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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

General Stability

General Stability on EC 2.7.3.2 - creatine kinase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol enhances pH-stability
-
a His6-tag portion has no effect on the enzyme activity
dimeric enzyme stable to 1-2 M urea
-
in the presence of cryoprotectant (sucrose or trehalose), the activities of wild-type and mutant M1-CK enzymes with a hydrophobic residue at 268 are higher, and the effect is more profound at pH 8.0
in the presence of cryoprotectant (sucrose or trehalose), the activities of wild-type and mutant RM-CK enzymes with a hydrophobic residue at 268 are higher, and the effect is more profound at pH 8.0
isozyme CK-MM is more stable against unfolding by urea up to 3 M, while isozymes CK-BB and CK-MB unfold at lower urea concentrations of 2 M, at 25°C and pH 8.0
-
polyethylene glycol 2000 (PEG 2000) and dextran 70 are used as model crowding agents to examine the effects of macromolecular crowding on the inactivation of recombinant HBCK (rHBCK) during denaturation by GdnHCl. Both PEG 2000 and dextran 70 have a protective effect on the inactivation of rHBCK induced by GdnHCl at 25°C. The presence of PEG 2000 results in the retention of 35.33% of rHBCK activity after 4 h of inactivation, while no rHBCK activity is observed after denaturation in the absence of macromolecular crowding agents. The presence of PEG 2000 and dextran 70 at a concentration of 100 g/l can decelerate the k2 value of the slow track to 21 and 33%, respectively, in comparison to values obtained in the absence of crowding agents
-
sensitive to denaturation
-
the activity of the 3-(4-chloro-6-p-glyoxal-phenoxy-1,3,5-triazinylamino)-7-(dimethylamino)-2-methylphenazine-labeled creatine kinase is found to be about 40% of that of the native creatine kinase, which supports that the modified arginine residue by 3-(4-chloro-6-p-glyoxal-phenoxy-1,3,5-triazinylamino)-7-(dimethylamino)-2-methylphenazine is at the active site
-
when incubated with 0.8 M guanidine hydrochloride, MM-CK accumulates as a monomeric molten globule which totally lost its enzymatic activity