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Literature summary for 7.2.2.13 extracted from

  • Cortes, V.F.; Veiga-Lopes, F.E.; Barrabin, H.; Alves-Ferreira, M.; Fontes, C.F.
    The gamma subunit of Na+, K+-ATPase: role on ATPase activity and regulatory phosphorylation by PKA (2006), Int. J. Biochem. Cell Biol., 38, 1901-1913.
    View publication on PubMed
Search for more literature for 7.2.2.13

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information changes in alphabetagamma stoichiometry of Na+K+-ATPase do not alter Km1 value for ATP, and slightly increase km², but Vmax decreases at both catalytic and regulatory sites Sus scrofa
0.00151
-
 ATP Km1 value, plus gamma subunit, pH 7.4, 37°C Sus scrofa
0.00199
-
 ATP Km1 value, pH 7.4, 37°C Sus scrofa
0.242
-
 ATP Km2 value, pH 7.4, 37°C Sus scrofa
0.364
-
 ATP Km2 value, plus gamma subunit, pH 7.4, 37°C Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein 52% of the accumulating phosphorylated Na+K+-ATPase is not via acyl-phosphate formation. Gamma subunit is phosphorylated by endogenous kinases and by commercial catalytic subunit of protein kinase A. Phosphorylation of the gamma subunit increases its capacity to stimulate ATP hydrolysis Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney outer medulla Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Sus scrofa ADP + phosphate
-
 ?