Component
Sodium-potassium ATPase phosphorylation
Formation of the pump phosphoenzyme during ATP-dependent catalytic cycling.
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
Shark-pump kinetic fits assigned E1-ATP Mg affinity mainly to ATP coordination, after accounting for free ATP competition.
Experimental context and source evidence
- cross_nutrient
- Magnesium-dependent ATP chemistry is coupled to sodium and potassium handling by the pump; serum magnesium is not the enzyme-site concentration.
- experimental_model
- Shark rectal-gland pump membrane fragments; stopped-flow RH421 fluorescence under Na-rich conditions.
- limitations
- Conclusion concerns E1-ATP; other pump conformations or Mg sites can behave differently.
- nutrient_topic
- Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
- organism
- Shark
- plain_language
- The ATP-associated magnesium supports phosphorylation; free ATP can compete for that magnesium.
- primary_references
- [pilotelle-2009-nka] Mechanism of Mg2+ binding in the Na+,K+-ATPase (2009). https://pmc.ncbi.nlm.nih.gov/articles/PMC2711396/ DOI: 10.1016/j.bpj.2009.01.042
- tissue_or_cell_type
- Rectal-gland enzyme membrane fragments
Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 795–805
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Shark rectal-gland pump membrane fragments; stopped-flow RH421 fluorescence under Na-rich conditions. · source_derived_draft · unverified_draft
### mg-nka-atp-dominates-mg-binding Shark-pump kinetic fits assigned E1-ATP Mg affinity mainly to ATP coordination, after accounting for free ATP competition. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: The ATP-associated magnesium supports phosphorylation; free ATP can compete for that magnesium. organism: Shark tissue_or_cell_type: Rectal-gland enzyme membrane fragments experimental_model: Shark rectal-gland pump membrane fragments; stopped-flow RH421 fluorescence under Na-rich conditions. limitations: Conclusion concerns E1-ATP; other pump conformations or Mg sites can behave differently. cross_nutrient: Magnesium-dependent ATP chemistry is coupled to sodium and potassium handling by the pump; serum magnesium is not the enzyme-site concentration. [pilotelle-2009-nka] Mechanism of Mg2+ binding in the Na+,K+-ATPase (2009). https://pmc.ncbi.nlm.nih.gov/articles/PMC2711396/ DOI: 10.1016/j.bpj.2009.01.042
Complete structured claim and evidencePre-steady-state pig-kidney pump experiments identified Mg as an essential activator of ATP-dependent phosphorylation.
Experimental context and source evidence
- cross_nutrient
- Magnesium-dependent ATP chemistry is coupled to sodium and potassium handling by the pump; serum magnesium is not the enzyme-site concentration.
- experimental_model
- Pig-kidney Na/K-ATPase rapid-mixing phosphorylation; Na-containing, K-free medium; varied ATP and MgCl2.
- limitations
- Na-containing, K-free assay; not the full physiological transport cycle.
- nutrient_topic
- Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
- organism
- Sus scrofa
- plain_language
- Magnesium enables the ATP-driven phosphate-transfer step of the sodium pump.
- primary_references
- [campos-1992-nka] Effects of magnesium and ATP on pre-steady-state phosphorylation kinetics of the Na+,K(+)-ATPase (1992). https://pubmed.ncbi.nlm.nih.gov/1314673/ DOI: 10.1016/0005-2736(92)90161-e
- tissue_or_cell_type
- Kidney enzyme
Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 771–781
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Pig-kidney Na/K-ATPase rapid-mixing phosphorylation; Na-containing, K-free medium; varied ATP and MgCl2. · source_derived_draft · unverified_draft
### mg-nka-phosphorylation-requirement Pre-steady-state pig-kidney pump experiments identified Mg as an essential activator of ATP-dependent phosphorylation. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Magnesium enables the ATP-driven phosphate-transfer step of the sodium pump. organism: Sus scrofa tissue_or_cell_type: Kidney enzyme experimental_model: Pig-kidney Na/K-ATPase rapid-mixing phosphorylation; Na-containing, K-free medium; varied ATP and MgCl2. limitations: Na-containing, K-free assay; not the full physiological transport cycle. cross_nutrient: Magnesium-dependent ATP chemistry is coupled to sodium and potassium handling by the pump; serum magnesium is not the enzyme-site concentration. [campos-1992-nka] Effects of magnesium and ATP on pre-steady-state phosphorylation kinetics of the Na+,K(+)-ATPase (1992). https://pubmed.ncbi.nlm.nih.gov/1314673/ DOI: 10.1016/0005-2736(92)90161-e
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.