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Literature summary for 7.2.2.10 extracted from

  • Pang, Y.; Zhu, H.; Wu, P.; Chen, J.
    The characterization of plasma membrane Ca2+-ATPase in rich sphingomyelin-cholesterol domains (2005), FEBS Lett., 579, 2397-2403.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane
-
Sus scrofa 5886
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Sus scrofa
Mg2+ required Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from brain by calmodulin affinity chromatography to homogeneity Sus scrofa

Renatured (Commentary)

Renatured (Comment) Organism
reconstitution of purified enzyme into proteoliposomes using microbeads, the enzyme is mixed with lipid in a 1:5000 protein to lipid molar ratio, removal of detergent, sealing of vesicles Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
Ca2+ uptake activity into artificial proteoliposomes, overview Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Ca2+/cis ATPase activity and Ca2+ uptake into artificial proteoliposomes activity Sus scrofa ADP + phosphate + Ca2+/trans
-
?
additional information the enzyme binds calmodulin with high affinity Sus scrofa ?
-
?

Subunits

Subunits Comment Organism
More PMCA is rich in sphingomyelin-cholesterol domains Sus scrofa

Synonyms

Synonyms Comment Organism
plasma membrane Ca2+-ATPase
-
Sus scrofa
PMCA
-
Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Sus scrofa