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Literature summary 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

EC Number Inhibitors Comment Organism Structure
2.7.3.2 4,4'-dithiodipyridine
-
 Equus caballus
2.7.3.2 5,5'-dithiobis(2-nitrobenzoate)
-
 Equus caballus

Localization

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.3.2 44000
-
 2 * 44000, SDS-PAGE, presence of 2-mercaptoethanol, high speed sedimentation equilibrium centrifugation of urea-treated enzyme Equus caballus
2.7.3.2 76000 78000 gel filtration Equus caballus
2.7.3.2 84500
-
 high speed and low speed sedimentation equilibrium centrifugation Equus caballus

Organism

EC Number Organism UniProt Comment Textmining
2.7.3.2 Equus caballus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.3.2 muscle skeletal Equus caballus
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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