KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.68 | - |
ATP | 25°C, euthermic squirrel | Urocitellus richardsonii | |
0.79 | - |
ATP | 25°C, myosin bound enzyme | Urocitellus richardsonii | |
1.18 | - |
ATP | 25°C, hibernating squirrel | Urocitellus richardsonii | |
1.2 | - |
Creatine | 25°C, myosin bound enzyme | Urocitellus richardsonii | |
1.62 | - |
Creatine | 25°C, euthermic squirrel | Urocitellus richardsonii | |
2.06 | - |
Creatine | 25°C, hibernating squirrel | Urocitellus richardsonii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
43000 | - |
x * 43000, SDS-PAGE | Urocitellus richardsonii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Urocitellus richardsonii | - |
creatine kinase activity and protein are 20% lower during hibernation than in euthermia, whereas enzyme mRNA is reduced by 70%. Hibernator creatine kinase shows reduced affinity for ATP and creatine. Soluble enzyme from euthermic squirrels is a mix of phosphorylated and dephosphorylated forms. in hibernating animals only phospho-enzyme is detected | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | soluble creatine kinase from euthermic squirrels is a mix of phosphorylated and dephosphorylated forms. In hibernating animals only phospho-enzyme is detected. High and low phosphate enzyme forms show different affinities for ATP and creatine substrates, but do not differ in stability to urea denaturation | Urocitellus richardsonii |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Urocitellus richardsonii | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + creatine | - |
Urocitellus richardsonii | ADP + creatine phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 43000, SDS-PAGE | Urocitellus richardsonii |