydrogenase complex

Context-specific entity; species, compartment and exposure are stated on each claim.

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. BAT-specific BCAA catabolic impairment reduced BCAA clearance and thermogenic fuel oxidation and promoted glucose intolerance in the tested mice.

    Mouse branched-chain alpha-ketoacid dehydrogenase complex → Systemic BCAA clearance supported by mouse BAT source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Mouse BAT-targeted Bckdha manipulation and metabolic assays.
    limitations
    Mixed BCAA pathway; not a claim that isolated isoleucine intake causes obesity.
    nutrient_topic
    L-Isoleucine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Isoleucine
    plain_language
    Loss of a tissue processing route changed whole-body amino-acid handling.
    primary_references
    BCAA catabolism in brown fat controls energy homeostasis through SLC25A44. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31435015/ · DOI 10.1038/s41586-019-1503-x
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Isoleucine: transport, translation, catabolism and cross-nutrient mechanisms (2026-09-19) · lines 66–72

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse BAT-targeted Bckdha manipulation and metabolic assays. · source_derived_draft · unverified_draft

    ## isoleucine-brown-fat-catabolic-loss Loss of a tissue processing route changed whole-body amino-acid handling. BAT-specific BCAA catabolic impairment reduced BCAA clearance and thermogenic fuel oxidation and promoted glucose intolerance in the tested mice. Model: Mouse BAT-targeted Bckdha manipulation and metabolic assays. Limitations: Mixed BCAA pathway; not a claim that isolated isoleucine intake causes obesity. Evidence access: Primary full text BCAA catabolism in brown fat controls energy homeostasis through SLC25A44. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31435015/ · DOI 10.1038/s41586-019-1503-x
    Complete structured claim and evidence

What acts on it

  1. PP2Cm bound the BCKDH complex and promoted substrate-dependent dephosphorylation of E1-alpha Ser293.

    Mouse BCKDH phosphatase PP2Cm / Ppm1k → Mouse branched-chain alpha-ketoacid dehydrogenase complex source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Mouse and cultured-cell protein interaction/phosphorylation experiments.
    limitations
    Rate depends on substrate and regulatory state; this is a shared BCAA step.
    nutrient_topic
    L-Isoleucine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Isoleucine
    plain_language
    A phosphatase removes the inhibitory mark and permits more breakdown.
    primary_references
    Protein phosphatase 2Cm is a critical regulator of branched-chain amino acid catabolism in mice and cultured cells. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19411760/ · DOI 10.1172/JCI38151

    L-Isoleucine: transport, translation, catabolism and cross-nutrient mechanisms (2026-09-19) · lines 274–280

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse and cultured-cell protein interaction/phosphorylation experiments. · source_derived_draft · unverified_draft

    ## isoleucine-ppm1k-activation A phosphatase removes the inhibitory mark and permits more breakdown. PP2Cm bound the BCKDH complex and promoted substrate-dependent dephosphorylation of E1-alpha Ser293. Model: Mouse and cultured-cell protein interaction/phosphorylation experiments. Limitations: Rate depends on substrate and regulatory state; this is a shared BCAA step. Evidence access: Primary abstract Protein phosphatase 2Cm is a critical regulator of branched-chain amino acid catabolism in mice and cultured cells. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19411760/ · DOI 10.1172/JCI38151
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The preprint reported that excluding BCKDH machinery from nuclei suppressed histone propionylation and associated gene-expression responses in PDA models.

    Mouse dihydrolipoyl branched-chain transacylase / Dbt → Nuclear isoleucine catabolism in mouse PDA cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary preprint full text; not peer reviewed
    experimental_model
    Engineered mouse KPC PDA cells; nuclear-exclusion/localization experiments.
    limitations
    Preprint and compartment-engineering result; not established as a general nuclear pathway in healthy human tissue.
    nutrient_topic
    L-Isoleucine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Isoleucine
    plain_language
    The location of an enzyme complex influenced which cellular process used its products.
    primary_references
    A nuclear branched-chain amino acid catabolism pathway controls histone propionylation in pancreatic cancer. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40568091/ · DOI 10.1101/2025.04.23.650241
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Isoleucine: transport, translation, catabolism and cross-nutrient mechanisms (2026-09-19) · lines 490–496

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Engineered mouse KPC PDA cells; nuclear-exclusion/localization experiments. · source_derived_draft · unverified_draft

    ## isoleucine-pancreatic-preprint-nuclear The location of an enzyme complex influenced which cellular process used its products. The preprint reported that excluding BCKDH machinery from nuclei suppressed histone propionylation and associated gene-expression responses in PDA models. Model: Engineered mouse KPC PDA cells; nuclear-exclusion/localization experiments. Limitations: Preprint and compartment-engineering result; not established as a general nuclear pathway in healthy human tissue. Evidence access: Primary preprint full text; not peer reviewed A nuclear branched-chain amino acid catabolism pathway controls histone propionylation in pancreatic cancer. · 2025 · https://pubmed.ncbi.nlm.nih.gov/40568091/ · DOI 10.1101/2025.04.23.650241
    Complete structured claim and evidence

  2. Ppm1k loss abolished substrate-induced E1-alpha dephosphorylation and impaired BCAA catabolism in mice.

    Mouse BCKDH phosphatase PP2Cm / Ppm1k → Substrate-induced BCKDH activation in mice source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Ppm1k-deficient mice and cultured cells.
    limitations
    Mouse MSUD-like phenotype is not a diagnosis of dietary BCAA excess.
    nutrient_topic
    L-Isoleucine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Isoleucine
    plain_language
    Failure to release the brake can produce accumulation rather than shortage.
    primary_references
    Protein phosphatase 2Cm is a critical regulator of branched-chain amino acid catabolism in mice and cultured cells. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19411760/ · DOI 10.1172/JCI38151
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Isoleucine: transport, translation, catabolism and cross-nutrient mechanisms (2026-09-19) · lines 282–288

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Ppm1k-deficient mice and cultured cells. · source_derived_draft · unverified_draft

    ## isoleucine-ppm1k-loss Failure to release the brake can produce accumulation rather than shortage. Ppm1k loss abolished substrate-induced E1-alpha dephosphorylation and impaired BCAA catabolism in mice. Model: Ppm1k-deficient mice and cultured cells. Limitations: Mouse MSUD-like phenotype is not a diagnosis of dietary BCAA excess. Evidence access: Primary abstract Protein phosphatase 2Cm is a critical regulator of branched-chain amino acid catabolism in mice and cultured cells. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19411760/ · DOI 10.1172/JCI38151
    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