Literature summary extracted from
Awama, A.M.; Mazon, H.; Vial, C.; Marcillat, O.
Despite its high similarity with monomeric arginine kinase, muscle creatine kinase is only enzymatically active as a dimer (2007), Arch. Biochem. Biophys., 458, 158-166.
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.3.2 |
W210Y |
mutation in the interface of enzyme dimer, dissociates more readily than wild-type to monomer. Dissociation equilibrium constant is 9.7 nM compared to 0.017 nM for wild-type |
Oryctolagus cuniculus |
General Stability
EC Number |
General Stability |
Organism |
---|
2.7.3.2 |
when incubated with 0.8 M guanidine hydrochloride, MM-CK accumulates as a monomeric molten globule which totally lost its enzymatic activity |
Oryctolagus cuniculus |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.7.3.2 |
guanidine hydrochloride |
in the absence of added guanidine hydrochloride, MM-CK activity slightly decreases with NaCl concentration up to 4 M, but a dramatic decline is observed above that value, with full inactivation at 4.5 M. When guanidine is added, curves with similar shapes are obtained but NaCl concentrations needed to inactivate the enzyme are shifted towards lower values |
Oryctolagus cuniculus |
|
2.7.3.2 |
Guanidinium chloride |
inhibitory, in presence of NaCl, increased inhibitory activity. Inactivation by NaCl is due to dissociation of dimeric creatine kinase into its constitutive subunits, and upon monomerization, the protein becomes more susceptible to guanidinium denaturing effect |
Oryctolagus cuniculus |
|
2.7.3.2 |
NaCl |
enzyme activity slightly decreases with NaCl concentration up to 4 M, and a dramatic decline is observed above that value, with full inactivation at 4.5 M. In presence of guanidinium chloride, inactivation occurs much earlier. Inactivation by NaCl is due to dissociation of dimeric creatine kinase into its constitutive subunits, and upon monomerization, the protein becomes more susceptible to guanidinium denaturing effect; in the absence of added guanidine hydrochloride, MM-CK activity slightly decreases with NaCl concentration up to 4 M, but a dramatic decline is observed above that value, with full inactivation at 4.5 M. When guanidine is added, curves with similar shapes are obtained but NaCl concentrations needed to inactivate the enzyme are shifted towards lower values |
Oryctolagus cuniculus |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.3.2 |
Oryctolagus cuniculus |
P00563 |
- |
- |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
2.7.3.2 |
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 |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.7.3.2 |
dimer |
muscle creatine kinase is only enzymatically active as a dimer |
Oryctolagus cuniculus |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.3.2 |
MM-CK |
- |
Oryctolagus cuniculus |