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.
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 it acts on
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
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)
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 evidenceHuman 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
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.