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2.7.3.2: creatine kinase

This is an abbreviated version!
For detailed information about creatine kinase, go to the full flat file.

Word Map on EC 2.7.3.2

Reaction

ATP
+
Creatine
=
ADP
 +
phosphocreatine

Synonyms

adenosine triphosphate-creatine transphosphorylase, adenosine-5'-triphosphate: creatine phosphotransferase, ATP-creatine transphosphorylase, ATP: creatine N-phosphotransferase, ATP:creatine phosphotransferase, B-type creatine kinase, BB-CK, BB-type creatine kinase, BCK, brain creatine kinase, brain type creatine kinase, brain-type CK, brain-type creatine kinase, CK, CK MM, CK-B, CK-BB, CK-MB, CK-MM, ckb, CKM, CKMB, CKMBI, CKMiMi, creatine kinase, creatine kinase B, creatine kinase M-type, creatine kinase MB, creatine kinase muscle type, creatine kinase-MB, creatine N-phosphotransferase, creatine phosphokinase, creatine phosphotransferase, creatinine kinase, creatinine kinase MB, hBBCK, hMMCK, kinase, creatine (phosphorylating), M-CK, M1-CK, MB-CK, MCK, Mi-CK, MiMi-CK, mit-CK, mitochondrial creatine kinase, MM-CK, MM-type creatine kinase, More, MtCK, muscle creatine kinase, muscle type creatine kinase, muscle-type creatine kinase, phosphocreatine kinase, plasma creatine kinase, PSCKM, recombinant human brain-type creatine kinase, rHBCK, RM-CK, s-type CK, sarcomeric CK, sMiCK, sMtCK, u-type CK, ubiquitous CK, ubiquitous MtCK, uMiCK, uMtCK, zMMCK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.3 Phosphotransferases with a nitrogenous group as acceptor
                2.7.3.2 creatine kinase

Renatured

Renatured on EC 2.7.3.2 - creatine kinase

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
dose- and time-dependent inhibition by cystine, cysteamine prevents and reverses this inhibition
-
enzyme, inactivated due to unfolding after treatment with lactic acid, refolds in presence of NaCl
-
freeze drying leads to rearrangement of isozyme CK-MB after dissociation of the subunits
-
inhibition of enzyme by sodium barbital may be reveresed by dilution
-
insoluble recombinant enzyme from Escherichia coli by 6 M urea, unfolding shows biphasic kinetic courses, aggregation during refolding follows first-order kinetics, refolding intermediates are stabilized by NaCl, refolded enzyme shows high specific activity
-
reactivation of 5,5'-dithiobis-(2-nitrobenzoic acid)-modified enzyme by excess of dithiothreitol, kinetics
-
reactivators are thiols, like N-acetylcysteine, beta-mercaptoethanol, dithiothreitol, monothioglycerol, glutathione
-
refolded in 50 mM Tris-HCl at pH 8.3 containing 500 mM NaCl and 5 mM dithiothreitol
study on enzyme aggregation and reassociation in presence of sodium dodecyl sulfate-cyclodextrin. Aggregation does not occur at concentrations below 0.002 mM or temperature below 17°C. Trapping of monomeric creatine kinase variants such as thiol residue modified enzyme, sodium dodecyl sulfate binding enzyme, cyclodextrin treated enzyme, or dithiothreitol treated enzyme. Reassociation in presence of sodium dodecly sulfate-cyclodextrin follows first-order kinetics
-
study on refolding of creatine kinase after denaturation with guanidine hydrochloride. Mixed macromolecular crowding agents, e.g. CT DNA and Ficoll 70, are more favorable and can reflect the physiological environment more accurately than single crowding agents
-