Component

Human mitochondrial branched-chain aminotransferase / BCAT2

Human mitochondrial branched-chain aminotransferase / BCAT2

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 BCAT2 transfers the isoleucine amino group through the PLP/PMP cycle, linking isoleucine/branched ketoacid interconversion to 2-oxoglutarate/glutamate.

    Human mitochondrial branched-chain aminotransferase / BCAT2 → 3-Methyl-2-oxopentanoate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract; reaction-intermediate structural study
    experimental_model
    Human BCAT2 intermediate structures and established reaction chemistry.
    limitations
    Reversible enzyme chemistry; concentration and compartment determine net flux.
    nutrient_topic
    L-Isoleucine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Isoleucine
    plain_language
    The first breakdown step passes nitrogen to another metabolite.
    primary_references
    Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269802/ · DOI 10.1021/bi020221c

    L-Isoleucine: transport, translation, catabolism and cross-nutrient mechanisms (2026-09-19) · lines 162–168

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human BCAT2 intermediate structures and established reaction chemistry. · source_derived_draft · unverified_draft

    ## isoleucine-bcat-reaction The first breakdown step passes nitrogen to another metabolite. Human BCAT2 transfers the isoleucine amino group through the PLP/PMP cycle, linking isoleucine/branched ketoacid interconversion to 2-oxoglutarate/glutamate. Model: Human BCAT2 intermediate structures and established reaction chemistry. Limitations: Reversible enzyme chemistry; concentration and compartment determine net flux. Evidence access: Primary abstract; reaction-intermediate structural study Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12269802/ · DOI 10.1021/bi020221c
    Complete structured claim and evidence

  2. Human BCAT2 transfers the leucine amino group to 2-oxoglutarate, producing alpha-ketoisocaproate and glutamate.

    Human mitochondrial branched-chain aminotransferase / BCAT2 → L-Leucine source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Essential amino-acid nitrogen transfer; net direction depends on substrate/product conditions.
    experimental_model
    Recombinant human BCAT1 and BCAT2; pre-steady-state kinetics and structures
    limitations
    Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds.
    nutrient_topic
    Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
    organism
    Homo sapiens
    plain_language
    B6-dependent transamination starts leucine processing and transfers nitrogen to glutamate.
    primary_references
    [b6-bcat1-2005] Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin (2005). https://pubmed.ncbi.nlm.nih.gov/16141215/ DOI: 10.1074/jbc.M506486200
    tissue_or_cell_type
    Purified recombinant protein; no intact tissue

    Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 729–739

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human BCAT1 and BCAT2; pre-steady-state kinetics and structures · source_derived_draft · unverified_draft

    ### b6-met-bcat2-leucine Human BCAT2 transfers the leucine amino group to 2-oxoglutarate, producing alpha-ketoisocaproate and glutamate. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: B6-dependent transamination starts leucine processing and transfers nitrogen to glutamate. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Recombinant human BCAT1 and BCAT2; pre-steady-state kinetics and structures limitations: Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds. cross_nutrient: Essential amino-acid nitrogen transfer; net direction depends on substrate/product conditions. [b6-bcat1-2005] Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin (2005). https://pubmed.ncbi.nlm.nih.gov/16141215/ DOI: 10.1074/jbc.M506486200
    Complete structured claim and evidence

  3. Human BCAT2 structures capture the isoleucine ketimine and PMP forms of its amino-transfer cycle.

    Human mitochondrial branched-chain aminotransferase / BCAT2 → Pyridoxamine 5-prime-phosphate source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human BCAT2 reaction-intermediate crystallography
    limitations
    Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds.
    nutrient_topic
    Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
    organism
    Homo sapiens
    plain_language
    The cofactor cycles between PLP and PMP as it carries an amino group.
    primary_references
    [b6-bcat2-2002] Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms (2002). https://pubmed.ncbi.nlm.nih.gov/12269802/ DOI: 10.1021/bi020221c
    tissue_or_cell_type
    Purified recombinant protein; no intact tissue

    Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 706–715

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human BCAT2 reaction-intermediate crystallography · source_derived_draft · unverified_draft

    ### b6-met-bcat2-pmp Human BCAT2 structures capture the isoleucine ketimine and PMP forms of its amino-transfer cycle. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cofactor cycles between PLP and PMP as it carries an amino group. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Human BCAT2 reaction-intermediate crystallography limitations: Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds. [b6-bcat2-2002] Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms (2002). https://pubmed.ncbi.nlm.nih.gov/12269802/ DOI: 10.1021/bi020221c
    Complete structured claim and evidence

What acts on it

  1. Human BCAT2 crystal structures show PLP covalently linked to the active-site lysine in active enzyme forms.

    PLP → Human mitochondrial branched-chain aminotransferase / BCAT2 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    B6 participates in essential branched-chain amino-acid metabolism.
    experimental_model
    Purified recombinant human BCAT2 crystallography
    limitations
    Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds.
    nutrient_topic
    Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
    organism
    Homo sapiens
    plain_language
    Mitochondrial branched-chain amino-acid metabolism uses bound active B6.
    primary_references
    [b6-bcat2-2001] The structure of human mitochondrial branched-chain aminotransferase (2001). https://doi.org/10.1107/S0907444901001925 DOI: 10.1107/S0907444901001925
    tissue_or_cell_type
    Purified recombinant protein; no intact tissue

    Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 694–704

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human BCAT2 crystallography · source_derived_draft · unverified_draft

    ### b6-met-bcat2-plp Human BCAT2 crystal structures show PLP covalently linked to the active-site lysine in active enzyme forms. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Mitochondrial branched-chain amino-acid metabolism uses bound active B6. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Purified recombinant human BCAT2 crystallography limitations: Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds. cross_nutrient: B6 participates in essential branched-chain amino-acid metabolism. [b6-bcat2-2001] The structure of human mitochondrial branched-chain aminotransferase (2001). https://doi.org/10.1107/S0907444901001925 DOI: 10.1107/S0907444901001925
    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