Component

Saccharopine

Independent small molecule record; interpretation is limited by each linked claim and its study context.

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 AASS dehydrogenase domain oxidatively cleaves saccharopine, producing alpha-aminoadipate semialdehyde and glutamate with NAD+ reduction.

    Saccharopine → alpha-Aminoadipate semialdehyde source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human AASS cloning, localization and familial hyperlysinemia genetics
    limitations
    Biochemical capacity does not quantify flux in every human tissue.
    organism
    Homo sapiens
    plain_language
    The second AASS activity opens the next lysine breakdown step.
    primary_references
    [sacksteder2000] Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia (2000). https://pmc.ncbi.nlm.nih.gov/articles/PMC1378037/ DOI: 10.1086/302919
    tissue_or_cell_type
    Mitochondrial matrix

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 84–92

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human AASS cloning, localization and familial hyperlysinemia genetics · source_derived_draft · unverified_draft

    ### aass-saccharopine-dehydrogenase The AASS dehydrogenase domain oxidatively cleaves saccharopine, producing alpha-aminoadipate semialdehyde and glutamate with NAD+ reduction. Plain language: The second AASS activity opens the next lysine breakdown step. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Mitochondrial matrix experimental_model: Human AASS cloning, localization and familial hyperlysinemia genetics limitations: Biochemical capacity does not quantify flux in every human tissue. [sacksteder2000] Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia (2000). https://pmc.ncbi.nlm.nih.gov/articles/PMC1378037/ DOI: 10.1086/302919
    Complete structured claim and evidence

  2. Excess saccharopine disrupts mitochondrial morphology and function in AASS-domain mutant models.

    Saccharopine → Mitochondrial homeostasis source_derived_draftungraded
    Experimental context and source evidence
    affected_machinery
    AASS
    availability_state
    machinery_impairment Imported condition classification; unverified.
    deficiency_not_equivalent
    Dietary lysine deficiency
    experimental_model
    Genetic and suppression experiments in worms and mice
    limitations
    Evidence is model-specific, not a toxicity threshold for normal human lysine intake.
    organism
    Caenorhabditis elegans and Mus musculus
    plain_language
    Accumulated saccharopine can harm mitochondria.
    primary_references
    [zhou2019] The lysine catabolite saccharopine impairs development by disrupting mitochondrial homeostasis (2019). https://pmc.ncbi.nlm.nih.gov/articles/PMC6363459/ DOI: 10.1083/jcb.201807204
    tissue_or_cell_type
    Worm hypodermis and mouse liver
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 242–252

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Genetic and suppression experiments in worms and mice · source_derived_draft · unverified_draft

    ### saccharopine-mitochondrial-toxicity Excess saccharopine disrupts mitochondrial morphology and function in AASS-domain mutant models. Plain language: Accumulated saccharopine can harm mitochondria. Condition category: machinery_impairment organism: Caenorhabditis elegans and Mus musculus tissue_or_cell_type: Worm hypodermis and mouse liver experimental_model: Genetic and suppression experiments in worms and mice limitations: Evidence is model-specific, not a toxicity threshold for normal human lysine intake. affected_machinery: AASS deficiency_not_equivalent: Dietary lysine deficiency [zhou2019] The lysine catabolite saccharopine impairs development by disrupting mitochondrial homeostasis (2019). https://pmc.ncbi.nlm.nih.gov/articles/PMC6363459/ DOI: 10.1083/jcb.201807204
    Complete structured claim and evidence

What acts on it

  1. The AASS reductase domain condenses lysine with 2-oxoglutarate using NADPH to form saccharopine.

    L-Lysine → Saccharopine source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Recombinant human AASS and isolated reductase domain
    limitations
    Reaction reversibility in vitro does not imply appreciable human lysine biosynthesis.
    organism
    Homo sapiens
    plain_language
    AASS starts the main lysine breakdown route.
    primary_references
    [leandro2022] Characterization and structure of the human lysine-2-oxoglutarate reductase domain, a novel therapeutic target for treatment of glutaric aciduria type 1 (2022). https://pmc.ncbi.nlm.nih.gov/articles/PMC9490328/ DOI: 10.1098/rsob.220179
    tissue_or_cell_type
    Mitochondrial matrix

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 74–82

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human AASS and isolated reductase domain · source_derived_draft · unverified_draft

    ### aass-reductase The AASS reductase domain condenses lysine with 2-oxoglutarate using NADPH to form saccharopine. Plain language: AASS starts the main lysine breakdown route. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Mitochondrial matrix experimental_model: Recombinant human AASS and isolated reductase domain limitations: Reaction reversibility in vitro does not imply appreciable human lysine biosynthesis. [leandro2022] Characterization and structure of the human lysine-2-oxoglutarate reductase domain, a novel therapeutic target for treatment of glutaric aciduria type 1 (2022). https://pmc.ncbi.nlm.nih.gov/articles/PMC9490328/ DOI: 10.1098/rsob.220179
    Complete structured claim and evidence

  2. Selective AASS saccharopine-dehydrogenase impairment while reductase activity persists causes saccharopine accumulation.

    AASS → Saccharopine source_derived_draftungraded
    Experimental context and source evidence
    affected_machinery
    AASS saccharopine dehydrogenase
    availability_state
    machinery_impairment Imported condition classification; unverified.
    deficiency_not_equivalent
    Dietary lysine deficiency or complete AASS knockout
    experimental_model
    AASS-domain mutant worms and engineered mice
    limitations
    Selective downstream-domain failure differs from complete AASS loss.
    organism
    Caenorhabditis elegans and Mus musculus
    plain_language
    Saccharopine builds up when its production continues but its removal fails.
    primary_references
    [zhou2019] The lysine catabolite saccharopine impairs development by disrupting mitochondrial homeostasis (2019). https://pmc.ncbi.nlm.nih.gov/articles/PMC6363459/ DOI: 10.1083/jcb.201807204
    tissue_or_cell_type
    Worm hypodermis and mouse liver
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 230–240

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · AASS-domain mutant worms and engineered mice · source_derived_draft · unverified_draft

    ### aass-sdh-saccharopine-accumulation Selective AASS saccharopine-dehydrogenase impairment while reductase activity persists causes saccharopine accumulation. Plain language: Saccharopine builds up when its production continues but its removal fails. Condition category: machinery_impairment organism: Caenorhabditis elegans and Mus musculus tissue_or_cell_type: Worm hypodermis and mouse liver experimental_model: AASS-domain mutant worms and engineered mice limitations: Selective downstream-domain failure differs from complete AASS loss. affected_machinery: AASS saccharopine dehydrogenase deficiency_not_equivalent: Dietary lysine deficiency or complete AASS knockout [zhou2019] The lysine catabolite saccharopine impairs development by disrupting mitochondrial homeostasis (2019). https://pmc.ncbi.nlm.nih.gov/articles/PMC6363459/ DOI: 10.1083/jcb.201807204
    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