Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.3.2 extracted from

  • Abnous, K.; Storey, K.B.
    Regulation of skeletal muscle creatine kinase from a hibernating mammal (2007), Arch. Biochem. Biophys., 467, 10-19.
    View publication on PubMed

KM Value [mM]

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 [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
x * 43000, SDS-PAGE Urocitellus richardsonii

Organism

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

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

Source Tissue Comment Organism Textmining
muscle
-
Urocitellus richardsonii
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + creatine
-
Urocitellus richardsonii ADP + creatine phosphate
-
?

Subunits

Subunits Comment Organism
? x * 43000, SDS-PAGE Urocitellus richardsonii