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Literature summary for 7.2.2.13 extracted from

  • Monti, J.L.E.; Montes, M.R.; Rossi, R.C.
    Steady-state analysis of enzymes with non-Michaelis-Menten kinetics The transport mechanism of Na+/K+-ATPase (2018), J. Biol. Chem., 293, 1373-1385 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.2.2.13

Metals/Ions

Metals/Ions Comment Organism Structure
Na+ Rb+ deocclusion is accelerated when Na+ binds to an allosteric, nonspecific site, leading to a 2fold increase in ATPase activity Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + Na+[side 1] + K+[side 2] Sus scrofa
-
 ADP + phosphate + Na+[side 2] + K+[side 1]
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Na+[side 1] + K+[side 2]
-
 Sus scrofa ADP + phosphate + Na+[side 2] + K+[side 1]
-
 ?
ATP + H2O + Na+[side 1] + Rb+[side 2]
-
 Sus scrofa ADP + phosphate + Na+[side 2] + Rb+[side 1]
-
 ?

Synonyms

Synonyms Comment Organism
Na+/K+-ATPase
-
 Sus scrofa