Component

2-Oxoadipate dehydrogenase complex

Independent protein complex record; interpretation is limited by each linked claim and its study context.

3 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. Human DHTKD1 supported 2-oxoadipate dehydrogenase activity when combined with the DLST and DLD components also used by OGDH.

    DHTKD1 → 2-Oxoadipate dehydrogenase complex source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    B1-dependent lysine catabolism converges on the same lipoyl, CoA and NAD/FAD machinery used in OGDH.
    evidence
    [{"paper_key": "nemeria-2018-oadh", "source_bundle": "artifacts/thiamine_metabolism_sources.json", "passage_ids": ["abstract"], "locator": "Primary publication abstract", "preservation": "Exact text retained in the source bundle; full source document retained when openly retrievable."}]
    experimental_model
    Human recombinant component reconstitution.
    limitations
    Reconstituted proteins; sharing does not establish competition for limiting subunits in vivo.
    nutrient
    Thiamine (vitamin B1) · Thiamine (vitamin B1)
    nutrient_topic
    Thiamine research collection; topical membership is not evidence of a direct dietary effect. · Thiamine (vitamin B1)
    organism
    Homo sapiens
    plain_language
    Lysine-related carbon disposal uses a different B1-dependent E1, while sharing the downstream E2 and E3 proteins with a TCA-cycle enzyme.
    primary_references
    [nemeria-2018-oadh] The mitochondrial 2-oxoadipate and 2-oxoglutarate dehydrogenase complexes share their E2 and E3 components for their function and both generate reactive oxygen species (2018). https://pubmed.ncbi.nlm.nih.gov/29191460/ DOI: 10.1016/j.freeradbiomed.2017.11.018
    tissue_or_cell_type
    Purified complex

    Thiamine: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 869–881

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human recombinant component reconstitution. · source_derived_draft · unverified_draft

    ### b1-dhtkd1-recruits-shared-dlst-dld Human DHTKD1 supported 2-oxoadipate dehydrogenase activity when combined with the DLST and DLD components also used by OGDH. Condition category: normal nutrient_topic: Thiamine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Lysine-related carbon disposal uses a different B1-dependent E1, while sharing the downstream E2 and E3 proteins with a TCA-cycle enzyme. organism: Homo sapiens tissue_or_cell_type: Purified complex experimental_model: Human recombinant component reconstitution. limitations: Reconstituted proteins; sharing does not establish competition for limiting subunits in vivo. evidence: [{"paper_key": "nemeria-2018-oadh", "source_bundle": "artifacts/thiamine_metabolism_sources.json", "passage_ids": ["abstract"], "locator": "Primary publication abstract", "preservation": "Exact text retained in the source bundle; full source document retained when openly retrievable."}] cross_nutrient: B1-dependent lysine catabolism converges on the same lipoyl, CoA and NAD/FAD machinery used in OGDH. nutrient: Thiamine (vitamin B1) [nemeria-2018-oadh] The mitochondrial 2-oxoadipate and 2-oxoglutarate dehydrogenase complexes share their E2 and E3 components for their function and both generate reactive oxygen species (2018). https://pubmed.ncbi.nlm.nih.gov/29191460/ DOI: 10.1016/j.freeradbiomed.2017.11.018
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Glutaryl-CoA inhibited human OGDH activity in reconstituted experiments, supporting possible regulatory communication from OADH-linked amino-acid degradation to the TCA cycle.

    Glutaryl-CoA → Human 2-oxoglutarate dehydrogenase E1 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Amino-acid catabolism and central carbon metabolism communicate through an acyl-CoA product.
    evidence
    [{"paper_key": "nemeria-2018-crosstalk", "source_bundle": "artifacts/thiamine_metabolism_sources.json", "passage_ids": ["abstract"], "locator": "Primary publication abstract", "preservation": "Exact text retained in the source bundle; full source document retained when openly retrievable."}]
    experimental_model
    Reconstituted human enzyme inhibition assays.
    limitations
    In vitro regulation; physiological free metabolite concentrations and net in vivo effect were not established.
    nutrient
    Thiamine (vitamin B1) · Thiamine (vitamin B1)
    nutrient_topic
    Thiamine research collection; topical membership is not evidence of a direct dietary effect. · Thiamine (vitamin B1)
    organism
    Homo sapiens
    plain_language
    A product of one B1-dependent route can restrain a different B1 enzyme in a test tube. Its importance inside tissues remains unquantified.
    primary_references
    [nemeria-2018-crosstalk] Evidence for functional and regulatory cross-talk between the tricarboxylic acid cycle 2-oxoglutarate dehydrogenase complex and 2-oxoadipate dehydrogenase on the l-lysine, l-hydroxylysine and l-tryptophan degradation pathways from studies in vitro (2018). https://pubmed.ncbi.nlm.nih.gov/29752936/ DOI: 10.1016/j.bbabio.2018.05.001
    tissue_or_cell_type
    Purified complexes

    Thiamine: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 936–948

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Reconstituted human enzyme inhibition assays. · source_derived_draft · unverified_draft

    ### b1-lysine-product-inhibits-ogdh Glutaryl-CoA inhibited human OGDH activity in reconstituted experiments, supporting possible regulatory communication from OADH-linked amino-acid degradation to the TCA cycle. Condition category: normal nutrient_topic: Thiamine research collection; topical membership is not evidence of a direct dietary effect. plain_language: A product of one B1-dependent route can restrain a different B1 enzyme in a test tube. Its importance inside tissues remains unquantified. organism: Homo sapiens tissue_or_cell_type: Purified complexes experimental_model: Reconstituted human enzyme inhibition assays. limitations: In vitro regulation; physiological free metabolite concentrations and net in vivo effect were not established. evidence: [{"paper_key": "nemeria-2018-crosstalk", "source_bundle": "artifacts/thiamine_metabolism_sources.json", "passage_ids": ["abstract"], "locator": "Primary publication abstract", "preservation": "Exact text retained in the source bundle; full source document retained when openly retrievable."}] cross_nutrient: Amino-acid catabolism and central carbon metabolism communicate through an acyl-CoA product. nutrient: Thiamine (vitamin B1) [nemeria-2018-crosstalk] Evidence for functional and regulatory cross-talk between the tricarboxylic acid cycle 2-oxoglutarate dehydrogenase complex and 2-oxoadipate dehydrogenase on the l-lysine, l-hydroxylysine and l-tryptophan degradation pathways from studies in vitro (2018). https://pubmed.ncbi.nlm.nih.gov/29752936/ DOI: 10.1016/j.bbabio.2018.05.001
    Complete structured claim and evidence

  2. DHTKD1 with DLST and DLD supports oxidative decarboxylation of 2-oxoadipate to glutaryl-CoA, with NADH and carbon dioxide formation.

    2-Oxoadipate → Glutaryl-CoA source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Recombinant human DHTKD1 and DLST; structural and biochemical assays; Two human patients; fibroblast isotope tracing and genetic complementation
    limitations
    DHTKD1 is the E1 component, not a stand-alone enzyme performing every complex reaction.
    organism
    Homo sapiens
    plain_language
    A three-enzyme complex converts the carbon skeleton into glutaryl-CoA.
    primary_references
    [bezerra2020] Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism (2020). https://pmc.ncbi.nlm.nih.gov/articles/PMC7340257/ DOI: 10.1107/S205225252000696X [danhauser2012] DHTKD1 mutations cause 2-aminoadipic and 2-oxoadipic aciduria (2012). https://pmc.ncbi.nlm.nih.gov/articles/PMC3516599/ DOI: 10.1016/j.ajhg.2012.10.006
    tissue_or_cell_type
    Mitochondrial matrix

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 125–134

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human DHTKD1 and DLST; structural and biochemical assays; Two human patients; fibroblast isotope tracing and genetic complementation · source_derived_draft · unverified_draft

    ### oxoadipate-dehydrogenase-complex DHTKD1 with DLST and DLD supports oxidative decarboxylation of 2-oxoadipate to glutaryl-CoA, with NADH and carbon dioxide formation. Plain language: A three-enzyme complex converts the carbon skeleton into glutaryl-CoA. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Mitochondrial matrix experimental_model: Recombinant human DHTKD1 and DLST; structural and biochemical assays; Two human patients; fibroblast isotope tracing and genetic complementation limitations: DHTKD1 is the E1 component, not a stand-alone enzyme performing every complex reaction. [bezerra2020] Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism (2020). https://pmc.ncbi.nlm.nih.gov/articles/PMC7340257/ DOI: 10.1107/S205225252000696X [danhauser2012] DHTKD1 mutations cause 2-aminoadipic and 2-oxoadipic aciduria (2012). https://pmc.ncbi.nlm.nih.gov/articles/PMC3516599/ DOI: 10.1016/j.ajhg.2012.10.006
    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