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Literature summary extracted from

  • Tang, H.M.; Ou, W.B.; Zhou, H.M.
    Effects of lactic acid and NaCl on creatine kinase from rabbit muscle (2003), Biochem. Cell Biol., 81, 1-7.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.3.2 Lactic acid induces dissociation of enzyme dimer and unfolding of the enzyme at 0.8 mM, but no aggregation at 25°C or 40°C even at high protein concentrations, inactivation kinetics Oryctolagus cuniculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.3.2 Mg2+ at 5 mM MgCl2 Oryctolagus cuniculus
2.7.3.2 NaCl induces folding of the enzyme unfolded by lactic acid, formation of the molten globule conformation with a compact structure Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.3.2 ATP + creatine Oryctolagus cuniculus
-
ADP + phosphocreatine
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.7.3.2 Oryctolagus cuniculus
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.7.3.2 enzyme, inactivated due to unfolding after treatment with lactic acid, refolds in presence of NaCl Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.3.2 skeletal muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.3.2 ATP + creatine
-
Oryctolagus cuniculus ADP + phosphocreatine
-
r

Subunits

EC Number Subunits Comment Organism
2.7.3.2 dimer
-
Oryctolagus cuniculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.3.2 25
-
assay at Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.3.2 9
-
assay at Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.3.2 ATP
-
Oryctolagus cuniculus