Component
Phosphoethanolamine
Independent biological entity. Read linked claims for experimental scope and context.
3 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 hydrolyzes phosphoethanolamine, releasing inorganic phosphate and ethanolamine; the enzyme requires Mg2+ in the assay.
Experimental context and source evidence
- experimental_model
- Purified-enzyme substrate assay
- limitations
- Catalytic capacity does not quantify phosphate supply in vivo; Pi denotes pH-dependent protonation states.
- nutrient_topic
- Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
- organism
- Homo sapiens
- plain_language
- PHOSPHO1 can release phosphate from a membrane-headgroup metabolite.
- 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; mineralizing-cell context
Calcium: mechanism-first literature curation (2026-09-17) · lines 897–906
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-phosphoethanolamine-hydrolysis Human PHOSPHO1 hydrolyzes phosphoethanolamine, releasing inorganic phosphate and ethanolamine; the enzyme requires Mg2+ in the assay. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: PHOSPHO1 can release phosphate from a membrane-headgroup metabolite. organism: Homo sapiens tissue_or_cell_type: Recombinant enzyme; mineralizing-cell context experimental_model: Purified-enzyme substrate assay limitations: Catalytic capacity does not quantify phosphate supply in vivo; Pi denotes pH-dependent protonation states. [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
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 evidenceActive PHOSPHO1 was detected inside osteoblast-derived matrix vesicles; phosphoethanolamine hydrolase activity became accessible after vesicle sonication.
Experimental context and source evidence
- compartment_description
- Matrix-vesicle lumen
- experimental_model
- Localization and activity assays, including Alpl-deficient vesicles
- limitations
- Localization does not establish the sole route for vesicle phosphate or calcium entry.
- nutrient_topic
- Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
- organism
- Mus musculus
- plain_language
- Mineralizing vesicles contain phosphate-generating machinery within their membrane.
- primary_references
- [roberts2007] Functional involvement of PHOSPHO1 in matrix vesicle-mediated skeletal mineralization (2007). https://pubmed.ncbi.nlm.nih.gov/17227223/ DOI: 10.1359/jbmr.070108
- tissue_or_cell_type
- Osteoblast-derived matrix vesicles
Calcium: mechanism-first literature curation (2026-09-17) · lines 919–929
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Localization and activity assays, including Alpl-deficient vesicles · source_derived_draft · unverified_draft
### phospho1-in-matrix-vesicles Active PHOSPHO1 was detected inside osteoblast-derived matrix vesicles; phosphoethanolamine hydrolase activity became accessible after vesicle sonication. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Mineralizing vesicles contain phosphate-generating machinery within their membrane. organism: Mus musculus tissue_or_cell_type: Osteoblast-derived matrix vesicles experimental_model: Localization and activity assays, including Alpl-deficient vesicles limitations: Localization does not establish the sole route for vesicle phosphate or calcium entry. compartment_description: Matrix-vesicle lumen [roberts2007] Functional involvement of PHOSPHO1 in matrix vesicle-mediated skeletal mineralization (2007). https://pubmed.ncbi.nlm.nih.gov/17227223/ DOI: 10.1359/jbmr.070108
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.