Component

Phosphocholine

Independent biological entity. Read linked claims for experimental scope and context.

4 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.

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 it acts on

  1. Human PHOSPHO1 also hydrolyzes phosphocholine, producing inorganic phosphate and choline.

    Experimental context and source evidence
    experimental_model
    Purified-enzyme substrate assay
    limitations
    This reaction uses magnesium-dependent machinery; calcium is the eventual mineral constituent, not the demonstrated phosphatase cofactor.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Homo sapiens
    plain_language
    A second phospholipid-headgroup metabolite can supply phosphate.
    primary_references
    [roberts2004] Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities (2004). https://pubmed.ncbi.nlm.nih.gov/15175005/ DOI: 10.1042/BJ20040511
    tissue_or_cell_type
    Recombinant enzyme

    Calcium: mechanism-first literature curation (2026-09-17) · lines 908–917

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified-enzyme substrate assay · source_derived_draft · unverified_draft

    ### phospho1-phosphocholine-hydrolysis Human PHOSPHO1 also hydrolyzes phosphocholine, producing inorganic phosphate and choline. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: A second phospholipid-headgroup metabolite can supply phosphate. organism: Homo sapiens tissue_or_cell_type: Recombinant enzyme experimental_model: Purified-enzyme substrate assay limitations: This reaction uses magnesium-dependent machinery; calcium is the eventual mineral constituent, not the demonstrated phosphatase cofactor. [roberts2004] Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities (2004). https://pubmed.ncbi.nlm.nih.gov/15175005/ DOI: 10.1042/BJ20040511
    Complete structured claim and evidence

What acts on it

  1. Human choline kinase alpha1 catalyzes ATP-dependent phosphorylation of choline, producing phosphocholine and ADP in magnesium-containing conditions.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/choline-research/25515750.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "742dc604629df5eae2bb6cfc0ef0a13cbd69f5e318a2f3292e98f2e707958aeb", "start_char": 0, "end_char": 1321, "text_sha256": "742dc604629df5eae2bb6cfc0ef0a13cbd69f5e318a2f3292e98f2e707958aeb"}
    experimental_model
    Human choline kinase alpha1 and pathogen-enzyme biochemical comparison
    exposure
    ATP-dependent choline phosphorylation in magnesium-containing assays
    limitations
    The shared enzyme requirement is not a clinical magnesium threshold or proof of a general supplement rescue.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Human alpha1 isoform; pathogen comparators remain separate
    plain_language
    Choline enters membrane synthesis through an ATP-powered phosphorylation step.
    primary_references
    [choline-p25515750] Choline kinase active site provides features for designing versatile inhibitors. (2014). https://pubmed.ncbi.nlm.nih.gov/25515750/ DOI: 10.2174/1568026614666141216093337
    tissue_or_cell_type
    Purified choline kinase active site

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 698–709

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human choline kinase alpha1 and pathogen-enzyme biochemical comparison · source_derived_draft · unverified_draft

    ### choline-chka-phosphocholine Human choline kinase alpha1 catalyzes ATP-dependent phosphorylation of choline, producing phosphocholine and ADP in magnesium-containing conditions. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: Choline enters membrane synthesis through an ATP-powered phosphorylation step. organism: Human alpha1 isoform; pathogen comparators remain separate tissue_or_cell_type: Purified choline kinase active site experimental_model: Human choline kinase alpha1 and pathogen-enzyme biochemical comparison limitations: The shared enzyme requirement is not a clinical magnesium threshold or proof of a general supplement rescue. exposure: ATP-dependent choline phosphorylation in magnesium-containing assays evidence_span: {"source_cache": "artifacts/choline-research/25515750.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "742dc604629df5eae2bb6cfc0ef0a13cbd69f5e318a2f3292e98f2e707958aeb", "start_char": 0, "end_char": 1321, "text_sha256": "742dc604629df5eae2bb6cfc0ef0a13cbd69f5e318a2f3292e98f2e707958aeb"} [choline-p25515750] Choline kinase active site provides features for designing versatile inhibitors. (2014). https://pubmed.ncbi.nlm.nih.gov/25515750/ DOI: 10.2174/1568026614666141216093337
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Recombinant human PHOSPHO1 showed strong Mg dependence when hydrolyzing phosphoethanolamine and phosphocholine.

    Experimental context and source evidence
    cross_nutrient
    Magnesium -> PHOSPHO1 -> phosphate production; joins the existing calcium PHOSPHO1 records.
    experimental_model
    Purified recombinant phosphatase assays.
    limitations
    Enzyme evidence does not measure the effect of oral Mg on bone; substrate Km values are not Mg deficiency thresholds.
    nutrient_topic
    Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
    organism
    Homo sapiens
    plain_language
    Magnesium helps a phosphate-releasing enzyme already connected to calcium mineralization.
    primary_references
    [mg-roberts2004] Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities (2004). https://pubmed.ncbi.nlm.nih.gov/15175005/ DOI: 10.1042/bj20040511
    tissue_or_cell_type
    Purified recombinant human PHOSPHO1

    Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 1455–1465

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant phosphatase assays. · source_derived_draft · unverified_draft

    ### mg-phospho1-cofactor Recombinant human PHOSPHO1 showed strong Mg dependence when hydrolyzing phosphoethanolamine and phosphocholine. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Magnesium helps a phosphate-releasing enzyme already connected to calcium mineralization. organism: Homo sapiens tissue_or_cell_type: Purified recombinant human PHOSPHO1 experimental_model: Purified recombinant phosphatase assays. limitations: Enzyme evidence does not measure the effect of oral Mg on bone; substrate Km values are not Mg deficiency thresholds. cross_nutrient: Magnesium -> PHOSPHO1 -> phosphate production; joins the existing calcium PHOSPHO1 records. [mg-roberts2004] Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities (2004). https://pubmed.ncbi.nlm.nih.gov/15175005/ DOI: 10.1042/bj20040511
    Complete structured claim and evidence
  2. Human CCTbeta expression increased CCT activity and cellular CDP-choline accumulation in COS-7 cells.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/phosphorus-research/9593753.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6ed2c0c0ceaa7eb2efb90c66565bae51b71023f77cdd0224159fd9814e3b7d45", "start_char": 0, "end_char": 1766, "text_sha256": "6ed2c0c0ceaa7eb2efb90c66565bae51b71023f77cdd0224159fd9814e3b7d45"}
    experimental_model
    Human isoform cloning and COS-7 expression studies
    exposure
    CCTbeta transfection and catalytic assays with lipid regulators
    limitations
    Expression-system findings; maximum activity required lipid regulators. Do not generalize the early clone to every subsequently described splice variant.
    nutrient_topic
    Phosphorus research collection; topical membership is not evidence of a direct dietary effect. · Phosphorus
    organism
    Human PCYT1B expressed in African-green-monkey-derived COS-7 cells
    plain_language
    A separately identified enzyme activates the phosphocholine building block.
    primary_references
    [phosphorus-p9593753] Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase. (1998). https://pubmed.ncbi.nlm.nih.gov/9593753/ DOI: 10.1074/jbc.273.22.14022
    tissue_or_cell_type
    Cytoplasm and phospholipid biosynthesis

    Phosphorus: metabolism, signaling and nutrient connections (2026-09-17) · lines 698–709

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human isoform cloning and COS-7 expression studies · source_derived_draft · unverified_draft

    ### phosphorus-pcyt-cdp Human CCTbeta expression increased CCT activity and cellular CDP-choline accumulation in COS-7 cells. Condition category: normal nutrient_topic: Phosphorus research collection; topical membership is not evidence of a direct dietary effect. plain_language: A separately identified enzyme activates the phosphocholine building block. organism: Human PCYT1B expressed in African-green-monkey-derived COS-7 cells tissue_or_cell_type: Cytoplasm and phospholipid biosynthesis experimental_model: Human isoform cloning and COS-7 expression studies limitations: Expression-system findings; maximum activity required lipid regulators. Do not generalize the early clone to every subsequently described splice variant. exposure: CCTbeta transfection and catalytic assays with lipid regulators evidence_span: {"source_cache": "artifacts/phosphorus-research/9593753.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6ed2c0c0ceaa7eb2efb90c66565bae51b71023f77cdd0224159fd9814e3b7d45", "start_char": 0, "end_char": 1766, "text_sha256": "6ed2c0c0ceaa7eb2efb90c66565bae51b71023f77cdd0224159fd9814e3b7d45"} [phosphorus-p9593753] Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase. (1998). https://pubmed.ncbi.nlm.nih.gov/9593753/ DOI: 10.1074/jbc.273.22.14022
    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