Component
Purified BCOADC in the 1986 ketoacid study, source species unverified
Context-specific entity; species, compartment and exposure are stated on each claim.
2 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
Purified BCOADC oxidized 2-oxobutyrate with a reported Km of 18 micromolar; purified PDC also accepted it, whereas OGDH did not.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Purified-enzyme comparison; source species is not specified in the accessible abstract.
- limitations
- This is not recorded as direct human enzyme evidence or an exclusive BCKDH route. Correction record: PubMed indexes an erratum in Biochemical Journal 1987;242(3):935. The notice text was inaccessible during this curation; its specific scope and impact remain unverified. The purified-enzyme findings are retained provisionally with this flag, and the abstract does not identify the source species. https://pubmed.ncbi.nlm.nih.gov/3800905/
- nutrient_topic
- L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
- plain_language
- More than one ketoacid complex can handle this carbon skeleton in vitro.
- primary_references
- Oxidative decarboxylation of 4-methylthio-2-oxobutyrate by branched-chain 2-oxo acid dehydrogenase complex. · 1986 · https://pubmed.ncbi.nlm.nih.gov/3800905/ · DOI 10.1042/bj2370621
L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 306–312
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified-enzyme comparison; source species is not specified in the accessible abstract. · source_derived_draft · unverified_draft
## l-threonine-ketoacid-oxidation More than one ketoacid complex can handle this carbon skeleton in vitro. Purified BCOADC oxidized 2-oxobutyrate with a reported Km of 18 micromolar; purified PDC also accepted it, whereas OGDH did not. Model: Purified-enzyme comparison; source species is not specified in the accessible abstract. Limitations: This is not recorded as direct human enzyme evidence or an exclusive BCKDH route. Correction record: PubMed indexes an erratum in Biochemical Journal 1987;242(3):935. The notice text was inaccessible during this curation; its specific scope and impact remain unverified. The purified-enzyme findings are retained provisionally with this flag, and the abstract does not identify the source species. https://pubmed.ncbi.nlm.nih.gov/3800905/ Evidence access: Primary abstract Oxidative decarboxylation of 4-methylthio-2-oxobutyrate by branched-chain 2-oxo acid dehydrogenase complex. · 1986 · https://pubmed.ncbi.nlm.nih.gov/3800905/ · DOI 10.1042/bj2370621
Complete structured claim and evidence
Where it participates (unsigned role)
2-Oxobutyrate inhibited BCOADC kinase, and reduced BCOADC phosphorylation was observed in isolated adipocytes.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Purified kinase and isolated-adipocyte assays; species unverified from abstract.
- limitations
- This does not prove that a threonine supplement changes BCAA oxidation in humans. Correction record: PubMed indexes an erratum in Biochemical Journal 1987;242(3):935. The notice text was inaccessible during this curation; its specific scope and impact remain unverified. The purified-enzyme findings are retained provisionally with this flag, and the abstract does not identify the source species. https://pubmed.ncbi.nlm.nih.gov/3800905/
- nutrient_topic
- L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
- plain_language
- A catabolic intermediate can influence the regulatory brake on its disposal machinery.
- primary_references
- Oxidative decarboxylation of 4-methylthio-2-oxobutyrate by branched-chain 2-oxo acid dehydrogenase complex. · 1986 · https://pubmed.ncbi.nlm.nih.gov/3800905/ · DOI 10.1042/bj2370621
L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 314–320
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified kinase and isolated-adipocyte assays; species unverified from abstract. · source_derived_draft · unverified_draft
## l-threonine-ketoacid-feedback A catabolic intermediate can influence the regulatory brake on its disposal machinery. 2-Oxobutyrate inhibited BCOADC kinase, and reduced BCOADC phosphorylation was observed in isolated adipocytes. Model: Purified kinase and isolated-adipocyte assays; species unverified from abstract. Limitations: This does not prove that a threonine supplement changes BCAA oxidation in humans. Correction record: PubMed indexes an erratum in Biochemical Journal 1987;242(3):935. The notice text was inaccessible during this curation; its specific scope and impact remain unverified. The purified-enzyme findings are retained provisionally with this flag, and the abstract does not identify the source species. https://pubmed.ncbi.nlm.nih.gov/3800905/ Evidence access: Primary abstract Oxidative decarboxylation of 4-methylthio-2-oxobutyrate by branched-chain 2-oxo acid dehydrogenase complex. · 1986 · https://pubmed.ncbi.nlm.nih.gov/3800905/ · DOI 10.1042/bj2370621
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.