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Literature summary for 7.2.2.10 extracted from

  • Zafar, S.; Hussain, A.; Liu, Y.; Lewis, D.; Inesi, G.
    Specificity of ligand binding to transport sites: Ca2+ binding to the Ca2+ transport ATPase and its dependence on H+ and Mg2+ (2008), Arch. Biochem. Biophys., 476, 87-94.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.2.2.10

Inhibitors

Inhibitors Comment Organism Structure
Mg2+ Mg2+ at high concentration (10 mM) and high pH inhibits the ATPase by binding to low affinity sites made available by the high pH in the medium Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
sarcoplasmic reticulum
-
 Oryctolagus cuniculus 16529
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ SERCA binds two Ca2+ per mole Oryctolagus cuniculus
Mg2+ 1 mM Mg2+ (a concentration equivalent to that of ATP) is an absolute requirement for ATPase activity Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Ca2+/cis
-
 Oryctolagus cuniculus ADP + phosphate + Ca2+/trans
-
 ?

Synonyms

Synonyms Comment Organism
Ca2+ ATPase of sarcoplasmic reticulum
-
 Oryctolagus cuniculus
Ca2+ transport ATPase of sarco-endoplasmic reticulum
-
 Oryctolagus cuniculus
SERCA
-
 Oryctolagus cuniculus