Component
Iminoaspartate
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 acts on it
Porcine kidney DDO oxidized D-aspartate to iminoaspartate while reducing enzyme-bound FAD.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Purified native and recombinant porcine kidney enzyme.
- limitations
- Species-specific enzyme evidence; FAD is recycled rather than consumed once per substrate molecule.
- nutrient_topic
- D-Aspartate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · D-Aspartate
- plain_language
- The first chemical step removes reducing equivalents from D-aspartate.
- primary_references
- Functional and structural characterization of D-aspartate oxidase from porcine kidney: non-Michaelis kinetics due to substrate activation. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17234685/ · DOI 10.1093/jb/mvm041
D-Aspartate: synthesis, clearance, neural and endocrine mechanisms (2026-09-19) · lines 104–110
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified native and recombinant porcine kidney enzyme. · source_derived_draft · unverified_draft
## d-aspartate-ddo-imino The first chemical step removes reducing equivalents from D-aspartate. Porcine kidney DDO oxidized D-aspartate to iminoaspartate while reducing enzyme-bound FAD. Model: Purified native and recombinant porcine kidney enzyme. Limitations: Species-specific enzyme evidence; FAD is recycled rather than consumed once per substrate molecule. Evidence access: Primary abstract Functional and structural characterization of D-aspartate oxidase from porcine kidney: non-Michaelis kinetics due to substrate activation. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17234685/ · DOI 10.1093/jb/mvm041
Complete structured claim and evidence
Where it participates (unsigned role)
Reoxidation of reduced FAD by oxygen during porcine DDO turnover produced hydrogen peroxide.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Purified porcine enzyme oxidative half-reaction.
- limitations
- This chemistry alone does not demonstrate oxidative injury after human oral supplementation.
- nutrient_topic
- D-Aspartate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · D-Aspartate
- plain_language
- Clearing D-aspartate also generates a peroxide-handling requirement.
- primary_references
- Functional and structural characterization of D-aspartate oxidase from porcine kidney: non-Michaelis kinetics due to substrate activation. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17234685/ · DOI 10.1093/jb/mvm041
D-Aspartate: synthesis, clearance, neural and endocrine mechanisms (2026-09-19) · lines 112–118
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified porcine enzyme oxidative half-reaction. · source_derived_draft · unverified_draft
## d-aspartate-ddo-peroxide Clearing D-aspartate also generates a peroxide-handling requirement. Reoxidation of reduced FAD by oxygen during porcine DDO turnover produced hydrogen peroxide. Model: Purified porcine enzyme oxidative half-reaction. Limitations: This chemistry alone does not demonstrate oxidative injury after human oral supplementation. Evidence access: Primary abstract Functional and structural characterization of D-aspartate oxidase from porcine kidney: non-Michaelis kinetics due to substrate activation. · 2007 · https://pubmed.ncbi.nlm.nih.gov/17234685/ · DOI 10.1093/jb/mvm041
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.