Component
L-alpha-Aminoadipate
Independent small molecule 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.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What it acts on
PLP-dependent AADAT transfers the amino group from aminoadipate to 2-oxoglutarate, generating 2-oxoadipate and glutamate.
Experimental context and source evidence
- experimental_model
- Human cDNA and recombinant bacterial expression; Purified recombinant human enzyme; kinetics and crystallography
- limitations
- AADAT also accepts other substrates; substrate breadth is not lysine-specific regulation.
- organism
- Homo sapiens
- plain_language
- AADAT removes the remaining amino group.
- primary_references
- [goh2002] Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT). (2002). https://pubmed.ncbi.nlm.nih.gov/12126930/ DOI: 10.1016/S1096-7192(02)00037-9 [han2008] Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II (2008). https://pmc.ncbi.nlm.nih.gov/articles/PMC2559858/ DOI: 10.1042/BSR20080085
- tissue_or_cell_type
- Mitochondrial lysine catabolism; human expression highest in liver in cloning study
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 114–123
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human cDNA and recombinant bacterial expression; Purified recombinant human enzyme; kinetics and crystallography · source_derived_draft · unverified_draft
### aadat-transamination PLP-dependent AADAT transfers the amino group from aminoadipate to 2-oxoglutarate, generating 2-oxoadipate and glutamate. Plain language: AADAT removes the remaining amino group. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Mitochondrial lysine catabolism; human expression highest in liver in cloning study experimental_model: Human cDNA and recombinant bacterial expression; Purified recombinant human enzyme; kinetics and crystallography limitations: AADAT also accepts other substrates; substrate breadth is not lysine-specific regulation. [goh2002] Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT). (2002). https://pubmed.ncbi.nlm.nih.gov/12126930/ DOI: 10.1016/S1096-7192(02)00037-9 [han2008] Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II (2008). https://pmc.ncbi.nlm.nih.gov/articles/PMC2559858/ DOI: 10.1042/BSR20080085
Complete structured claim and evidence
What acts on it
ALDH7A1 oxidizes alpha-aminoadipate semialdehyde to alpha-aminoadipate using NAD+.
Experimental context and source evidence
- experimental_model
- Human ALDH7A1 biochemical and genetic study
- limitations
- Compartmental isoform distribution is not resolved by this claim.
- organism
- Homo sapiens
- plain_language
- Antiquitin clears the aldehyde intermediate.
- primary_references
- [luo2015] Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1 (2015). https://pubmed.ncbi.nlm.nih.gov/26260980/ DOI: 10.1021/acs.biochem.5b00754
- tissue_or_cell_type
- Lysine-catabolizing tissues
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 104–112
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human ALDH7A1 biochemical and genetic study · source_derived_draft · unverified_draft
### aldh7a1-oxidation ALDH7A1 oxidizes alpha-aminoadipate semialdehyde to alpha-aminoadipate using NAD+. Plain language: Antiquitin clears the aldehyde intermediate. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Lysine-catabolizing tissues experimental_model: Human ALDH7A1 biochemical and genetic study limitations: Compartmental isoform distribution is not resolved by this claim. [luo2015] Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1 (2015). https://pubmed.ncbi.nlm.nih.gov/26260980/ DOI: 10.1021/acs.biochem.5b00754
Complete structured claim and evidence
Where it participates (unsigned role)
Patient DHTKD1-deficient fibroblasts accumulated deuterium-labeled 2-oxoadipate from labeled lysine; wild-type DHTKD1 expression normalized the biochemical defect.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- cross_nutrient
- A B1-dependent enzyme connects lysine degradation to glutaryl-CoA metabolism.
- evidence
- [{"paper_key": "danhauser-2012-dhtkd1", "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
- Patient fibroblasts, isotope tracing and lentiviral complementation.
- limitations
- Two individuals; neurological phenotypes vary and biochemical rescue does not prove a clinical treatment.
- 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
- Replacing the faulty enzyme restored the tested metabolic step. The experiment identifies a machinery defect rather than a lack of dietary B1.
- primary_references
- [danhauser-2012-dhtkd1] DHTKD1 mutations cause 2-aminoadipic and 2-oxoadipic aciduria (2012). https://pubmed.ncbi.nlm.nih.gov/23141293/ DOI: 10.1016/j.ajhg.2012.10.006
- tissue_or_cell_type
- Cultured fibroblasts
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Thiamine: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 909–921
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Patient fibroblasts, isotope tracing and lentiviral complementation. · source_derived_draft · unverified_draft
### b1-dhtkd1-patient-lysine-turnover Patient DHTKD1-deficient fibroblasts accumulated deuterium-labeled 2-oxoadipate from labeled lysine; wild-type DHTKD1 expression normalized the biochemical defect. Condition category: machinery_impairment nutrient_topic: Thiamine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Replacing the faulty enzyme restored the tested metabolic step. The experiment identifies a machinery defect rather than a lack of dietary B1. organism: Homo sapiens tissue_or_cell_type: Cultured fibroblasts experimental_model: Patient fibroblasts, isotope tracing and lentiviral complementation. limitations: Two individuals; neurological phenotypes vary and biochemical rescue does not prove a clinical treatment. evidence: [{"paper_key": "danhauser-2012-dhtkd1", "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: A B1-dependent enzyme connects lysine degradation to glutaryl-CoA metabolism. nutrient: Thiamine (vitamin B1) [danhauser-2012-dhtkd1] DHTKD1 mutations cause 2-aminoadipic and 2-oxoadipic aciduria (2012). https://pubmed.ncbi.nlm.nih.gov/23141293/ DOI: 10.1016/j.ajhg.2012.10.006
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.