Component
Pig GABA aminotransferase / ABAT
Pig GABA aminotransferase / ABAT
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
Native and inhibitor-bound pig liver GABA-AT structures resolved a [2Fe-2S] cluster near the PLP sites.
Experimental context and source evidence
- cross_nutrient
- B6 and iron-sulfur cluster coexistence; functional nutritional interaction remains untested.
- experimental_model
- Pig liver GABA aminotransferase; inhibitor complexes and spectroscopy
- exposure
- Native and inhibitor-bound enzyme crystallography.
- limitations
- The cluster function was unknown; no iron-deficiency or B6-rescue response was demonstrated.
- nutrient_topic
- Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
- organism
- Sus scrofa
- plain_language
- Iron and B6 occur in the same enzyme structure.
- primary_references
- [storici-2004-gaba-at] Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin (2004). https://doi.org/10.1074/jbc.M305884200 DOI: 10.1074/jbc.M305884200
- tissue_or_cell_type
- Pig liver enzyme
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1083–1094
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Pig liver GABA aminotransferase; inhibitor complexes and spectroscopy · source_derived_draft · unverified_draft
### b6-neuro-gaba-at-iron-cluster Native and inhibitor-bound pig liver GABA-AT structures resolved a [2Fe-2S] cluster near the PLP sites. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron and B6 occur in the same enzyme structure. organism: Sus scrofa tissue_or_cell_type: Pig liver enzyme experimental_model: Pig liver GABA aminotransferase; inhibitor complexes and spectroscopy limitations: The cluster function was unknown; no iron-deficiency or B6-rescue response was demonstrated. exposure: Native and inhibitor-bound enzyme crystallography. cross_nutrient: B6 and iron-sulfur cluster coexistence; functional nutritional interaction remains untested. [storici-2004-gaba-at] Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin (2004). https://doi.org/10.1074/jbc.M305884200 DOI: 10.1074/jbc.M305884200
Complete structured claim and evidencePig GABA aminotransferase contains a PLP-dependent active site for GABA degradation.
Experimental context and source evidence
- experimental_model
- Purified pig GABA aminotransferase; crystallography
- exposure
- Purified native pig GABA aminotransferase structure.
- limitations
- Pig enzyme evidence cannot alone predict human brain GABA responses to B6.
- nutrient_topic
- Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
- organism
- Sus scrofa
- plain_language
- B6 participates in GABA breakdown as well as synthesis.
- primary_references
- [storici-1999-gaba-at] Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy (1999). https://iris.uniroma1.it/handle/11573/393739 DOI: 10.1021/bi990478j
- tissue_or_cell_type
- Purified pig enzyme
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1071–1081
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified pig GABA aminotransferase; crystallography · source_derived_draft · unverified_draft
### b6-neuro-gaba-degradation Pig GABA aminotransferase contains a PLP-dependent active site for GABA degradation. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: B6 participates in GABA breakdown as well as synthesis. organism: Sus scrofa tissue_or_cell_type: Purified pig enzyme experimental_model: Purified pig GABA aminotransferase; crystallography limitations: Pig enzyme evidence cannot alone predict human brain GABA responses to B6. exposure: Purified native pig GABA aminotransferase structure. [storici-1999-gaba-at] Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy (1999). https://iris.uniroma1.it/handle/11573/393739 DOI: 10.1021/bi990478j
Complete structured claim and evidence
What acts on it
Vigabatrin formed a covalent adduct involving pig GABA-AT Lys329 and its PLP cofactor.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- experimental_model
- Pig liver GABA aminotransferase; inhibitor complexes and spectroscopy
- exposure
- Inhibitor-treated purified enzyme.
- limitations
- Does not establish systemic B6 depletion.
- nutrient_topic
- Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
- organism
- Sus scrofa
- plain_language
- The drug traps the enzyme together with its B6 cofactor.
- primary_references
- [storici-2004-gaba-at] Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin (2004). https://doi.org/10.1074/jbc.M305884200 DOI: 10.1074/jbc.M305884200
- tissue_or_cell_type
- Pig liver enzyme
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1096–1106
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Pig liver GABA aminotransferase; inhibitor complexes and spectroscopy · source_derived_draft · unverified_draft
### b6-neuro-vigabatrin-plp-adduct Vigabatrin formed a covalent adduct involving pig GABA-AT Lys329 and its PLP cofactor. Condition category: machinery_impairment nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The drug traps the enzyme together with its B6 cofactor. organism: Sus scrofa tissue_or_cell_type: Pig liver enzyme experimental_model: Pig liver GABA aminotransferase; inhibitor complexes and spectroscopy limitations: Does not establish systemic B6 depletion. exposure: Inhibitor-treated purified enzyme. [storici-2004-gaba-at] Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin (2004). https://doi.org/10.1074/jbc.M305884200 DOI: 10.1074/jbc.M305884200
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.