Component

Human lipoyl-GCSH

Human lipoyl-GCSH. Species, exposure and limitations are retained in each linked 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 acts on it

  1. Reconstituted LIPT1 transfers the lipoyl group from GCSH to dehydrogenase E2 lipoyl domains.

    Human lipoyl amidotransferase / LIPT1 → Human lipoyl-GCSH source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ala-research/29987032.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3fc07be493a0d6e22ea55c9509cb2d727180f5921d588a52d2d9300a25aa49a2", "start_char": 0, "end_char": 989, "text_sha256": "3fc07be493a0d6e22ea55c9509cb2d727180f5921d588a52d2d9300a25aa49a2"}
    experimental_model
    Purified enzymes and bacterial pathway reconstruction
    exposure
    Recombinant proteins and radiolabeled substrates
    limitations
    Human and mouse constructs must not be conflated. Recombinant reconstruction establishes chemistry, not supplementation efficacy.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human proteins; mouse Lipt2 in purified transfer assays; E. coli host
    plain_language
    GCSH carries the cofactor before LIPT1 passes it to energy-processing enzymes.
    primary_references
    [ala-p29987032] Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes. (2018). https://pubmed.ncbi.nlm.nih.gov/29987032/ DOI: 10.1073/pnas.1805862115
    tissue_or_cell_type
    Lipoyl assembly pathway

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 208–219

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified enzymes and bacterial pathway reconstruction · source_derived_draft · unverified_draft

    ### ala-lipt1-gcsh-transfer Reconstituted LIPT1 transfers the lipoyl group from GCSH to dehydrogenase E2 lipoyl domains. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: GCSH carries the cofactor before LIPT1 passes it to energy-processing enzymes. organism: Human proteins; mouse Lipt2 in purified transfer assays; E. coli host tissue_or_cell_type: Lipoyl assembly pathway experimental_model: Purified enzymes and bacterial pathway reconstruction limitations: Human and mouse constructs must not be conflated. Recombinant reconstruction establishes chemistry, not supplementation efficacy. exposure: Recombinant proteins and radiolabeled substrates evidence_span: {"source_cache": "artifacts/ala-research/29987032.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3fc07be493a0d6e22ea55c9509cb2d727180f5921d588a52d2d9300a25aa49a2", "start_char": 0, "end_char": 989, "text_sha256": "3fc07be493a0d6e22ea55c9509cb2d727180f5921d588a52d2d9300a25aa49a2"} [ala-p29987032] Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes. (2018). https://pubmed.ncbi.nlm.nih.gov/29987032/ DOI: 10.1073/pnas.1805862115
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. LIAS installs sulfur at carbon 6 and carbon 8 of an octanoyl-lysyl residue on GCSH.

    Lipoic acid synthetase / LIAS → LIAS sulfur insertion into octanoyl-GCSH source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ala-research/40640146.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "292f83149906d0c3be473ce3b23be4ee13d1c662b2665993808021098523cd23", "start_char": 0, "end_char": 953, "text_sha256": "292f83149906d0c3be473ce3b23be4ee13d1c662b2665993808021098523cd23"}
    experimental_model
    X-ray structures of catalytic stages with human lipoyl synthase
    exposure
    Structural trapping of sulfur-insertion intermediates
    limitations
    Structural snapshots establish reaction intermediates, not clinical nutrient requirements.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human recombinant proteins
    plain_language
    LIAS turns the attached precursor into a sulfur-bearing working cofactor.
    primary_references
    [ala-p40640146] Structural basis for catalysis by human lipoyl synthase. (2025). https://pubmed.ncbi.nlm.nih.gov/40640146/ DOI: 10.1038/s41467-025-61393-x
    tissue_or_cell_type
    LIAS and H-protein substrate

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 260–271

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray structures of catalytic stages with human lipoyl synthase · source_derived_draft · unverified_draft

    ### ala-lias-sulfur-installation LIAS installs sulfur at carbon 6 and carbon 8 of an octanoyl-lysyl residue on GCSH. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: LIAS turns the attached precursor into a sulfur-bearing working cofactor. organism: Human recombinant proteins tissue_or_cell_type: LIAS and H-protein substrate experimental_model: X-ray structures of catalytic stages with human lipoyl synthase limitations: Structural snapshots establish reaction intermediates, not clinical nutrient requirements. exposure: Structural trapping of sulfur-insertion intermediates evidence_span: {"source_cache": "artifacts/ala-research/40640146.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "292f83149906d0c3be473ce3b23be4ee13d1c662b2665993808021098523cd23", "start_char": 0, "end_char": 953, "text_sha256": "292f83149906d0c3be473ce3b23be4ee13d1c662b2665993808021098523cd23"} [ala-p40640146] Structural basis for catalysis by human lipoyl synthase. (2025). https://pubmed.ncbi.nlm.nih.gov/40640146/ DOI: 10.1038/s41467-025-61393-x
    Complete structured claim and evidence

  2. The lipoyl cofactor is attached through an amide linkage to a conserved carrier-protein lysine side chain.

    Protein-bound oxidized lipoyl-lysine → Human glycine-cleavage H-protein / GCSH source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ala-research/40640146.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "292f83149906d0c3be473ce3b23be4ee13d1c662b2665993808021098523cd23", "start_char": 0, "end_char": 953, "text_sha256": "292f83149906d0c3be473ce3b23be4ee13d1c662b2665993808021098523cd23"}
    experimental_model
    X-ray structures of catalytic stages with human lipoyl synthase
    exposure
    Structural trapping of sulfur-insertion intermediates
    limitations
    Structural snapshots establish reaction intermediates, not clinical nutrient requirements.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human recombinant proteins
    plain_language
    The enzyme uses a tethered cofactor; free supplement molecules are a different pool.
    primary_references
    [ala-p40640146] Structural basis for catalysis by human lipoyl synthase. (2025). https://pubmed.ncbi.nlm.nih.gov/40640146/ DOI: 10.1038/s41467-025-61393-x
    tissue_or_cell_type
    LIAS and H-protein substrate

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 247–258

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray structures of catalytic stages with human lipoyl synthase · source_derived_draft · unverified_draft

    ### ala-lipoyl-lysine-anchor The lipoyl cofactor is attached through an amide linkage to a conserved carrier-protein lysine side chain. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme uses a tethered cofactor; free supplement molecules are a different pool. organism: Human recombinant proteins tissue_or_cell_type: LIAS and H-protein substrate experimental_model: X-ray structures of catalytic stages with human lipoyl synthase limitations: Structural snapshots establish reaction intermediates, not clinical nutrient requirements. exposure: Structural trapping of sulfur-insertion intermediates evidence_span: {"source_cache": "artifacts/ala-research/40640146.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "292f83149906d0c3be473ce3b23be4ee13d1c662b2665993808021098523cd23", "start_char": 0, "end_char": 953, "text_sha256": "292f83149906d0c3be473ce3b23be4ee13d1c662b2665993808021098523cd23"} [ala-p40640146] Structural basis for catalysis by human lipoyl synthase. (2025). https://pubmed.ncbi.nlm.nih.gov/40640146/ DOI: 10.1038/s41467-025-61393-x
    Complete structured claim and evidence

  3. Despite LIPT1 deficiency, H-protein lipoylation, glycine-cleavage activity and glycine concentrations were normal in this case.

    Human lipoyl amidotransferase / LIPT1 → Glycine cleavage flux source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/ala-research/24256811.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "57599dd35c58b21d16f2a5955ea667ec8211ab129ee7d0b639b31f18f0976eb2", "start_char": 0, "end_char": 1749, "text_sha256": "57599dd35c58b21d16f2a5955ea667ec8211ab129ee7d0b639b31f18f0976eb2"}
    experimental_model
    Affected patient, biochemical testing and complementation
    exposure
    Compound-heterozygous LIPT1 variants
    limitations
    Single rare inherited case; enzyme deficits are not interchangeable with nutritional deficiency.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human
    plain_language
    The glycine pathway can keep working when a later transfer step fails.
    primary_references
    [ala-p24256811] Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes. (2014). https://pubmed.ncbi.nlm.nih.gov/24256811/ DOI: 10.1093/hmg/ddt585
    tissue_or_cell_type
    Patient-derived cells
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 468–479

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Affected patient, biochemical testing and complementation · source_derived_draft · unverified_draft

    ### ala-lipt1-glycine-spared Despite LIPT1 deficiency, H-protein lipoylation, glycine-cleavage activity and glycine concentrations were normal in this case. Condition category: machinery_impairment nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The glycine pathway can keep working when a later transfer step fails. organism: Human tissue_or_cell_type: Patient-derived cells experimental_model: Affected patient, biochemical testing and complementation limitations: Single rare inherited case; enzyme deficits are not interchangeable with nutritional deficiency. exposure: Compound-heterozygous LIPT1 variants evidence_span: {"source_cache": "artifacts/ala-research/24256811.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "57599dd35c58b21d16f2a5955ea667ec8211ab129ee7d0b639b31f18f0976eb2", "start_char": 0, "end_char": 1749, "text_sha256": "57599dd35c58b21d16f2a5955ea667ec8211ab129ee7d0b639b31f18f0976eb2"} [ala-p24256811] Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes. (2014). https://pubmed.ncbi.nlm.nih.gov/24256811/ DOI: 10.1093/hmg/ddt585
    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