Component
N-Carbamoyl-L-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
Purified human CAD aspartate-transcarbamylase domain converted carbamoyl phosphate and aspartate to carbamoyl-aspartate in an initial-rate assay.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Recombinant human CAD ATCase domain fused to MBP; biochemical assay.
- limitations
- Isolated-domain kinetics are not whole-cell nucleotide flux.
- nutrient_topic
- L-Aspartate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Aspartate
- plain_language
- Aspartate becomes part of the precursor used to build pyrimidine bases.
- primary_references
- Succinate dehydrogenase loss suppresses pyrimidine biosynthesis via succinate-mediated inhibition of aspartate transcarbamylase. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42082831/ · DOI 10.1038/s42255-026-01524-w
L-Aspartate: redox transfer, nitrogen partitioning and cross-nutrient mechanisms (2026-09-19) · lines 146–152
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human CAD ATCase domain fused to MBP; biochemical assay. · source_derived_draft · unverified_draft
## l-aspartate-cad-aspartate-reaction Aspartate becomes part of the precursor used to build pyrimidine bases. Purified human CAD aspartate-transcarbamylase domain converted carbamoyl phosphate and aspartate to carbamoyl-aspartate in an initial-rate assay. Model: Recombinant human CAD ATCase domain fused to MBP; biochemical assay. Limitations: Isolated-domain kinetics are not whole-cell nucleotide flux. Evidence access: Primary full text Succinate dehydrogenase loss suppresses pyrimidine biosynthesis via succinate-mediated inhibition of aspartate transcarbamylase. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42082831/ · DOI 10.1038/s42255-026-01524-w
Complete structured claim and evidence
Where it participates (unsigned role)
Succinate competitively inhibited aspartate utilization by the purified human CAD ATCase domain.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Recombinant human ATCase kinetic experiments with succinate and substrate titration.
- limitations
- This is not proof that ordinary dietary succinate or aspartate concentrations cause the same inhibition in a person.
- nutrient_topic
- L-Aspartate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Aspartate
- plain_language
- An accumulated carbon-cycle metabolite competes with aspartate at a nucleotide-making enzyme.
- primary_references
- Succinate dehydrogenase loss suppresses pyrimidine biosynthesis via succinate-mediated inhibition of aspartate transcarbamylase. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42082831/ · DOI 10.1038/s42255-026-01524-w
L-Aspartate: redox transfer, nitrogen partitioning and cross-nutrient mechanisms (2026-09-19) · lines 210–216
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human ATCase kinetic experiments with succinate and substrate titration. · source_derived_draft · unverified_draft
## l-aspartate-succinate-atcase An accumulated carbon-cycle metabolite competes with aspartate at a nucleotide-making enzyme. Succinate competitively inhibited aspartate utilization by the purified human CAD ATCase domain. Model: Recombinant human ATCase kinetic experiments with succinate and substrate titration. Limitations: This is not proof that ordinary dietary succinate or aspartate concentrations cause the same inhibition in a person. Evidence access: Primary full text Succinate dehydrogenase loss suppresses pyrimidine biosynthesis via succinate-mediated inhibition of aspartate transcarbamylase. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42082831/ · DOI 10.1038/s42255-026-01524-w
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.