Component

Human 2-oxoglutarate dehydrogenase E1

OGDH E1 component of the human mitochondrial 2-oxoglutarate dehydrogenase complex.

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. The human OGDH cryo-EM model 7WGR contains Mg and ThDP as well as a separate Ca-binding site.

    Human 2-oxoglutarate dehydrogenase E1 → Mg2+ source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Magnesium and thiamine-derived ThDP intersect at mitochondrial carbon metabolism; purified-enzyme responses do not measure whole-body energy supply.
    experimental_model
    Human OGDH cryo-EM structure; deposited coordinate model 7WGR.
    limitations
    Structure does not establish a clinical Mg threshold or metal replacement equivalence.
    nutrient_topic
    Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
    organism
    Homo sapiens
    plain_language
    The human alpha-ketoglutarate-processing enzyme has distinct cofactor and calcium-regulatory architecture.
    primary_references
    [zhong-2022-ogdh] Structural basis for the activity and regulation of human α-ketoglutarate dehydrogenase revealed by Cryo-EM (2022). https://pubmed.ncbi.nlm.nih.gov/35272141/ DOI: 10.1016/j.bbrc.2022.02.093
    structure_url
    https://pdbj.org/mine/summary/7wgr
    tissue_or_cell_type
    Recombinant mitochondrial OGDH

    Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 662–673

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human OGDH cryo-EM structure; deposited coordinate model 7WGR. · source_derived_draft · unverified_draft

    ### mg-ogdh-human-cofactor-structure The human OGDH cryo-EM model 7WGR contains Mg and ThDP as well as a separate Ca-binding site. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: The human alpha-ketoglutarate-processing enzyme has distinct cofactor and calcium-regulatory architecture. organism: Homo sapiens tissue_or_cell_type: Recombinant mitochondrial OGDH experimental_model: Human OGDH cryo-EM structure; deposited coordinate model 7WGR. limitations: Structure does not establish a clinical Mg threshold or metal replacement equivalence. cross_nutrient: Magnesium and thiamine-derived ThDP intersect at mitochondrial carbon metabolism; purified-enzyme responses do not measure whole-body energy supply. structure_url: https://pdbj.org/mine/summary/7wgr [zhong-2022-ogdh] Structural basis for the activity and regulation of human α-ketoglutarate dehydrogenase revealed by Cryo-EM (2022). https://pubmed.ncbi.nlm.nih.gov/35272141/ DOI: 10.1016/j.bbrc.2022.02.093
    Complete structured claim and evidence

  2. Human recombinant OGDH reacted with 2-oxoglutarate to produce spectroscopic signals supporting a ThDP-bound post-decarboxylation enamine.

    Human 2-oxoglutarate dehydrogenase E1 → OGDH-bound carboxypropylidene-ThDP enamine source_derived_draftungraded
    Experimental context and source evidence
    evidence
    [{"paper_key": "nemeria-2014-ogdh", "source_bundle": "artifacts/thiamine_metabolism_sources.json", "passage_ids": ["p-48"], "locator": "CD titration of E1o-h", "preservation": "Exact text retained in the source bundle; full source document retained when openly retrievable."}]
    experimental_model
    Human OGDH circular dichroism and related spectroscopy.
    limitations
    Enamine assignment integrates spectroscopy and comparative experiments; fine kinetic rates were separately measured in E. coli.
    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
    At this TCA-cycle step, B1 holds the carbon fragment left after carbon dioxide loss. Bacterial stopped-flow numbers in the same paper are not human kinetic constants.
    primary_references
    [nemeria-2014-ogdh] Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate (2014). https://pubmed.ncbi.nlm.nih.gov/25210035/ DOI: 10.1074/jbc.m114.591073
    tissue_or_cell_type
    Purified E1

    Thiamine: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 842–853

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human OGDH circular dichroism and related spectroscopy. · source_derived_draft · unverified_draft

    ### b1-ogdh-thdp-enamine-chemistry Human recombinant OGDH reacted with 2-oxoglutarate to produce spectroscopic signals supporting a ThDP-bound post-decarboxylation enamine. Condition category: normal nutrient_topic: Thiamine research collection; topical membership is not evidence of a direct dietary effect. plain_language: At this TCA-cycle step, B1 holds the carbon fragment left after carbon dioxide loss. Bacterial stopped-flow numbers in the same paper are not human kinetic constants. organism: Homo sapiens tissue_or_cell_type: Purified E1 experimental_model: Human OGDH circular dichroism and related spectroscopy. limitations: Enamine assignment integrates spectroscopy and comparative experiments; fine kinetic rates were separately measured in E. coli. evidence: [{"paper_key": "nemeria-2014-ogdh", "source_bundle": "artifacts/thiamine_metabolism_sources.json", "passage_ids": ["p-48"], "locator": "CD titration of E1o-h", "preservation": "Exact text retained in the source bundle; full source document retained when openly retrievable."}] nutrient: Thiamine (vitamin B1) [nemeria-2014-ogdh] Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate (2014). https://pubmed.ncbi.nlm.nih.gov/25210035/ DOI: 10.1074/jbc.m114.591073
    Complete structured claim and evidence

What acts on it

  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

Where it participates (unsigned role)

  1. Human OGDH, lipoylated DLST and DLD assembled into an active complex coupling 2-oxoglutarate oxidation to NADH production in the CoA-containing assay.

    2-Oxoglutarate dehydrogenase complex → Succinyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    B1, B5-derived CoA, B2-derived FAD and niacin-related NAD act at different steps of one complex.
    evidence
    [{"paper_key": "nemeria-2014-ogdh", "source_bundle": "artifacts/thiamine_metabolism_sources.json", "passage_ids": ["p-28"], "locator": "The reaction medium contained the following in 1.0 ml", "preservation": "Exact text retained in the source bundle; full source document retained when openly retrievable."}]
    experimental_model
    Reconstituted human multienzyme assay.
    limitations
    NADH assay measures overall complex turnover, not every intermediate independently.
    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
    B1-dependent E1 feeds a lipoyl/CoA transfer pathway, and E3 transfers the resulting reducing equivalents to NAD.
    primary_references
    [nemeria-2014-ogdh] Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate (2014). https://pubmed.ncbi.nlm.nih.gov/25210035/ DOI: 10.1074/jbc.m114.591073
    tissue_or_cell_type
    Purified enzyme complex

    Thiamine: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 855–867

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

    ### b1-ogdh-complex-couples-succinyl-nadh Human OGDH, lipoylated DLST and DLD assembled into an active complex coupling 2-oxoglutarate oxidation to NADH production in the CoA-containing assay. Condition category: normal nutrient_topic: Thiamine research collection; topical membership is not evidence of a direct dietary effect. plain_language: B1-dependent E1 feeds a lipoyl/CoA transfer pathway, and E3 transfers the resulting reducing equivalents to NAD. organism: Homo sapiens tissue_or_cell_type: Purified enzyme complex experimental_model: Reconstituted human multienzyme assay. limitations: NADH assay measures overall complex turnover, not every intermediate independently. evidence: [{"paper_key": "nemeria-2014-ogdh", "source_bundle": "artifacts/thiamine_metabolism_sources.json", "passage_ids": ["p-28"], "locator": "The reaction medium contained the following in 1.0 ml", "preservation": "Exact text retained in the source bundle; full source document retained when openly retrievable."}] cross_nutrient: B1, B5-derived CoA, B2-derived FAD and niacin-related NAD act at different steps of one complex. nutrient: Thiamine (vitamin B1) [nemeria-2014-ogdh] Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate (2014). https://pubmed.ncbi.nlm.nih.gov/25210035/ DOI: 10.1074/jbc.m114.591073
    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