Component
L-Pipecolate
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
Human peroxisomal PIPOX oxidizes L-pipecolate to P6C.
Experimental context and source evidence
- experimental_model
- Human cDNA cloning and expressed enzyme
- limitations
- Enzyme capability does not establish that this route predominates in human brain; see conflict.
- organism
- Homo sapiens
- plain_language
- Pipecolate can join the common lysine breakdown route.
- primary_references
- [ijlst2000] Molecular cloning and expression of human L-pipecolate oxidase (2000). https://pubmed.ncbi.nlm.nih.gov/10772957/ DOI: 10.1006/bbrc.2000.2575
- tissue_or_cell_type
- Peroxisomes
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 146–154
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human cDNA cloning and expressed enzyme · source_derived_draft · unverified_draft
### pipox-pipecolate-oxidation Human peroxisomal PIPOX oxidizes L-pipecolate to P6C. Plain language: Pipecolate can join the common lysine breakdown route. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Peroxisomes experimental_model: Human cDNA cloning and expressed enzyme limitations: Enzyme capability does not establish that this route predominates in human brain; see conflict. [ijlst2000] Molecular cloning and expression of human L-pipecolate oxidase (2000). https://pubmed.ncbi.nlm.nih.gov/10772957/ DOI: 10.1006/bbrc.2000.2575
Complete structured claim and evidence
What acts on it
CRYM ketimine reductase reduces P2C to L-pipecolate using reduced nicotinamide cofactors.
Experimental context and source evidence
- experimental_model
- Recombinant human CRYM and mammalian enzyme substrate assays
- limitations
- Catalytic capacity does not determine the route's quantitative contribution to human brain lysine clearance.
- organism
- Homo sapiens enzyme; ovine enzyme used for initial purification
- plain_language
- A ring-shaped intermediate can be reduced to pipecolate.
- primary_references
- [hallen2011] Mammalian forebrain ketimine reductase identified as mu-crystallin; potential regulation by thyroid hormones. (2011). https://pubmed.ncbi.nlm.nih.gov/21332720/ DOI: 10.1111/j.1471-4159.2011.07220.x [hallen2015] Insights into Enzyme Catalysis and Thyroid Hormone Regulation of Cerebral Ketimine Reductase/mu-Crystallin Under Physiological Conditions. (2015). https://pubmed.ncbi.nlm.nih.gov/25931162/ DOI: 10.1007/s11064-015-1590-5
- tissue_or_cell_type
- Cytosolic enzyme; forebrain biochemical context
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 336–345
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human CRYM and mammalian enzyme substrate assays · source_derived_draft · unverified_draft
### crym-p2c-reduction CRYM ketimine reductase reduces P2C to L-pipecolate using reduced nicotinamide cofactors. Plain language: A ring-shaped intermediate can be reduced to pipecolate. Condition category: normal organism: Homo sapiens enzyme; ovine enzyme used for initial purification tissue_or_cell_type: Cytosolic enzyme; forebrain biochemical context experimental_model: Recombinant human CRYM and mammalian enzyme substrate assays limitations: Catalytic capacity does not determine the route's quantitative contribution to human brain lysine clearance. [hallen2011] Mammalian forebrain ketimine reductase identified as mu-crystallin; potential regulation by thyroid hormones. (2011). https://pubmed.ncbi.nlm.nih.gov/21332720/ DOI: 10.1111/j.1471-4159.2011.07220.x [hallen2015] Insights into Enzyme Catalysis and Thyroid Hormone Regulation of Cerebral Ketimine Reductase/mu-Crystallin Under Physiological Conditions. (2015). https://pubmed.ncbi.nlm.nih.gov/25931162/ DOI: 10.1007/s11064-015-1590-5
Complete structured claim and evidence
Where it participates (unsigned role)
Elevated AASA was observed in an 18-patient PDE cohort with ALDH7A1 investigation, including during pyridoxine treatment.
Experimental context and source evidence
- affected_machinery
- ALDH7A1 under investigation
- availability_state
- biomarker_context Imported condition classification; unverified.
- deficiency_not_equivalent
- Dietary lysine deficiency
- experimental_model
- Human clinical cohort; plasma and urine assays
- limitations
- A biomarker is not itself a diagnosis or proof of dietary lysine deficiency.
- organism
- Homo sapiens
- plain_language
- AASA measurement can reveal disturbed lysine breakdown.
- primary_references
- [plecko2007] Biochemical and molecular characterization of 18 patients with pyridoxine-dependent epilepsy and mutations of the antiquitin (ALDH7A1) gene (2007). https://pubmed.ncbi.nlm.nih.gov/17068770/ DOI: 10.1002/humu.20433
- tissue_or_cell_type
- Plasma and urine
- trigger_kind
- biomarker_context Imported condition classification; unverified.
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 324–334
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human clinical cohort; plasma and urine assays · source_derived_draft · unverified_draft
### aasa-pde-biomarker Elevated AASA was observed in an 18-patient PDE cohort with ALDH7A1 investigation, including during pyridoxine treatment. Plain language: AASA measurement can reveal disturbed lysine breakdown. Condition category: biomarker_context organism: Homo sapiens tissue_or_cell_type: Plasma and urine experimental_model: Human clinical cohort; plasma and urine assays limitations: A biomarker is not itself a diagnosis or proof of dietary lysine deficiency. affected_machinery: ALDH7A1 under investigation deficiency_not_equivalent: Dietary lysine deficiency [plecko2007] Biochemical and molecular characterization of 18 patients with pyridoxine-dependent epilepsy and mutations of the antiquitin (ALDH7A1) gene (2007). https://pubmed.ncbi.nlm.nih.gov/17068770/ DOI: 10.1002/humu.20433
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.