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Literature summary for 2.7.3.2 extracted from

  • Takasawa, T.; Fukushi, K.; Shiokawa, H.
    Crystallization and properties of creatine kinase from equine skeletal muscle (1981), J. Biochem., 89, 1619-1631.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
4,4'-dithiodipyridine
-
Equus caballus
5,5'-dithiobis(2-nitrobenzoate)
-
Equus caballus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Equus caballus 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
2 * 44000, SDS-PAGE, presence of 2-mercaptoethanol, high speed sedimentation equilibrium centrifugation of urea-treated enzyme Equus caballus
76000 78000 gel filtration Equus caballus
84500
-
high speed and low speed sedimentation equilibrium centrifugation Equus caballus

Organism

Organism UniProt Comment Textmining
Equus caballus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle skeletal Equus caballus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Equus caballus

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 44000, SDS-PAGE, presence of 2-mercaptoethanol, high speed sedimentation equilibrium centrifugation of urea-treated enzyme Equus caballus