Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Oryctolagus cuniculus | 5829 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + creatine | Oryctolagus cuniculus | - |
ADP + phosphocreatine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | P00563 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
skeletal muscle | MM isoform | Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + creatine | - |
Oryctolagus cuniculus | ADP + phosphocreatine | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | dual active-site cysteine 283 residues, spectral observations localized at the active-site cysteines indicate an intrinsic, dynamic asymmetry between the two subunits that exists already in the apo form of the dimeric creatine kinase enzyme, rather than being induced by the substrate. Unmodified and Cys283-modified enzymes are investigated in the apo and transition state analogue forms of the enzyme. The narrow and invariant S-H vibrational bands report a homogeneous environment for the unmodified active-site cysteines, indicating that their thiols are hydrogen bonded to the same H-bond acceptor in the presence and absence of the substrate. The S-H peak persists at all physiologically relevant pH's, indicating that Cys283 is protonated at all pH's relevant to enzymatic activity. The S-H hydrogen bond acceptor is a single, long-resident water molecule and the role of the conserved yet catalytically unnecessary thiol may be to dynamically rigidify that part of the active site through specific H-bonding to water. The asymmetric and broad CN stretching bands from the CN-modified Cys283 suggest an asymmetric structure in the apo form of the enzyme in which there is a dynamic exchange between spectral subpopulations associated with water-exposed and water-excluded probe environments, homogeneous orientation of the SCN probe group in the active site. Molecular dynamics simulations, overview | Oryctolagus cuniculus |
Synonyms | Comment | Organism |
---|---|---|
CK MM | - |
Oryctolagus cuniculus |
muscle creatine kinase | - |
Oryctolagus cuniculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Oryctolagus cuniculus | |
ATP | - |
Oryctolagus cuniculus |
General Information | Comment | Organism |
---|---|---|
additional information | dual active-site cysteine 283 residues | Oryctolagus cuniculus |