Component
Porcine-heart pyruvate dehydrogenase complex
Porcine-heart pyruvate dehydrogenase complex. Identity is distinct from its gene and experimentally modified states; see each claim for organism and scope.
1 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.
Where it participates (unsigned role)
In-vitro CoAlation of immunoprecipitated recombinant PDK2 reduced its phosphorylation of PDH E1, and DTT restored kinase activity.
Experimental context and source evidence
- cross_nutrient
- false
- evidence_location
- Full text lines 33, 61 and 141; Fig. 6D
- experimental_model
- FLAG-PDK2 expressed in HEK293 cells, immunoprecipitated and assayed with porcine-heart PDH
- exposure
- 1 mM CoA disulfide preincubation for 20 minutes; PDH phosphorylation assay with/without 2 mM DTT.
- limitations
- CoA disulfide is distinct from reduced CoA. The assay does not establish net mitochondrial PDH flux or a supplementation effect in vivo. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation.
- nutrient_topic
- Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
- organism
- Human PDK2; Sus scrofa PDH assay substrate
- plain_language
- Adding CoA through a disulfide bond reversibly inhibited the kinase that regulates pyruvate dehydrogenase.
- primary_references
- [b5-met-coalation2017] Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells. (2017). https://pubmed.ncbi.nlm.nih.gov/28341808/ DOI: 10.1042/bcj20170129
- tissue_or_cell_type
- Cell-free kinase assay
Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 1089–1101
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · FLAG-PDK2 expressed in HEK293 cells, immunoprecipitated and assayed with porcine-heart PDH · source_derived_draft · unverified_draft
### b5-met-pdk2-coalation-inhibition In-vitro CoAlation of immunoprecipitated recombinant PDK2 reduced its phosphorylation of PDH E1, and DTT restored kinase activity. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: Adding CoA through a disulfide bond reversibly inhibited the kinase that regulates pyruvate dehydrogenase. organism: Human PDK2; Sus scrofa PDH assay substrate tissue_or_cell_type: Cell-free kinase assay experimental_model: FLAG-PDK2 expressed in HEK293 cells, immunoprecipitated and assayed with porcine-heart PDH limitations: CoA disulfide is distinct from reduced CoA. The assay does not establish net mitochondrial PDH flux or a supplementation effect in vivo. This experiment does not establish a dietary pantothenate threshold or benefit from B5 supplementation. exposure: 1 mM CoA disulfide preincubation for 20 minutes; PDH phosphorylation assay with/without 2 mM DTT. cross_nutrient: false evidence_location: Full text lines 33, 61 and 141; Fig. 6D [b5-met-coalation2017] Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells. (2017). https://pubmed.ncbi.nlm.nih.gov/28341808/ DOI: 10.1042/bcj20170129
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.