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Literature summary for 7.2.2.13 extracted from

  • Kristensen, M.; Juel, C.
    Na+,K+-ATPase Na+ affinity in rat skeletal muscle fiber types (2010), J. Membr. Biol., 234, 35-45.
    View publication on PubMed
Search for more literature for 7.2.2.13

Activating Compound

Activating Compound Comment Organism Structure
additional information The Na+-affinity is higher in oxidative muscle compared with glycolytic muscle and in purified membranes from oxidative muscle compared with glycolytic muscle Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4
-
 Na+/in alpha1beta1 heterodimer, 37°C, pH 7.4 Rattus norvegicus
5.5
-
 Na+/in alpha2beta1 heterodimer, 37°C, pH 7.4 Rattus norvegicus
7.5
-
 Na+/in alpha1beta2 heterodimer, 37°C, pH 7.4 Rattus norvegicus
13
-
 Na+/in alpha2beta2 heterodimer, 37°C, pH 7.4 Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Rattus norvegicus 16020
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3 Na+/in
-
 Rattus norvegicus ADP + phosphate + 3 Na+/out
-
 ?

Subunits

Subunits Comment Organism
More heterodimers containing the beta1 isoform have a higher N+-affinity than heterodimers containing the beta2 isoform. Dimers with alpha1 isoform are responsible for approximately 36% of the total Na+/K+ATPase activity. Heterodimers containing the alpha1 isoform have a higher Na+-affinity than heterodimers containing the alpha2 isoform Rattus norvegicus

General Information

General Information Comment Organism
physiological function the degree of activation of Na+/K+-ATPase at physiological Na+-concentrations differs between oxidative and glycolytic muscles and between subcellular membrane domains with different isoform compositions Rattus norvegicus