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Literature summary for 2.7.3.2 extracted from

  • Londergan, C.H.; Baskin, R.; Bischak, C.G.; Hoffman, K.W.; Snead, D.M.; Reynoso, C.
    Dynamic asymmetry and the role of the conserved active-site thiol in rabbit muscle creatine kinase (2015), Biochemistry, 54, 83-95.
    View publication on PubMed
Search for more literature for 2.7.3.2

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Oryctolagus cuniculus 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P00563
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle MM isoform Oryctolagus cuniculus
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms Comment Organism
CK MM
-
 Oryctolagus cuniculus
muscle creatine kinase
-
 Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ADP
-
 Oryctolagus cuniculus
ATP
-
 Oryctolagus cuniculus

General Information

General Information Comment Organism
additional information dual active-site cysteine 283 residues Oryctolagus cuniculus