Component
N-Methyl-D-aspartate
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
Human DDO-1 also oxidized N-methyl-D-aspartate, with reported Km 6.8 mM and kcat 37.7 per second.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Purified recombinant human DDO-1.
- limitations
- Does not establish endogenous NMDA synthesis or justify conflating NMDA with D-aspartate.
- nutrient_topic
- D-Aspartate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · D-Aspartate
- plain_language
- The enzyme accepts a related chemical that is distinct from the NMDA receptor.
- primary_references
- Structural and functional characterization of the human brain D-aspartate oxidase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9163533/ · DOI 10.1093/oxfordjournals.jbchem.a021655
D-Aspartate: synthesis, clearance, neural and endocrine mechanisms (2026-09-19) · lines 80–86
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified recombinant human DDO-1. · source_derived_draft · unverified_draft
## d-aspartate-human-ddo-nmda The enzyme accepts a related chemical that is distinct from the NMDA receptor. Human DDO-1 also oxidized N-methyl-D-aspartate, with reported Km 6.8 mM and kcat 37.7 per second. Model: Purified recombinant human DDO-1. Limitations: Does not establish endogenous NMDA synthesis or justify conflating NMDA with D-aspartate. Evidence access: Primary abstract Structural and functional characterization of the human brain D-aspartate oxidase. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9163533/ · DOI 10.1093/oxfordjournals.jbchem.a021655
Complete structured claim and evidence
Where it participates (unsigned role)
Porcine DDO showed substrate activation above approximately 0.2 mM D-aspartate; N-methyl-D-aspartate instead produced substrate inhibition.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Purified porcine enzyme concentration-response assays.
- limitations
- Do not extrapolate assay thresholds to dietary dosing.
- nutrient_topic
- D-Aspartate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · D-Aspartate
- plain_language
- Different substrates change the enzyme kinetics differently.
- 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 120–126
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified porcine enzyme concentration-response assays. · source_derived_draft · unverified_draft
## d-aspartate-ddo-substrate-activation Different substrates change the enzyme kinetics differently. Porcine DDO showed substrate activation above approximately 0.2 mM D-aspartate; N-methyl-D-aspartate instead produced substrate inhibition. Model: Purified porcine enzyme concentration-response assays. Limitations: Do not extrapolate assay thresholds to dietary dosing. 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.