Component

Carbamoyl phosphate

Carbamoyl phosphate. Species, exposure and limitations are retained in each linked claim.

3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

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.

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.

Recorded relationships

What acts on it

  1. CPS1 uses two ATP-dependent phosphorylation steps to convert bicarbonate and ammonia into carbamoyl phosphate.

    Human carbamoyl-phosphate synthetase 1 / CPS1 → Carbamoyl phosphate source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/citrulline-research/26592762.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9807338d87ba1b5602512aa3765c7cc48d391595cc1f35e6a43bcbe1250d3c7d", "start_char": 1169, "end_char": 1477, "text_sha256": "c5e2a8e1d3e3a09064b7b233635f7d573f8761b3f6ae18a68bc9b102a2d5874c"}
    experimental_model
    Human recombinant enzyme crystallography and mutation analysis
    exposure
    Structures without NAG and with NAG plus nucleotides
    limitations
    Mechanism of enzyme activation; clinical effects of adding nutritional cofactors were not tested.
    nutrient_topic
    Citrulline research collection; topical membership is not evidence of a direct dietary effect. · L-Citrulline
    organism
    Human CPS1
    plain_language
    The upstream part of citrulline synthesis consumes energy to handle ammonia.
    primary_references
    [citrulline-p26592762] Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis. (2015). https://pubmed.ncbi.nlm.nih.gov/26592762/ DOI: 10.1038/srep16950
    tissue_or_cell_type
    Mitochondrial carbamoyl-phosphate synthesis

    Citrulline: arginine recycling, nitrogen disposal and nutrient connections (2026-09-17) · lines 242–253

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human recombinant enzyme crystallography and mutation analysis · source_derived_draft · unverified_draft

    ### citrulline-cps1-product CPS1 uses two ATP-dependent phosphorylation steps to convert bicarbonate and ammonia into carbamoyl phosphate. Condition category: normal nutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect. plain_language: The upstream part of citrulline synthesis consumes energy to handle ammonia. organism: Human CPS1 tissue_or_cell_type: Mitochondrial carbamoyl-phosphate synthesis experimental_model: Human recombinant enzyme crystallography and mutation analysis limitations: Mechanism of enzyme activation; clinical effects of adding nutritional cofactors were not tested. exposure: Structures without NAG and with NAG plus nucleotides evidence_span: {"source_cache": "artifacts/citrulline-research/26592762.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9807338d87ba1b5602512aa3765c7cc48d391595cc1f35e6a43bcbe1250d3c7d", "start_char": 1169, "end_char": 1477, "text_sha256": "c5e2a8e1d3e3a09064b7b233635f7d573f8761b3f6ae18a68bc9b102a2d5874c"} [citrulline-p26592762] Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis. (2015). https://pubmed.ncbi.nlm.nih.gov/26592762/ DOI: 10.1038/srep16950
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Human OTC converts ornithine and carbamoyl phosphate into citrulline, releasing inorganic phosphate.

    Human ornithine transcarbamylase / OTC → L-Citrulline source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/citrulline-research/38940639.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5eca9d57812cf3d8efe7c0beb62b9b364cc25e1aeca647c95e4abf0fd9eb8365", "start_char": 194, "end_char": 364, "text_sha256": "c5ddbcd5c91cfcdc72d6e556c77228f8ecd6c25ebaa3c25fd9617f6baa145692"}
    experimental_model
    Recombinant enzyme site-directed mutagenesis and kinetic assays
    exposure
    Ornithine and carbamoyl phosphate; active-site and remote variants
    limitations
    Recombinant mutation experiments; do not equate altered enzyme function with a dietary shortage.
    nutrient_topic
    Citrulline research collection; topical membership is not evidence of a direct dietary effect. · L-Citrulline
    organism
    Human OTC
    plain_language
    Citrulline is built from ornithine and a nitrogen-containing carbamoyl group.
    primary_references
    [citrulline-p38940639] Revisiting the Roles of Catalytic Residues in Human Ornithine Transcarbamylase. (2024). https://pubmed.ncbi.nlm.nih.gov/38940639/ DOI: 10.1021/acs.biochem.4c00206
    tissue_or_cell_type
    Mitochondrial urea-cycle enzyme

    Citrulline: arginine recycling, nitrogen disposal and nutrient connections (2026-09-17) · lines 203–214

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant enzyme site-directed mutagenesis and kinetic assays · source_derived_draft · unverified_draft

    ### citrulline-otc-citrulline Human OTC converts ornithine and carbamoyl phosphate into citrulline, releasing inorganic phosphate. Condition category: normal nutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect. plain_language: Citrulline is built from ornithine and a nitrogen-containing carbamoyl group. organism: Human OTC tissue_or_cell_type: Mitochondrial urea-cycle enzyme experimental_model: Recombinant enzyme site-directed mutagenesis and kinetic assays limitations: Recombinant mutation experiments; do not equate altered enzyme function with a dietary shortage. exposure: Ornithine and carbamoyl phosphate; active-site and remote variants evidence_span: {"source_cache": "artifacts/citrulline-research/38940639.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5eca9d57812cf3d8efe7c0beb62b9b364cc25e1aeca647c95e4abf0fd9eb8365", "start_char": 194, "end_char": 364, "text_sha256": "c5ddbcd5c91cfcdc72d6e556c77228f8ecd6c25ebaa3c25fd9617f6baa145692"} [citrulline-p38940639] Revisiting the Roles of Catalytic Residues in Human Ornithine Transcarbamylase. (2024). https://pubmed.ncbi.nlm.nih.gov/38940639/ DOI: 10.1021/acs.biochem.4c00206
    Complete structured claim and evidence

  2. Purified human CAD aspartate-transcarbamylase domain converted carbamoyl phosphate and aspartate to carbamoyl-aspartate in an initial-rate assay.

    Human CAD multifunctional pyrimidine synthesis enzyme → N-Carbamoyl-L-aspartate source_derived_draftungraded
    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

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards