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 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Rattus norvegicus | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
skeletal muscle | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 3 Na+/in | - |
Rattus norvegicus | ADP + phosphate + 3 Na+/out | - |
? |
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 | 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 |