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Literature summary for 7.2.2.10 extracted from

  • Tadini-Buoninsegni, F.; Bartolommei, G.; Moncelli, M.R.; Tal, D.M.; Lewis, D.; Inesi, G.
    Effects of high-affinity inhibitors on partial reactions, charge movements, and conformational states of the Ca2+ transport ATPase (sarco-endoplasmic reticulum Ca2+ ATPase) (2008), Mol. Pharmacol., 73, 1134-1140.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
1,3-dibromo-2,4,6-tri(methylisothiouronium)benzene micromolar inhibitor of SERCA Oryctolagus cuniculus
2,5-di(tert-butyl)hydroquinone micromolar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation Oryctolagus cuniculus
cyclopiazonic acid nanomalar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation Oryctolagus cuniculus
thapsigargin nanomalar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation Oryctolagus cuniculus

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ dependent on Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P04191
-
-

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+ transport ATPase
-
Oryctolagus cuniculus
sarco-endoplasmic reticulum Ca2+ ATPase
-
Oryctolagus cuniculus
SERCA
-
Oryctolagus cuniculus