Information on EC 2.7.3.2 - creatine kinase

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The expected taxonomic range for this enzyme is: Metazoa

EC NUMBER
COMMENTARY
2.7.3.2
-
RECOMMENDED NAME
GeneOntology No.
creatine kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
; N-ethylglycocyamine can also act as acceptor
-
-
-
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
mitochondrial enzymes, mechanism, overview
-
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
enzyme is functionally coupled to ouabain-inhibited (Na+,K+)-ATPase
-
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
kinetic model of reaction
-
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
mechanism
-
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
random-order rapid-equilibrium mechanism
P00563
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
catalytic mechanism and substrate binding involving 2 flexible loops and a specificity pocket formed by Ile69 and Val325 determining substrate specificity, active site structure
-
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
bireactant catalytic mechanism, transition state stabilization by six arginines clustered in the active site of the enzyme
-
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
catalytic cysteine, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview
-
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
catalytic cysteine, active site residues are Glu226, Glu227, and Asp228, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview
P11009
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
catalytic cysteine, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview
-
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
catalytic cysteine, active site structure involving His66 and Asp326, overview, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
creatine-phosphate biosynthesis
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
ATP:creatine N-phosphotransferase
N-Ethylglycocyamine can also act as acceptor.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
adenosine triphosphate-creatine transphosphorylase
-
-
-
-
ATP: creatine N-phosphotransferase
-
-
ATP: creatine N-phosphotransferase
-
-
ATP:creatine phosphotransferase
-
-
-
-
BB-CK
-
-
-
-
BB-CK
-
brain-type cytosolic isoform of creatine kinase
BB-CK
P12277
-
BB-type creatine kinase
-
-
brain creatine kinase
-
-
brain creatine kinase
-
-
brain creatine kinase
-
-
brain type creatine kinase
-
-
brain-type creatine kinase
-
-
CK
-
-
-
-
CK-B
-
-
CK-BB
-
-
-
-
CK-BB
-
-
CK-MB
-
-
-
-
CK-MM
-
-
-
-
CKMiMi
-
-
-
-
creatine kinase
-
-
creatine kinase
-
-
creatine kinase
-
-
creatine kinase
Q7ZYQ9, Q8AVH2
-
creatine N-phosphotransferase
-
-
creatine phosphokinase
-
-
-
-
creatine phosphotransferase
-
-
-
-
creatinine kinase
-
-
hBBCK
-
-
kinase, creatine (phosphorylating)
-
-
-
-
MB-CK
-
-
-
-
Mi-CK
-
-
-
-
MiMi-CK
-
-
-
-
mit-CK
-
-
mitochondrial creatine kinase
-
-
mitochondrial creatine kinase
-
-
MM-CK
-
-
-
-
MM-CK
-
muscle form of creatine kinase
muscle creatine kinase
-
-
muscle creatine kinase
-
-
muscle-type creatine kinase
Q90X19
-
muscle-type creatine kinase
-
-
phosphocreatine kinase
-
-
-
-
plasma creatine kinase
-
-
recombinant human brain-type creatine kinase
-
-
rHBCK
-
-
sMiCK
-
-
uMiCK
P06732
-
zMMCK
Q90X19
-
MM-type creatine kinase
-
-
additional information
-
the enzyme is a member of the phosphagen (guanidino) kinase family
additional information
-
the enzyme is a member of the phosphagen kinase superfamily of enzymes
additional information
-
the enzyme is a member of the phosphagen (guanidino) kinase family
CAS REGISTRY NUMBER
COMMENTARY
9001-15-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
4 isozymes encoded by 4 different genes: 2 cytosolic isozymes, a muscle-type MM-CK and a brain-type BB-CK or a heterodimer MB-CK, and 2 mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
two isoforms, interconversion by reversible oxidation of protein sulfhydryl groups
-
-
Manually annotated by BRENDA team
Antarctic icefish
-
-
Manually annotated by BRENDA team
polychaete worm
-
-
Manually annotated by BRENDA team
2 cytosolic and a mitochondrial isozymes
-
-
Manually annotated by BRENDA team
herring
-
-
Manually annotated by BRENDA team
isoforms CK1, CK2
-
-
Manually annotated by BRENDA team
pigeon
-
-
Manually annotated by BRENDA team
mirror carp, three isoforms
-
-
Manually annotated by BRENDA team
recombinant cytoplasmic isoforms M1, M2, and B
-
-
Manually annotated by BRENDA team
zebrafish
-
-
Manually annotated by BRENDA team
recombinant mitochondrial isoform
-
-
Manually annotated by BRENDA team
tropical fruit bat
-
-
Manually annotated by BRENDA team
Frog
-
-
-
Manually annotated by BRENDA team
atlantic cod
-
-
Manually annotated by BRENDA team
4 isozymes encoded by 4 different genes: 2 cytosolic isozymes, a muscle-type MM-CK and a brain-type BB-CK or a heterodimer MB-CK, and 2 mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK
Uniprot
Manually annotated by BRENDA team
nurse shark
-
-
Manually annotated by BRENDA team
recombinant cytoplasmic and mitochondrial isoforms
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
2 typical mitochondrial enzyme types, the sarcomeric and the ubiquitous, encoded by 2 different genes
-
-
Manually annotated by BRENDA team
4 isozymes encoded by 4 different genes: 2 cytosolic isozymes, a muscle-type MM-CK and a brain-type BB-CK or a heterodimer MB-CK, and 2 mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK
-
-
Manually annotated by BRENDA team
acute myocardial infarction patient
-
-
Manually annotated by BRENDA team
computational approach to study the contribution of side chain residues to the very low pKa value of active site cysteine
Uniprot
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
patients with Alzheimers disease
-
-
Manually annotated by BRENDA team
three isoforms
-
-
Manually annotated by BRENDA team
green sunfish
-
-
Manually annotated by BRENDA team
recombinant cytoplasmic isoforms M1, M2, and B
-
-
Manually annotated by BRENDA team
recombinant cytoplasmic isoforms M, B and mitochondrial isoform
-
-
Manually annotated by BRENDA team
rainbow trout
-
-
Manually annotated by BRENDA team
4 isozymes encoded by 4 different genes: 2 cytosolic isozymes, a muscle-type MM-CK and a brain-type BB-CK or a heterodimer MB-CK, and 2 mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK
-
-
Manually annotated by BRENDA team
commercial preparation
Uniprot
Manually annotated by BRENDA team
cytosolic isozyme
Uniprot
Manually annotated by BRENDA team
isozymes CK-MM, CK-BB, and CK-MB
-
-
Manually annotated by BRENDA team
red sea bream
-
-
Manually annotated by BRENDA team
monkey
-
-
Manually annotated by BRENDA team
21-day-old Wistar rats
-
-
Manually annotated by BRENDA team
treatment with single injection or for one week with daily injection of saline or L-Arg plus Nomega-nitro-L-arginine methyl ester or alpha-tocopherol plus ascorbic acid
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
Wistar
-
-
Manually annotated by BRENDA team
pacific mackerel
-
-
Manually annotated by BRENDA team
sea urchin, two isoforms
-
-
Manually annotated by BRENDA team
syn. Pseudemys scripta elegans, freshwater turtle
-
-
Manually annotated by BRENDA team
trout
-
-
-
Manually annotated by BRENDA team
creatine kinase activity and protein are 20% lower during hibernation than in euthermia, whereas enzyme mRNA is reduced by 70%. Hibernator creatine kinase shows reduced affinity for ATP and creatine. Soluble enzyme from euthermic squirrels is a mix of phosphorylated and dephosphorylated forms. in hibernating animals only phospho-enzyme is detected
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
complete brain-type creatine kinase deficiency in mice blocks seizure activity and affects intracellular calcium kinetics
malfunction
-
absence of creatine kinase in muscle cells leads to morphological and functional adaptations towards preservation of muscle contractile abilities
malfunction
-
oxygen consumption dynamics during electrical stimulation in superfused fast-twitch hindlimb muscles isolated from wild-type and transgenic mice deficient in the myoplasmic and mitochondrial creatine isoforms (MiM CK-/-), respectively. Transgenic mice deficient in the mitochondrial creatinine isoforms (MiM CK-/-) show muscle oxygen consumption activation kinetics 30% faster than wild-type. MiM CK-/- muscle oxygen consumption deactivation kinetics are 380% faster than wild-type
physiological function
-
cerebral ischemia is accompanied by opposite changes in activities of mitochondrial creatine kinase (mCK) and cytoplasmic creatine kinase (cCK). Catalytic properties of mCK depend on the functional interaction with mitochondrial membranes. Acute ischemia impairs enzyme interaction with the mitochondrial membrane. These changes manifest in activation of mCK and change in the dimer/octamer ratio toward the formation of octamer. Mitochondrial creatine kinase gains new properties under conditions of oxygen eficiency in nerve cells
physiological function
-
sarcomeric mitochondrial creatine kinase (sMiCK) interacts with NCX1IL (sodium-calcium exchanger). In addition to sMiCK, cytoplasmic muscle-type creatine kinase (CKM) is also able to interact with NCX1 in mammalian cells. Sarcomeric mitochondrial creatine kinase (sMiCK) and cytoplasmic muscle-type CK (CKM) are able to produce a recovery in the decreased NCX1 activity that is lost under energy-compromised conditions
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
-
synergistic substrate binding, mitochondrial isoform sMiCK, synergistic substrate binding, muscle-type isoform MCK
-
-
?
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
?
alpha-(RP)-borano-ADP + phosphocreatine
alpha-(RP)-borano-ATP + creatine
show the reaction diagram
-
the SP-ADPalphaB isomer is a 70fold better substrate for creatine kinase than the RP isomer
-
-
?
alpha-(SP)-borano-ADP + phosphocreatine
alpha-(SP)-borano-ATP + creatine
show the reaction diagram
-
the SP-ADPalphaB isomer is a 70fold better substrate for creatine kinase than the RP isomer
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
-
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
-
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
-
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
-
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
-
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
-
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
-
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
Q90X19
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
ATP required as MgATP2-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
ATP required as MgATP2-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
ATP required as MgATP2-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
ATP required as MgATP2-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
ATP required as MgATP2-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
ATP required as MgATP2-
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
ATP required as MgATP2-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
ATP required as MgATP2-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
ATP required as MgATP2-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
ATP required as MgATP2-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
ATP required as MgATP2-
in the reverse direction ADP can be replaced by IDP with 18% efficiency, ADP cannot be replaced by GDP, CDP, UDP, dTDP
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
creatine cannot be replaced by creatinine
-
-
r
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
Mg-complexes of ATP and ADP are the true substrates for the mitochondrial enzymes
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
P11009
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
P12277
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
P00563
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
-
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
role in anaerobic metabolism
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
regeneration of ATP as primary energy source
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
mitochondrial model of CK in energy transport
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
coupled to (Na+,K+)ATPase system
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
physiological roles: 1. buffering of ADP/ATP ratio, 2. transport of high-energy phosphates from sites of ATP production to sites of ATP consumption
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
overview on physiological roles
-
-
-
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
evolution of enzyme, phylogenetics
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
P11009
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
key enzyme of energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
the enzyme is involved in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
the reaction equilibrium lies towards ATP production
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
the brain-type cytosolic isoform of creatine kinase, which is found mainly in the brain and retina, is a key enzyme in brain energy metabolism, because high-energy phosphates are transfered through the creatine kinase/phosphocreatine shuttle system
-
-
?
ATP + cyclocreatine
ADP + phospho-cyclocreatine
show the reaction diagram
-
i.e. 1-carboxymethy-2-iminoimidazolidine
-
-
?
ATP + cyclocreatine
ADP + phospho-cyclocreatine
show the reaction diagram
P12277
i.e. 1-carboxymethyl-2-iminoimidazolidine
-
-
?
ATP + cyclocreatine
ADP + phospho-cyclocreatine
show the reaction diagram
-
i.e. 1-carboxymethyl-2-iminoimidazolidine
-
-
?
ATP + glycocyamine
ADP + glycocyamine phosphate
show the reaction diagram
P12277
very low activity
-
-
?
ATP + glycocyamine
ADP + glycocyamine phosphate
show the reaction diagram
-
very low activity
-
-
?
ATP + N-ethylglycocyamine
ADP + N-ethylglycocyamine phosphate
show the reaction diagram
P12277
-
-
-
?
ATP + N-ethylglycocyamine
ADP + N-ethylglycocyamine phosphate
show the reaction diagram
-
-
-
-
?
dADP + phosphocreatine
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
ATP undergoes substrate channelling between enzyme and myosin ATPase
-
-
-
additional information
?
-
-
enzyme inhibition, e.g. by branched chain alpha-amino acids, might contribute to the brain damage maple syrup urine disease MSUD
-
-
-
additional information
?
-
P11009
probable enzyme evolution, overview
-
-
-
additional information
?
-
-
probable enzyme evolution, overview
-
-
-
additional information
?
-
-
substrate binding structure, arginine residues R130, R132, R236, R292, and R320 form a nucleotide phosphate bindig pocket, reaction equilibrium is highly influenced by pH and Mg2+ concentration, substrate specificity of isozymes
-
-
-
additional information
?
-
-
substrate binding structure, reaction equilibrium is highly influenced by pH and Mg2+ concentration, assay methods, overview, structure-function analysis, substrate specificity of isozymes, the cytosolic isozymes of skeletal muscle shows broad substrate specificity
-
-
-
additional information
?
-
P11009
substrate binding structure, reaction equilibrium is highly influenced by pH and Mg2+ concentration, substrate specificity of isozymes
-
-
-
additional information
?
-
-
substrate binding structure, reaction equilibrium is highly influenced by pH and Mg2+ concentration, substrate specificity of isozymes
-
-
-
additional information
?
-
-
substrate binding structure, substrate binding at both subunits
-
-
-
additional information
?
-
-
ADP re-cycling accomplished by mitochondrial creatine kinase regulates reactive oxygen species generation, particularly in high glucose concentrations. Key role of enzyme as a preventive antioxidant against oxidative stress
-
-
-
additional information
?
-
-
using a yeast two-hybrid screening to search for molecules that interact with NCX1 (sodium-calcium exchanger) it is shown that sarcomeric mitochondrial creatine kinase (sMiCK) interacts with NCX1IL. In addition to sMiCK, cytoplasmic muscle-type CK (CKM) is also able to interact with NCX1 in mammalian cells
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
Q90X19
-
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
P12277
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
P00563
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
role in anaerobic metabolism
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
regeneration of ATP as primary energy source
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
mitochondrial model of CK in energy transport
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
coupled to (Na+,K+)ATPase system
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
physiological roles: 1. buffering of ADP/ATP ratio, 2. transport of high-energy phosphates from sites of ATP production to sites of ATP consumption
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
overview on physiological roles
-
-
-
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
evolution of enzyme, phylogenetics
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
P11009
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
key enzyme of energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
-
the enzyme is involved in energy homeostasis
-
-
r
additional information
?
-
-
enzyme inhibition, e.g. by branched chain alpha-amino acids, might contribute to the brain damage maple syrup urine disease MSUD
-
-
-
additional information
?
-
P11009
probable enzyme evolution, overview
-
-
-
additional information
?
-
-
probable enzyme evolution, overview
-
-
-
additional information
?
-
-
ADP re-cycling accomplished by mitochondrial creatine kinase regulates reactive oxygen species generation, particularly in high glucose concentrations. Key role of enzyme as a preventive antioxidant against oxidative stress
-
-
-
additional information
?
-
-
using a yeast two-hybrid screening to search for molecules that interact with NCX1 (sodium-calcium exchanger) it is shown that sarcomeric mitochondrial creatine kinase (sMiCK) interacts with NCX1IL. In addition to sMiCK, cytoplasmic muscle-type CK (CKM) is also able to interact with NCX1 in mammalian cells
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
can substitute for Mg2+
Mg2+
-
required as MgATP
Mg2+
-
required as MgATP
Mg2+
-
required as MgATP; required, regulatory effect of Mg2+-concentration
Mg2+
-
required as MgATP
Mg2+
-
at 5 mM MgCl2
Mg2+
-
MgATP2- or MgADP- protect the enzyme from inactivation by 4-hydroxy-3-nitrophenylglyoxal or 2,3-butadiene
Mg2+
-
MgATP2-, at 1 mM, dissociation constants of wild-type and mutant enzymes
Mg2+
-
-
Mg2+
P11009
-
Mn2+
-
required
NaCl
-
induces folding of the enzyme unfolded by lactic acid, formation of the molten globule conformation with a compact structure
NaCl
-
prevents aggregation of the enzyme during recombinant expression in Escherichia coli
Zn2+
-
can substitute for Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-anilinonaphthalene-8-sulfonate
P00563
unfolding agent
2,3-butadiene
-
complete inhibition, MgATP2- or MgADP- protect the enzyme from inactivation
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
organotellurium inhibits creatine kinase activity by two different mechanisms: competition with ADP and oxidation of critical sulfhydryl groups for the functioning of the enzyme
-
4,4'-dithiodipyridine
-
-
4-hydroxy-2-nonenal
-
dose-dependent inhibition of creatine kinase, inhibition correlates with 4-hydroxy-2-nonenal adduct formation on specific amino acid residues including the active site residues H66, H191, C283, and H296
4-hydroxy-3-nitrophenylglyoxal
-
complete inactivation, modification of 2 arginine residues per enzyme subunit, inhibition kinetics at pH 8.7, MgATP2- or MgADP- protect the enzyme from inactivation
4-hydroxymercuribenzoic acid
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5-(4-([(benzoylphenyl)amino]carbonyl)phenyl)-2-furoic acid
-
35% inhibition, docking energy -49.5 kcal/mol
5-(4-([(biphenyl-4-ylmethyl)amino]carbony)phenyl)-2-furoic acid
-
63% inhibition, docking energy -51.8 kcal/mol
5-(4-benzoylbiphenyl-4-yl)-2-furoic acid
-
; 63% inhibition, docking energy -46.3 kcal/mol
5-(4-[(benzylamino)carbonyl]phenyl)-2-furoic acid
-
20% inhibition, docking energy -47.4 kcal/mol
5-(4-[[(benzoylphenyl)amino]carbonyl]phenyl)-2-furoic acid
-
-
5-(4-[[(biphenyl-4-ylmethyl)amino]carbony]phenyl)-2-furoic acid
-
-
5-[4-[(benzylamino)carbonyl]phenyl]-2-furoic acid
-
-
acetaminophen
-
inhibits creatine kinase in cerebellum and hippocampus, the administration of N-acetylcysteine plus deferoxamine reverses the inhibition of creatine kinase activity
Acrylamide
-
significantly inactivate screatine kinase and glutathione S-transferase and deplete glutathione. When the dietary constituents, tea polyphenols, resveratrol, and diallyl trisulfide are cotreated with acrylamide, all of them can effectively recover the activities of creatine kinase
Acrylamide
-
CK-BB is kinetically reversibly inactivated by acrylamide accompanied by the disruption of the hydrophobic surface, complete inhibition at 800 mM
alpha-P-borano substituted ADP Sp isomer
-
strong competitive inhibitor
Bovine serum albumin
-
no influence on enzyme activity
-
carbon tetrachloride
-
inhibits creatine kinase activity in cerebellum, the administration of N-acetylcysteine plus deferoxamine reverses the inhibition of creatine kinase activity
Chromium ADP
-
competitive to MgADP-
Chromium ATP
-
competitive to MgATP2-
-
Cl-
-
inactivation at -17C
clozapine
-
inhibition of enzyme in cerebellum and prefrontal cortex after chronic administration
copper metabolism gene MURR1 domain 6
-
0.006 mg is capable of inhibiting the activities of both the MM- and BB-type creatine kinases
-
Creatinine phosphate
-
competitive to phosphocreatine
Creatinine phosphate
-
competitive to MgATP2-
cystine
-
cystine inhibited the enzyme activity in a dose- and time-dependent manner and cysteamine prevents and reverses the inhibition caused by cystine, suggesting that cystine inhibits creatine kinase activity by oxidation of the sulfhydryl groups of the enzyme; dose- and time-dependent inhibition, cysteamine prevents and reverses this inhibition
cystine
-
inhibits creatine kinase activity possibly by oxidation of the sulfhydryl groups of the enzyme. Considering that creatine kinase like other thiol-containing enzymes, is crucial for energy homeostasis and antioxidant defenses, the enzymes inhibition caused by cystine released from lysosomes could be one of the mechanisms of tissue damage in patients with cystinosis
cystine dimethylester
-
-
ethylmalonic acid
-
accumulation in patients affected by short-chain acyl-CoA dehydrogenase deficiency and other diseases. Ethylmalonic acid inhibits the activity of respiratory chain complexes and also inhibits creatine kinase at concentrations o 1 mM and 5 mM
Fe3+
-
-
-
formate
-
mimics the phosphoryl group in the transition state
formate
P11009
mimics the phosphoryl group in the transition state
formate
-
mimics the phosphoryl group in the transition state
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
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
guanidinium hydrochloride
P00563
inactivation mechanism of wild-type and mutant enzymes, overview
guanidinium hydrochloride
-
first dissociation of subunits, then unfolding into random coil
Guanidinoacetate
-
vitamins E and C prevent the effects of intrastriatal administration of guanidinoacetate on the inhibition of creatine kinase
imidazole
-
-
iodoacetamide
-
protection by MgATP2-, MgADP-, urea
iodoacetamide
-
substrates can protect against alkylation
iodoacetamide
P11009
substrates can protect against alkylation
iodoacetamide
-
substrates can protect against alkylation
iodoacetamide
-
70.9% inhibition of the atypical ubiquitous mitochondrial enzyme, 74.6% inhibition of the typical ubiquitous mitochondrial enzyme
iodoacetamide
-
-
iodoacetic acid
-
-
L-arginine
-
treatment with single injection or for one week with daily injection of saline or L-Arg plus Nomega-nitro-L-arginine methyl ester or alpha-tocopherol plus ascorbic acid. Total and cytosolic creatine kinase activities are significantly inhibitied by L-arginine adminstration, mitochondrial enzyme activity is not affected. simultaneous injection of Nomega-nitro-L-arginine methyl ester and alpha-tocopherol plus ascorbic acid prevent inhibition
L-isoleucine
-
branched chain alpha-amino acids bind at the active site, competitive inhibition mechanism against substrates phosphocreatine and ADP, inhibition kinetics
L-leucine
-
branched chain alpha-amino acids bind at the active site, competitive inhibition mechanism against substrates phosphocreatine and ADP, inhibition kinetics
L-lysine
-
total and cytosolic creatine kinase activities are significantly inhibited by L-lysine, in contrast to the mitochondrial isoform which is not affected, the inhibitory effect of L-lysine on total creatine kinase activity is totally prevented by reduced glutathione
L-valine
-
branched chain alpha-amino acids bind at the active site, competitive inhibition mechanism against substrates phosphocreatine and ADP, inhibition kinetics
Lactic acid
-
induces dissociation of enzyme dimer and unfolding of the enzyme at 0.8 mM, but no aggregation at 25C or 40C even at high protein concentrations, inactivation kinetics
LiCl
-
inactivation due to subunit dissociation, mechanism
N-ethylmaleimide
-
-
NaCl
-
inactivation due to subunit dissociation, mechanism
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
nitrate
-
mimics the phosphoryl group in the transition state
-
nitrate
P11009
mimics the phosphoryl group in the transition state
-
nitrate
-
mimics the phosphoryl group in the transition state
-
nitrite
-
mimics the phosphoryl group in the transition state
nitrite
P11009
mimics the phosphoryl group in the transition state
nitrite
-
mimics the phosphoryl group in the transition state
NO3-
-
inactivation at -17C
p-hydroxymercuribenzoate
-
-
Pb2+
-
lead inhibits in vitro the cytosolic and mitochondrial creatine kinase activity at 0.2 mM and that this inhibition is prevented by addition cysteamine to the assay at 0.1 mM and 0.5 mM final concentration
Phenylglyoxal
-
complete inactivation, reacts on arginine residues
phosphate
-
competitive against ATP and phosphocreatine, noncompetitive against ADP and creatine
Pipes buffer
-
i.e. 1,4-piperazine diethanesulfonic acid
quercetin
-
mechanism, role of radicals
SDS
-
dissociation of subunits, no unfolding
SDS
-
strongly inhibits the CK-BB activity in a noncompetitive manner, although almost all the activity is eliminated by SDS CK-BB is never completely inactivated (4% to 5% activity is still sustained), regardless of increased incubation time or SDS concentration
sodium barbital
-
slow inactivation of enzyme that can be reversed by dilution. Sodium barbital may compete mainly with creatine, but also with ATP, for inhibition
sulfate
-
competitive against ATP and phosphocreatine, noncompetitive against ADP and creatine
trans-[RuCl2(3-pyridinecarboxylic acid)4]
-
administration at 180.7 micromol/kg, inhibition of creatine kinase activity in hippocampus, striatum, cerebral cortex, heart and skeletal muscle. No effect on enzyme in vitro
transition state analogue complex
-
consists of creatine, MgADP, and planar ions such as nitrate, nitrite, and formate, binding structure
-
transition state analogue complex
-
creatine, MgADP-, and planar ions such as nitrate, nitrite, and formate
-
Zn2+
-
Zn2+ may induce CK-BB inactivation and misfolding, when the Zn2+ concentration is 0.4 mM, CK-BB activity is completely abolished
MOPS buffer
-
i.e. 3-(N-morpholino)propane sulfonate
additional information
-
haloperidol, no effect on enzyme. Aripiprazole, no effect on enzyme in hippocampus, cerebellum and prefrontal cortex
-
additional information
-
no effect: trans-[RuCl2(4-pyridinecarboxylic acid)4]
-
additional information
-
cysteamine, glutathione, and sodium acetate does not affect cytosolic and mitochondrial creatine kinase activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
-
activation of creatine kinase and induction of a state 3-like respiration in isolated brain mitochondria, and prevention of H2O2 production obeys the steady-state kinetics of the enzyme to phosphorylate creatine
aripiprazole
-
activation of enzyme in striatum and cerebral cortex after chronic administration at 10 or 20 mg/kg. No effect on enzyme in hippocampus, cerebellum and prefrontal cortex
ATP
-
activation of creatine kinase and induction of a state 3-like respiration in isolated brain mitochondria, and prevention of H2O2 production obeys the steady-state kinetics of the enzyme to phosphorylate creatine
NADH
-
lowers Km for phosphocreatine 3fold
olanzapine
-
activation of enzyme in striatum after chronic administration at 10 mg/kg
trans-[RuCl2(3,4-pyridinedicarboxylic acid)4]
-
administration at 180.7 micromol/kg, increase of creatine kinase activity in hippocampus, striatum, cerebral cortex and heart, but not in skeletal muscle. No effect on enzyme in vitro
trans-[RuCl2(3,5-pyridinedicarboxylic acid)4]
-
administration at 180.7 micromol/kg, increase of creatine kinase activity in hippocampus, striatum, cerebral cortex and heart, but not in skeletal muscle. No effect on enzyme in vitro
Creatine
-
activation of creatine kinase and induction of a state 3-like respiration in isolated brain mitochondria, and prevention of H2O2 production obeys the steady-state kinetics of the enzyme to phosphorylate creatine
additional information
-
increase of enzymatic activity post-exercise
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.027
-
ADP
-
30C
0.03
-
ADP
-
pH 7.0, muscle-type cytosolic isozyme
0.04
-
ADP
-
pH 7.0, brain-type cytosolic isozyme
0.047
-
ADP
-
-
0.06
-
ADP
-
0.5C, pH 7.6
0.13
-
ADP
-
pH 7.0, ubiquitous mitochondrial isozyme
0.15
-
ADP
-
pH 7.0, ubiquitous mitochondrial isozyme
0.3
-
ADP
-
pH 7.5, 37C
1
-
alpha-(RP)-borano substituted ADP
-
-
0.008
-
alpha-(SP)-borano substituted ADP
-
-
0.11
-
ATP
-
25C, pH 8.0, ubiquitous mitochondrial isoform
0.11
-
ATP
-
pH 8.0, ubiquitous mitochondrial isozyme
0.2
-
ATP
-
cytoplasmic isoform M1, 25C
0.27
-
ATP
-
mutant L115D
0.3
-
ATP
-
hybrid form consisting of muscle and brain creatine kinase isoforms, pH and temperature not specified in the publication
0.31
-
ATP
-
mitochondrial isoform, 25C
0.33
-
ATP
-
mutant L110D
0.34
-
ATP
-
isoform III isolated after expression in Escherichia coli, pH 8.0, 30C
0.35
-
ATP
-
mutant L121D
0.35
-
ATP
-
wild-type hBBCK, pH and temperature not specified in the publication
0.36
-
ATP
-
isoform II isolated after expression in Escherichia coli, pH 8.0, 30C
0.36
-
ATP
Q90X19
25C, pH not specified in the publication, mutant T304K
0.37
-
ATP
-
reduced form of creatine kinase
0.38
-
ATP
-
wild-type containing both oxidized and reduced form
0.4
-
ATP
-
wild-type
0.4
-
ATP
-
wild-type and isoform I isolated after expression in Escherichia coli, pH 8.0, 30C
0.41
-
ATP
-
wild-type
0.42
-
ATP
Q90X19
25C, pH not specified in the publication, mutant S329A
0.43
-
ATP
-
mutant C74A, 25C
0.43
-
ATP
-
isoform IV isolated after expression in Escherichia coli, pH 8.0, 30C
0.43
-
ATP
-
oxidized form of creatine kinase
0.44
-
ATP
-
wild-type hMMCK, pH and temperature not specified in the publication
0.45
-
ATP
-
wild-type, 25C
0.45
-
ATP
Q90X19
25C, pH not specified in the publication, mutant N146C
0.46
-
ATP
-
mutant A76G, 25C
0.46
-
ATP
-
wild-type; wild-type enzyme
0.47
-
ATP
-
mutant C74S, 25C
0.49
-
ATP
Q90X19
25C, pH not specified in the publication, wild-type
0.51
-
ATP
-
mutant V72A, 25C
0.57
-
ATP
-
mutant V75A, 25C
0.58
-
ATP
Q90X19
25C, pH not specified in the publication, mutant A205S; 25C, pH not specified in the publication, mutant Q46E
0.62
-
ATP
Q90X19
25C, pH not specified in the publication, mutant H267A
0.62
-
ATP
-
25C, pH not specified in the publication, wild-type
0.65
-
ATP
-
cytoplasmic isoform B, 25C
0.65
-
ATP
-
25C, pH not specified in the publication, mutant S205A
0.66
-
ATP
-
mutant C74M, 25C
0.68
-
ATP
-
25C, pH 8.0, sarcomeric mitochondrial isoform
0.68
-
ATP
-
pH 8.0, ubiquitous mitochondrial isozyme
0.68
-
ATP
-
25C, euthermic squirrel
0.68
-
ATP
-
mutant G73A, 25C
0.7
-
ATP
-
mutant C74L, 25C
0.7
-
ATP
-
cytoplasmic isoform M1, 25C
0.73
-
ATP
-
fusion protein CK-AK
0.73
-
ATP
-
25C, pH not specified in the publication, mutant A267H
0.74
-
ATP
-
25C, pH not specified in the publication, mutant K304T; 25C, pH not specified in the publication, mutant L36K
0.75
-
ATP
-
cytoplasmic isoform M, 25C
0.79
-
ATP
-
25C, myosin bound enzyme
0.8
-
ATP
-
cytoplasmic isoform M2, 25C
0.8
-
ATP
-
cytoplasmic isoform M1, 25C
0.81
-
ATP
-
pH 9.0, brain-type cytosolic isozyme
0.82
-
ATP
Q90X19
25C, pH not specified in the publication, mutant A189D
0.84
-
ATP
-
25C, pH not specified in the publication, mutant D189A
0.85
-
ATP
Q90X19
25C, pH not specified in the publication, mutant K36L
0.86
-
ATP
-
fusion protein AK-CK
0.89
-
ATP
-
pH 9.0, muscle-type cytosolic isozyme
0.9
-
ATP
-
mitochondrial isoform M2, 25C
0.91
-
ATP
-
25C, pH not specified in the publication, mutant C146N
0.92
-
ATP
Q90X19
25C, pH not specified in the publication, mutant E185Q
1
-
ATP
-
cytoplasmic isoform B, 25C
1
-
ATP
-
cytoplasmic isoform M2, 25C
1.09
-
ATP
-
25C, pH not specified in the publication, mutant E46Q
1.18
-
ATP
-
25C, hibernating squirrel
1.24
-
ATP
-
25C, pH not specified in the publication, mutant Q185E
1.35
-
ATP
-
mitochondrial isoform M2, 25C
1.37
-
ATP
-
0.020 mM organotellurium, preincubation time 5 min, mitochondrial fraction, pH 7.5, 37C
1.38
-
ATP
-
0.005 mM organotellurium, preincubation time 5 min, mitochondrial fraction, pH 7.5, 37C
1.38
-
ATP
-
25C, pH not specified in the publication, mutant A329S
1.75
-
ATP
-
no organotellurium, preincubation time 30 min, cytosolic fraction, pH 7.5, 37C
1.94
-
ATP
-
0.005 mM organotellurium, preincubation time 30 min, mitochondrial fraction, pH 7.5, 37C
2.03
-
ATP
-
0.020 mM organotellurium, preincubation time 30 min, cytosolic fraction, pH 7.5, 37C
2.1
-
ATP
-
0.005 mM organotellurium, preincubation time 30 min, cytosolic fraction, pH 7.5, 37C; no organotellurium, preincubation time 5 min, mitochondrial fraction, including reduced glutathione (GSH), pH 7.5, 37C
2.2
-
ATP
-
mutant D54G; mutant enzyme D54G
2.49
-
ATP
-
0.020 mM organotellurium, preincubation time 30 min, mitochondrial fraction, pH 7.5, 37C
2.82
-
ATP
-
no organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37C
2.84
-
ATP
-
0.005 mM organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37C
3.15
-
ATP
-
no organotellurium, preincubation time 30 min, mitochondrial fraction, pH 7.5, 37C
3.19
-
ATP
-
no organotellurium, preincubation time 5 min, cytosolic fraction, including reduced glutathione (GSH), pH 7.5, 37C
3.55
-
ATP
-
no organotellurium, preincubation time 5 min, mitochondrial fraction, pH 7.5, 37C
3.92
-
ATP
-
0.020 mM organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37C
5.3
6
ATP
-
0.005 mM organotellurium, preincubation time 5 min, mitochondrial fraction, including reduced glutathione (GSH), pH 7.5, 37C
6.68
-
ATP
-
0.005 mM organotellurium, preincubation time 5 min, cytosolic fraction, including reduced glutathione (GSH), pH 7.5, 37C
9.38
-
ATP
-
mitochondrial isoform sMiCK
17.52
-
ATP
-
0.020 mM organotellurium, preincubation time 5 min, cytosolic fraction, including reduced glutathione (GSH), pH 7.5, 37C
20
-
ATP
-
0.020 mM organotellurium, preincubation time 5 min, mitochondrial fraction, including reduced glutathione (GSH), pH 7.5, 37C
0.35
-
Creatine
-
mitochondrial isoform, 25C
0.69
-
Creatine
-
37C, atypical ubiquitous mitochondrial enzyme
0.74
-
Creatine
-
37C, typical ubiquitous mitochondrial enzyme
1.01
-
Creatine
-
25C, pH 8.0, ubiquitous mitochondrial isoform
1.01
-
Creatine
-
pH 8.0, ubiquitous mitochondrial isozyme
1.2
-
Creatine
-
25C, myosin bound enzyme
1.5
-
Creatine
-
cytoplasmic isoform B, 25C
1.62
-
Creatine
-
25C, euthermic squirrel
2
3
Creatine
-
isoform I isolated after expression in Escherichia coli, pH 8.0, 30C
2
3.4
Creatine
-
25C, pH not specified in the publication, mutant A329S
2.06
-
Creatine
-
25C, hibernating squirrel
2.5
-
Creatine
-
soluble enzyme from muscle
2.7
-
Creatine
-
cytoplasmic isoform B, 25C
2.8
-
Creatine
-
mutant L110D
3.1
-
Creatine
-
mutant L115D
3.26
-
Creatine
-
enzyme from embryonic stem cell-derived cardiomyocytes, pH 6.5, 37C
3.4
-
Creatine
-
pH 7.4, dimeric form
3.6
-
Creatine
-
mutant L121D
3.9
-
Creatine
-
wild-type hBBCK, pH and temperature not specified in the publication
4.3
-
Creatine
-
mitochondrial isoform sMiCK
4.5
-
Creatine
-
30C
4.7
-
Creatine
-
cytoplasmic isoform M, 25C
4.9
5
Creatine
-
30C, pH 7.4
4.9
-
Creatine
-
pH 9.0, brain-type cytosolic isozyme
5
-
Creatine
-
hybrid form consisting of muscle and brain creatine kinase isoforms, pH and temperature not specified in the publication
5.67
-
Creatine
-
enzyme from neonatal cardiomyocytes, pH 6.5, 37C
5.9
-
Creatine
-
25C, pH not specified in the publication, wild-type
6.2
-
Creatine
-
wild-type hMMCK, pH and temperature not specified in the publication
6.4
-
Creatine
-
wild-type
6.6
-
Creatine
-
25C, pH not specified in the publication, mutant S205A
7.1
-
Creatine
-
25C, pH not specified in the publication, mutant L36K
7.31
-
Creatine
-
25C, pH 8.0, sarcomeric mitochondrial isoform
7.31
-
Creatine
-
pH 8.0, ubiquitous mitochondrial isozyme
8
-
Creatine
-
-
8.1
-
Creatine
-
pH 7.4, octameric form
8.2
-
Creatine
-
pH 9.0, 30C, recombinant mutant R340A
8.33
-
Creatine
-
reduced form of creatine kinase
8.39
-
Creatine
-
wild-type containing both oxidized and reduced form
8.48
-
Creatine
-
oxidized form of creatine kinase
8.7
-
Creatine
-
mutant C74A, 25C
8.7
-
Creatine
-
wild-type
8.7
-
Creatine
-
25C, pH not specified in the publication, mutant A267H
8.9
-
Creatine
-
mutant A76G, 25C
8.9
-
Creatine
-
25C, pH not specified in the publication, mutant K304T
9
-
Creatine
-
pH 9.0, 30C, recombinant wild-type enzyme
9
-
Creatine
-
mutant C74S, 25C
9.1
-
Creatine
-
wild-type, 25C
9.38
-
Creatine
-
-
9.5
-
Creatine
-
pH 9.0, muscle-type cytosolic isozyme
9.6
-
Creatine
-
wild-type; wild-type enzyme
10.5
-
Creatine
Q90X19
25C, pH not specified in the publication, mutant S329A
10.8
-
Creatine
-
cytoplasmic isoform M1, 25C
11
-
Creatine
Q90X19
25C, pH not specified in the publication, mutant N146C
11.1
-
Creatine
-
25C, pH not specified in the publication, mutant Q185E
11.2
-
Creatine
-
cytoplasmic isoform M2, 25C
12.9
-
Creatine
-
25C, pH not specified in the publication, mutant C146N
13
-
Creatine
-
fusion protein CK-AK
13.8
-
Creatine
-
mutant V75A, 25C
14
-
Creatine
-
fusion protein AK-CK
14.2
-
Creatine
Q90X19
25C, pH not specified in the publication, wild-type
14.5
-
Creatine
-
cytoplasmic isoform M1, 25C
14.8
-
Creatine
-
25C, pH not specified in the publication, mutant E46Q
16.7
-
Creatine
Q90X19
25C, pH not specified in the publication, mutant H267A
17.1
-
Creatine
Q90X19
25C, pH not specified in the publication, mutant Q46E
17.8
-
Creatine
Q90X19
25C, pH not specified in the publication, mutant T304K
18.3
-
Creatine
-
mutant C74M, 25C
18.6
-
Creatine
-
mutant C74L, 25C
19
-
Creatine
-
pH 9.0, 30C, recombinant mutant R340K
19
-
Creatine
-
isoform II isolated after expression in Escherichia coli, pH 8.0, 30C
20
-
Creatine
-
isoform III isolated after expression in Escherichia coli, pH 8.0, 30C
20.2
-
Creatine
-
mitochondrial isoform M2, 25C
20.6
-
Creatine
-
25C, pH not specified in the publication, mutant D189A
20.8
-
Creatine
Q90X19
25C, pH not specified in the publication, mutant A205S
21
-
Creatine
-
wild-type and isoform IV isolated after expression in Escherichia coli, pH 8.0, 30C
21.4
-
Creatine
-
mutant V72A, 25C
21.6
-
Creatine
Q90X19
25C, pH not specified in the publication, mutant K36L
23.5
-
Creatine
-
cytoplasmic isoform M1, 25C
25
-
Creatine
-
mutant G73A, 25C
25.5
-
Creatine
-
mitochondrial isoform M2, 25C
26.4
-
Creatine
-
cytoplasmic isoform M2, 25C
28.5
-
Creatine
Q90X19
25C, pH not specified in the publication, mutant A189D
34
-
Creatine
-
mutant D54G; mutant enzyme D54G
44.1
-
Creatine
Q90X19
25C, pH not specified in the publication, mutant E185Q
72
-
Creatine
-
pH 9.0, 30C, recombinant mutant R235K
76
-
Creatine
-
pH 9.0, 30C, recombinant mutant R291K
79
-
Creatine
-
30C
163
-
Creatine
-
pH 9.0, 30C, recombinant mutant R340Q
167
-
Creatine
-
pH 9.0, 30C, recombinant mutant R129A
0.23
-
creatine phosphate
-
pH 7.4, dimeric form
0.31
-
creatine phosphate
-
30C
0.4
-
creatine phosphate
-
pH 7.0, 25C
0.4
-
creatine phosphate
-
-
0.49
0.5
creatine phosphate
-
30C, pH 7.4
0.68
-
creatine phosphate
-
pH 7.4, octameric form
1.07
-
creatine phosphate
-
37C, ubiquitous isoform
1.19
-
creatine phosphate
-
37C, sarcomeric isoform
1.9
2.2
creatine phosphate
-
acetylcholine receptor membrane-associated enzyme
1.9
2.2
creatine phosphate
-
-
3
-
creatine phosphate
-
-
3.7
-
creatine phosphate
-
30C
17
-
creatine phosphate
-
0.5C, pH 7.6
50
-
creatine phosphate
-
-
0.015
-
MgADP-
-
30C
0.017
-
MgADP-
-
pH 7.4, dimeric form
0.043
-
MgADP-
-
pH 7.4, octameric form
0.051
0.052
MgADP-
-
30C, pH 7.4
0.15
-
MgADP-
-
-
0.22
-
MgADP-
-
acetylcholine receptor membrane-asscociated enzyme
0.54
-
MgADP-
-
soluble enzyme from muscle
0.042
-
MgATP2-
-
pH 7.4, dimeric form
0.056
-
MgATP2-
-
30C
0.082
-
MgATP2-
-
pH 7.4, octameric form
0.22
-
MgATP2-
-
pH 9.0, 30C, recombinant wild-type enzyme, with substrate creatine
0.29
-
MgATP2-
-
pH 9.0, 30C, recombinant wild-type enzyme, with substrate cyclocreatine
0.62
-
MgATP2-
-
pH 9.0, 30C, recombinant wild-type enzyme, with substrate N-ethylglycocyamine
0.7
-
MgATP2-
-
pH 9.0, 30C, recombinant wild-type enzyme
0.73
-
MgATP2-
-
30C, pH 7.4
1.1
-
MgATP2-
-
pH 9.0, 30C, recombinant mutant R340K
1.6
-
MgATP2-
-
pH 9.0, 30C, recombinant mutant R291K; pH 9.0, 30C, recombinant mutant R340A
1.7
-
MgATP2-
-
-
3.6
-
MgATP2-
-
pH 9.0, 30C, recombinant mutant R235K
7.3
-
MgATP2-
-
pH 9.0, 30C, recombinant mutant R340Q
0.51
-
phosphocreatine
-
pH 7.0, brain-type cytosolic isozyme
0.55
-
phosphocreatine
-
pH 7.0, ubiquitous mitochondrial isozyme
0.61
-
phosphocreatine
-
0.005 mM organotellurium, preincubation time 5 min, mitochondrial fraction, including reduced glutathione (GSH), pH 7.5, 37C
0.67
-
phosphocreatine
-
no organotellurium, preincubation time 5 min, mitochondrial fraction, including reduced glutathione (GSH), pH 7.5, 37C
0.7
-
phosphocreatine
-
0.020 mM organotellurium, preincubation time 5 min, mitochondrial fraction, including reduced glutathione (GSH), pH 7.5, 37C
0.8
-
phosphocreatine
-
pH 7.5, 37C
0.87
-
phosphocreatine
-
no organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37C
1.11
-
phosphocreatine
-
no organotellurium, preincubation time 5 min, cytosolic fraction, including reduced glutathione (GSH), pH 7.5, 37C
1.15
-
phosphocreatine
-
0.005 mM organotellurium, preincubation time 5 min, cytosolic fraction, including reduced glutathione (GSH), pH 7.5, 37C
1.16
-
phosphocreatine
-
pH 7.0, ubiquitous mitochondrial isozyme
1.32
-
phosphocreatine
-
0.005 mM organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37C
1.33
-
phosphocreatine
-
pH 7.0, muscle-type cytosolic isozyme
1.34
-
phosphocreatine
-
no organotellurium, preincubation time 5 min, mitochondrial fraction, pH 7.5, 37C
1.41
-
phosphocreatine
-
0.020 mM organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37C
1.72
-
phosphocreatine
-
0.020 mM organotellurium, preincubation time 5 min, cytosolic fraction, including reduced glutathione (GSH), pH 7.5, 37C
1.73
-
phosphocreatine
-
0.005 mM organotellurium, preincubation time 5 min, mitochondrial fraction, pH 7.5, 37C
2.04
-
phosphocreatine
-
0.020 mM organotellurium, preincubation time 5 min, mitochondrial fraction, pH 7.5, 37C
3.26
-
phosphocreatine
-
0.005 mM organotellurium, preincubation time 30 min, cytosolic fraction, pH 7.5, 37C
3.34
-
phosphocreatine
-
0.020 mM organotellurium, preincubation time 30 min, cytosolic fraction, pH 7.5, 37C
3.54
-
phosphocreatine
-
no organotellurium, preincubation time 30 min, cytosolic fraction, pH 7.5, 37C
5.77
-
phosphocreatine
-
0.005 mM organotellurium, preincubation time 30 min, mitochondrial fraction, pH 7.5, 37C
6.43
-
phosphocreatine
-
0.020 mM organotellurium, preincubation time 30 min, mitochondrial fraction, pH 7.5, 37C
8.97
-
phosphocreatine
-
no organotellurium, preincubation time 30 min, mitochondrial fraction, pH 7.5, 37C
10.3
-
MgATP2-
-
pH 9.0, 30C, recombinant mutant R129A
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
effect of temperature on values for MgATP2- and creatine
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
temperature dependence of reaction, in vivo measurements
-
additional information
-
additional information
-
dextran strongly increases Km
-
additional information
-
additional information
-
-
-
additional information
-
additional information
P00563
kinetics
-
additional information
-
additional information
-
kinetics, recombinant wild-type and mutant enzymes
-
additional information
-
additional information
-
kinetics, negative cooperativity
-
additional information
-
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
-
additional information
-
kinetics, the enzyme shows negative cooperativity and nonidentical active sites
-
additional information
-
additional information
P11009
kinetics, the enzyme shows negative cooperativity and nonidentical active sites
-
additional information
-
additional information
-
kinetic mechanism, the enzyme shows negative cooperativity and nonidentical active sites
-
additional information
-
additional information
-
kinetics, the enzyme shows negative cooperativity and nonidentical active sites
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics for ADP in mitochondria, enhancing effect of creatine, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
78.3
-
ADP
-
pH 7.0, ubiquitous mitochondrial isozyme
90
-
ADP
-
pH 7.0, ubiquitous mitochondrial isozyme
350
-
ADP
-
pH 7.0, brain-type cytosolic isozyme
483.3
-
ADP
-
pH 7.0, muscle-type cytosolic isozyme
0.06
-
alpha-(RP)-borano substituted ADP
-
-
0.03
-
alpha-(SP)-borano substituted ADP
-
-
36.4
-
ATP
-
muscle-type isoform MCK
38.4
-
ATP
-
mitochondrial isoform sMiCK
51.7
-
ATP
-
pH 8.0, ubiquitous mitochondrial isozyme
75
-
ATP
-
pH 8.0, ubiquitous mitochondrial isozyme
76
-
ATP
-
isoform II isolated after expression in Escherichia coli, pH 8.0, 30C
88
-
ATP
-
isoform IV isolated after expression in Escherichia coli, pH 8.0, 30C
115
-
ATP
-
isoform III isolated after expression in Escherichia coli, pH 8.0, 30C
143
-
ATP
-
wild-type, pH 8.0, 30C
153.5
-
ATP
-
pH 9.0, muscle-type cytosolic isozyme
155
-
ATP
-
isoform I isolated after expression in Escherichia coli, pH 8.0, 30C
215
-
ATP
-
pH 9.0, brain-type cytosolic isozyme
0.08
-
Creatine
-
pH 9.0, 30C, recombinant mutant R129A
0.54
-
Creatine
-
pH 9.0, 30C, recombinant mutant R235K
1.33
-
Creatine
-
pH 9.0, 30C, recombinant mutant R340Q
2.14
-
Creatine
-
pH 9.0, 30C, recombinant mutant R340A
2.18
-
Creatine
-
pH 9.0, 30C, recombinant mutant R291K
4.2
-
Creatine
-
pH 9.0, 30C, recombinant mutant I69A
4.5
-
Creatine
-
mitochondrial isoform, 25C
12.5
-
Creatine
-
cytoplasmic isoform M2, 25C
13.1
-
Creatine
-
cytoplasmic isoform B, 25C
14.7
-
Creatine
-
cytoplasmic isoform M1, 25C
15
-
Creatine
-
mitochondrial isoform, 25C
15.4
-
Creatine
-
pH 9.0, 30C, recombinant mutant V325A
16.3
-
Creatine
-
cytoplasmic isoform M, 25C
19.9
-
Creatine
-
cytoplasmic isoform M2, 25C
20.3
-
Creatine
-
cytoplasmic isoform B, 25C
25.2
-
Creatine
-
cytoplasmic isoform M1, 25C
27.9
-
Creatine
-
cytoplasmic isoform, 25C
36.4
-
Creatine
-
muscle-type isoform MCK
38.4
-
Creatine
-
mitochondrial isoform sMiCK
41.3
-
Creatine
-
mitochondrial isoform, 25C
45
-
Creatine
-
pH 9.0, 30C, recombinant mutant I69L
50.1
-
Creatine
-
pH 9.0, 30C, recombinant mutant R340K
51.7
-
Creatine
-
pH 8.0, ubiquitous mitochondrial isozyme
75
-
Creatine
-
pH 8.0, ubiquitous mitochondrial isozyme
82.7
-
Creatine
-
pH 9.0, 30C, recombinant mutant I69V
85.3
-
Creatine
-
pH 9.0, 30C, recombinant wild-type enzyme
106
-
Creatine
-
co-substrate: ATP, 25C, pH not specified in the publication, mutant Q185E
112
-
Creatine
-
co-substrate: ATP, 25C, pH not specified in the publication, mutant A329S
115
-
Creatine
-
co-substrate: ATP, 25C, pH not specified in the publication, mutant E46Q
117
-
Creatine
-
co-substrate: ATP, 25C, pH not specified in the publication, mutant D189A
119
-
Creatine
Q90X19
co-substrate: ATP, 25C, pH not specified in the publication, mutant E185Q
122
-
Creatine
-
co-substrate: ATP, 25C, pH not specified in the publication, mutant K304T
126
-
Creatine
Q90X19
co-substrate: ATP, 25C, pH not specified in the publication, mutant K36L
128
-
Creatine
Q90X19
co-substrate: ATP, 25C, pH not specified in the publication, mutant T304K
132
-
Creatine
Q90X19
co-substrate: ATP, 25C, pH not specified in the publication, mutant Q46E
138
-
Creatine
-
co-substrate: ATP, wild-type hMMCK, pH and temperature not specified in the publication
140
-
Creatine
Q90X19
co-substrate: ATP, 25C, pH not specified in the publication, mutant N146C
142
-
Creatine
Q90X19
co-substrate: ATP, 25C, pH not specified in the publication, mutant H267A; co-substrate: ATP, 25C, pH not specified in the publication, mutant S329A
148
-
Creatine
-
pH 9.0, 30C, recombinant wild-type enzyme
153.5
-
Creatine
-
pH 9.0, muscle-type cytosolic isozyme
159
-
Creatine
Q90X19
co-substrate: ATP, 25C, pH not specified in the publication, wild-type
163
-
Creatine
Q90X19
co-substrate: ATP, 25C, pH not specified in the publication, mutant A189D
170
-
Creatine
-
co-substrate: ATP, 25C, pH not specified in the publication, wild-type
173
-
Creatine
Q90X19
co-substrate: ATP, 25C, pH not specified in the publication, mutant A205S
173
-
Creatine
-
co-substrate: ATP, 25C, pH not specified in the publication, mutant C146N
175
-
Creatine
-
co-substrate: ATP, 25C, pH not specified in the publication, mutant L36K
178
-
Creatine
-
co-substrate: ATP, 25C, pH not specified in the publication, mutant S205A
196
-
Creatine
-
co-substrate: ATP, 25C, pH not specified in the publication, mutant A267H
215
-
Creatine
-
pH 9.0, brain-type cytosolic isozyme
238
-
Creatine
-
co-substrate: ATP, hybrid form consisting of muscle and brain creatine kinase isoforms, pH and temperature not specified in the publication
417
-
Creatine
-
co-substrate: ATP, wild-type hBBCK, pH and temperature not specified in the publication
1.5
-
cyclocreatine
-
pH 9.0, 30C, recombinant mutant I69L
4.4
-
cyclocreatine
-
pH 9.0, 30C, recombinant mutant I69V
18
-
cyclocreatine
-
pH 9.0, 30C, recombinant mutant V325A
35.2
-
cyclocreatine
-
pH 9.0, 30C, recombinant wild-type enzyme
0.08
-
MgATP2-
-
pH 9.0, 30C, recombinant mutant R129A
0.54
-
MgATP2-
-
pH 9.0, 30C, recombinant mutant R235K
1.33
-
MgATP2-
-
pH 9.0, 30C, recombinant mutant R340Q
2.14
-
MgATP2-
-
pH 9.0, 30C, recombinant mutant R340A
2.18
-
MgATP2-
-
pH 9.0, 30C, recombinant mutant R291K
50.1
-
MgATP2-
-
pH 9.0, 30C, recombinant mutant R340K
0.55
-
N-ethylglycocyamine
-
pH 9.0, 30C, recombinant mutant I69L
4.3
-
N-ethylglycocyamine
-
pH 9.0, 30C, recombinant mutant V325A
12
-
N-ethylglycocyamine
-
pH 9.0, 30C, recombinant mutant I69V
14.5
-
N-ethylglycocyamine
-
pH 9.0, 30C, recombinant wild-type enzyme
78.3
-
phosphocreatine
-
pH 7.0, ubiquitous mitochondrial isozyme
90
-
phosphocreatine
-
pH 7.0, ubiquitous mitochondrial isozyme
350
-
phosphocreatine
-
pH 7.0, brain-type cytosolic isozyme
483.3
-
phosphocreatine
-
pH 7.0, muscle-type cytosolic isozyme
148
-
MgATP2-
-
pH 9.0, 30C, recombinant wild-type enzyme
additional information
-
additional information
-
comparison of kinetic constants with enzymes from Mus musculus, Lampetra japonica, Neanthes diversicolor, Dendronephthya gigantea
-
additional information
-
additional information
-
comparison of kinetic constants with enzymes from Mus musculus, Danio rerio, Lampetra japonica, Neanthes diversicolor
-
additional information
-
additional information
-
comparison of kinetic constants with enzymes from Mus musculus, Danio rerio, Lampetra japonica, Dendronephthya gigantea
-
additional information
-
additional information
-
comparison of kinetic constants with enzymes from Mus musculus, Danio rerio, Neanthes diversicolor, Dendronephthya gigantea
-
additional information
-
additional information
-
comparison of kinetic constants with enzymes from Danio rerio, Lampetra japonica, Neanthes diversicolor, Dendronephthya gigantea
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.37
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min, ADP variable, mitochondrial fraction, pH 7.5, 37C
-
2.53
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), ADP variable, mitochondrial fraction, pH 7.5, 37C
-
5.02
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), ADP variable, cytosolic fraction, pH 7.5, 37C
-
5.46
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min, phosphocreatine variable, mitochondrial fraction, pH 7.5, 37C
-
5.67
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.020 mM organotellurium, preincubation time 5 min, ADP variable, mitochondrial fraction, pH 7.5, 37C
-
5.78
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.020 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), ADP variable, mitochondrial fraction, pH 7.5, 37C
-
6.49
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min, phosphocreatine variable, cytosolic fraction, pH 7.5, 37C
-
7.1
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.020 mM organotellurium, preincubation time 30 min, ADP variable, cytosolic fraction, pH 7.5, 37C
-
7.18
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.020 mM organotellurium, preincubation time 30 min, phosphocreatine variable, mitochondrial fraction, pH 7.5, 37C
-
7.5
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.020 mM organotellurium, preincubation time 30 min, ADP variable, mitochondrial fraction, pH 7.5, 37C
-
7.56
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.020 mM organotellurium, preincubation time 30 min, phosphocreatine variable, cytosolic fraction, pH 7.5, 37C
-
8
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.005 mM organotellurium, preincubation time 30 min, phosphocreatine variable, mitochondrial fraction, pH 7.5, 37C
-
8.12
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.005 mM organotellurium, preincubation time 30 min, ADP variable, cytosolic fraction, pH 7.5, 37C
-
8.2
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.005 mM organotellurium, preincubation time 30 min, phosphocreatine variable, cytosolic fraction, pH 7.5, 37C
-
8.22
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.005 mM organotellurium, preincubation time 30 min, ADP variable, mitochondrial fraction, pH 7.5, 37C
-
8.69
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), phosphocreatine variable, cytosolic fraction, pH 7.5, 37C
-
8.76
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), phosphocreatine variable, mitochondrial fraction, pH 7.5, 37C
-
9.65
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.020 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), ADP variable, cytosolic fraction, pH 7.5, 37C
-
10.25
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.020 mM organotellurium, preincubation time 5 min, phosphocreatine variable, mitochondrial fraction, pH 7.5, 37C
-
10.55
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min, ADP variable, cytosolic fraction, pH 7.5, 37C
-
15.45
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.020 mM organotellurium, preincubation time 5 min, ADP variable, cytosolic fraction, pH 7.5, 37C
-
16
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.020 mM organotellurium, preincubation time 5 min, phosphocreatine variable, cytosolic fraction, pH 7.5, 37C
-
16.15
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.020 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), phosphocreatine variable, mitochondrial fraction, pH 7.5, 37C
-
16.46
-
3-butyl-1-phenyl-2-(phenyltelluro)oct-en-1-one
-
0.020 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), phosphocreatine variable, cytosolic fraction, pH 7.5, 37C
-
0.025
-
5-(4-([(benzoylphenyl)amino]carbonyl)phenyl)-2-furoic acid
-
-
0.025
-
5-(4-[[(benzoylphenyl)amino]carbonyl]phenyl)-2-furoic acid
-
-
0.049
-
alpha-P-borano substituted ADP Sp isomer
-
-
10
-
L-isoleucine
-
versus phosphocreatine, pH 7.5, 37C
21
-
L-isoleucine
-
versus ADP, pH 7.5, 37C
16
-
L-leucine
-
versus phosphocreatine, pH 7.5, 37C
22
-
L-leucine
-
versus ADP, pH 7.5, 37C
14
-
L-valine
-
versus phosphocreatine, pH 7.5, 37C
1.22
-
SDS
-
in 5 mM glycine-NaOH (pH 9.0), at 25C
23
-
L-valine
-
versus ADP, pH 7.5, 37C
additional information
-
additional information
-
inhibition kinetics with 4-hydroxy-3-nitrophenylglyoxal, overview
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.15
-
Zn2+
-
at 25C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.99
-
-
crude homogenate
15
-
-
synthesis of phosphocreatine
22
-
-
mutant Trp to Phe
26
-
-
mutant Trp to Asn
26.8
-
-
mutant Tyr to Asn
28.8
-
-
mutant Tyr to His
29.6
-
-
mutant Trp to Cys
31.8
-
-
wild-type
32
-
-
mutant Trp to His
36.2
-
-
wild-type
36.4
-
-
mutant Trp to Tyr
43.48
-
-
enzyme from embryonic stem cell-derived cardiomyocytes, pH 6.5, 37C
43.7
-
-
mutant W264C
46.5
-
-
mutant L115D
49.5
-
-
synthesis of ATP
50.25
-
-
enzyme from neonatal cardiomyocytes, pH 6.5, 37C
52
-
-
mutant D54G; mutant enzyme D54G
62.3
-
-
mutant W264Y
70.2
-
-
wild-type
71.2
-
-
mutant Tyr to Trp
94.4
-
-
mutant L121D
148
-
-
mutant V72A, 25C
205.1
-
-
after 68.6fold purification
206
-
-
purified cytosolic isozyme
210
-
-
oxidized form of creatine kinase
240
-
-
purified mitochondrial isozyme
245.5
-
-
wild-type enzyme
246
-
-
wild-type
250
-
-
30C, pH 7.0
256
-
-
mutant C74M, 25C
258
-
-
mutant C74L, 25C
261
-
-
wild-type, 25C
261
-
-
wild-type containing both oxidized and reduced form
263
-
-
mutant V75A, 25C
266
-
-
mutant C74S, 25C
272
-
-
mutant A76G, 25C
274.9
-
-
reduced form of creatine kinase
276
-
-
wild-type
278
-
-
mutant C74A, 25C
299
-
-
mutant L110D
345
-
-
isoform CK1, pH 6.7
410
-
-
30C
511
-
-
isoform CK2, pH 6.7
8208
-
-
mutant G73A, 25C
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
assay method
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
assay method
additional information
-
-
-
additional information
-
-
-
additional information
-
-
activity in whole muscle fibers and myofibrillar activity
additional information
-
-
assay method
additional information
-
-
substrate specificities of recombinant wild-type and mutant enzymes
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
6.5
-
synthesis of MgATP2-
6.3
-
-
synthesis of MgATP2-
6.5
-
-
enzyme from neonatal cardiomyocytes
6.7
-
-
synthesis of MgATP2-
6.8
-
P00563
native enzyme in solution
7
-
-
enzyme from embryonic stem cell-derived cardiomyocytes
7.4
-
-
assay at
7.5
-
-
assay at
8
8.3
-
synthesis of phosphocreatine
8
-
-
synthesis of phosphocreatine
8
-
-
assay at
9
-
-
assay at
9
-
P00563
assay at
9
-
-
assay at
9
-
-
assay at
additional information
-
-
substrate channelling under different pH conditions
additional information
-
P00563
in comparison to free enzyme in solution, enzyme adsorbed onto silicon wafers presents a shift of the optimal pH value toward alkaline pH
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
-
assay at
30
-
P00563
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
36
-
-
-
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
42
45
-
synthesis of ATP
42
-
-
synthesis of phosphocreatine
45
-
-
both for enzyme from embryonic stem cell-derived cardiomyocytes and from neonatal cardiomyocytes
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
25
Q90X19
optimal temperature
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.2
-
-
isoelectric focusing
6.2
-
-
isoelectric focusing, enzyme variant IV
6.3
6.8
-
isoelectric focusing
6.4
-
-
isoelectric focusing, enzyme variant IV
6.55
6.95
-
isoelectric focusing, dimeric sarcomeric isoform
6.6
-
-
isoelectric focusing, dimeric ubiquitous isoform
6.67
-
-
cytoplasmic enzyme
6.7
-
-
isoelectric focusing, enzyme variant III
6.8
-
-
several bands in serum of a patient with ovarian hepatoid yolk sac tumor, atypical ubiquitous mitochondrial enzyme, isoelectric focusing
6.9
-
-
isoelectric focusing, enzyme variant II
6.9
-
-
ubiquitous mitochondrial enzyme, 2 bands at pH 6.9 and pH 7.0 in isoelectric focusing
7
7.8
-
several bands in serum of a patient with ovarian hepatoid yolk sac tumor, atypical ubiquitous mitochondrial enzyme, isoelectric focusing
7
-
-
ubiquitous mitochondrial enzyme, 2 bands at pH 6.9 and pH 7.0 in isoelectric focusing
7.1
-
-
isoelectric focusing, octameric sarcomeric isoform; isoelectric focusing, octameric ubiquitous isoform
7.2
-
-
isoelectric focusing, enzyme variant I
7.3
7.4
-
isoelectric focusing, isoform MM3
7.37
-
-
mitochondrial enzyme
7.43
-
-
isoelectric focusing, isoform MM2
7.44
-
-
isoelectric focusing, dimeric form
7.5
-
-
isoelectric focusing, dimeric form
7.58
-
-
isoelectric focusing, isoform MM1
7.7
-
-
isoelectric focusing, octameric form
8.3
-
-
isoelectric focusing, octameric form
additional information
-
-
-
additional information
-
-
overview methods, behaviour of oligomeric forms
additional information
-
-
the mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK differ in their pI and ar therefore also termed the acidic and basic isozymes
additional information
-
P11009
the mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK differ in their pI and ar therefore also termed the acidic and basic isozymes
additional information
-
-
the mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK differ in their pI and ar therefore also termed the acidic and basic isozymes
additional information
-
-
the mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK differ in their pI and are therefore also termed the acidic and basic isozymes
additional information
-
-
the enzyme from serum of a patient with ovarian hepatoid yolk sac tumor shows an atypical pI value compared to enzyme from other, healthy tissue, overview
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
creatine kinase activity is much greater females than in males. Plasma creatine kinase activity may reflect the protein turnover, which is closely related to muscle growth rate
Manually annotated by BRENDA team
-
phenylbutyrate greatly decreases the adriamycin-associated elevations of serum lactate dehydrogenase and creatine kinase activities, two nonspecific widely used cardiac injury markers
Manually annotated by BRENDA team
-
measurement of creatine kinase activity (hippocampus, striatum, cerebellum, cerebral cortex and prefrontal cortex) in brain if rats are submitted to renal ischemia and the effect of administration of antioxidants (N-acetylcysteine, N-acetylcysteine and deferoxamine, deferoxamine) on this enzyme. Creatine kinase activity is not altered in cerebellum and striatum of rats. Creatine kinase activity is inhibited in prefrontal cortex and hippocampus of rats 12 h after renal ischemia. The treatment with antioxidants prevents such effect. In cerebral cortex creatine kinase activity is inhibited 6 and 12 h after renal ischemia. Only N-acetylcysteine or N-acetylcysteine plus deferoxamine are able to prevent the inhibition on the enzyme. Although it is difficult to extrapolate the findings to the human condition, the inhibition of brain creatine kinase activity after renal failure may be associated to neuronal loss and may be involved in the pathogenesis of uremic encephalopathy
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
measurement of creatine kinase activity (hippocampus, striatum, cerebellum, cerebral cortex and prefrontal cortex) in brain if rats are submitted to renal ischemia and the effect of administration of antioxidants (N-acetylcysteine, N-acetylcysteine and deferoxamine, deferoxamine) on this enzyme. Creatine kinase activity is not altered in cerebellum and striatum of rats. Creatine kinase activity is inhibited in prefrontal cortex and hippocampus of rats 12 h after renal ischemia. The treatment with antioxidants prevents such effect. In cerebral cortex creatine kinase activity is inhibited 6 and 12 h after renal ischemia. Only N-acetylcysteine or N-acetylcysteine plus deferoxamine are able to prevent the inhibition on the enzyme. Although it is difficult to extrapolate the findings to the human condition, the inhibition of brain creatine kinase activity after renal failure may be associated to neuronal loss and may be involved in the pathogenesis of uremic encephalopathy
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
embryonic stem cell- and neonatal-derived cardiomyocytes
Manually annotated by BRENDA team
-
inhibition of creatine kinase blunts high extracellular Ca2+-induced increases in cardiomyocyte contractile response
Manually annotated by BRENDA team
-
creatine kinase activity is not altered if rats are submitted to renal ischemia
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
creatine kinase activity is not altered if rats are submitted to renal ischemia
-
Manually annotated by BRENDA team
-
in cerebral cortex creatine kinase activity is inhibited 6 and 12 h after renal ischemia. Only N-acetylcysteine or N-acetylcysteine plus deferoxamine are able to prevent the inhibition on the enzyme
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
in cerebral cortex creatine kinase activity is inhibited 6 and 12 h after renal ischemia. Only N-acetylcysteine or N-acetylcysteine plus deferoxamine are able to prevent the inhibition on the enzyme
-
Manually annotated by BRENDA team
-
creatine kinase activity is not altered if rats are submitted to renal ischemia
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
creatine kinase activity is not altered if rats are submitted to renal ischemia
-
Manually annotated by BRENDA team
Q7ZYQ9, Q8AVH2
-
Manually annotated by BRENDA team
Q7ZYQ9, Q8AVH2
;
Manually annotated by BRENDA team
-
embryonic stem cell-derived cardiomyocytes
Manually annotated by BRENDA team
Q7ZYQ9, Q8AVH2
-
Manually annotated by BRENDA team
P06732
expresses low levels of cytoplasmic, high levels of mitochondrial creatine kinase. Targeting the dominating isoform by its siRNA has strong effect on overall enzyme activity. Inhibition of mitochondrial isoform causes a strong decline in cell viability and cell proliferation and also substantial alteration of mitochondrial morphology as well as mitochondrial membrane topology; HaCaT cells express low levels of cytoplasmic creatine kinase (BB-CK) and high levels of mitochondrial creatine kinase (uMiCK). HeLa-S3 cells express high levels of cytoplasmic creatine kinase (BB-CK) and low levels of mitochondrial creatine kinase (uMiCK); HaCaT cells express low levels of cytoplasmic creatine kinase (BB-CK) and high levels of mitochondrial creatine kinase (uMiCK). HeLa-S3 cells express high levels of cytoplasmic creatine kinase (BB-CK) and low levels of mitochondrial creatine kinase (uMiCK)
Manually annotated by BRENDA team
-
after beta-actin, cytosolic brain isoform of creatin kinase is the most abundant protein in hair bundle and capable of maintaining high aTP levels despite 1 mM/s ATP consumption by the plasma-membrane Ca2+-ATPase
Manually annotated by BRENDA team
-
creatine kinase circuit is essential for high-sensitivity hearing
Manually annotated by BRENDA team
-
enzyme variants IIV
Manually annotated by BRENDA team
trout
-
-
Manually annotated by BRENDA team
Q7ZYQ9, Q8AVH2
-
Manually annotated by BRENDA team
-
human heart cDNA library is used
Manually annotated by BRENDA team
P06732
expresses high levels of cytoplasmic, low levels of mitochondrial creatine kinase. Targeting the dominating isoform by its siRNA has strong effect on overall enzyme activity. Inhibition of mitochondrial isoform causes a strong decline in cell viability and cell proliferation and also substantial alteration of mitochondrial morphology as well as mitochondrial membrane topology; HaCaT cells express low levels of cytoplasmic creatine kinase (BB-CK) and high levels of mitochondrial creatine kinase (uMiCK). HeLa-S3 cells express high levels of cytoplasmic creatine kinase (BB-CK) and low levels of mitochondrial creatine kinase (uMiCK); HaCaT cells express low levels of cytoplasmic creatine kinase (BB-CK) and high levels of mitochondrial creatine kinase (uMiCK). HeLa-S3 cells express high levels of cytoplasmic creatine kinase (BB-CK) and low levels of mitochondrial creatine kinase (uMiCK)
Manually annotated by BRENDA team
-
creatine kinase activity is inhibited in prefrontal cortex and hippocampus of rats 12 h after renal ischemia. The treatment with antioxidants prevents such effect
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
creatine kinase activity is inhibited in prefrontal cortex and hippocampus of rats 12 h after renal ischemia. The treatment with antioxidants prevents such effect
-
Manually annotated by BRENDA team
Q7ZYQ9, Q8AVH2
-
Manually annotated by BRENDA team
-
CKB mRNA and protein levels are significantly higher in probands affected with autosomal dominant inherited anomaly CKBE
Manually annotated by BRENDA team
-
enzyme variants I-IV; skeletal
Manually annotated by BRENDA team
-
commercial preparation
Manually annotated by BRENDA team
-
skinned psoas muscle
Manually annotated by BRENDA team
-
two muscle-specific isoforms
Manually annotated by BRENDA team
-
oxidized form of enzyme
Manually annotated by BRENDA team
-
at 24 hours post-injection of artesunate into the left gluteal muscle, plasma creatine kinase concentrations are elevated above normal. At 7 days after injection, creatine kinase concentrations are normal
Manually annotated by BRENDA team
Q7ZYQ9, Q8AVH2
hypaxial
Manually annotated by BRENDA team
-
leptin decreases creatibe kinase
Manually annotated by BRENDA team
Q7ZYQ9, Q8AVH2
;
Manually annotated by BRENDA team
-
CKB mRNA and protein levels are significantly higher in probands affected with autosomal dominant inherited anomaly CKBE
Manually annotated by BRENDA team
-
creatine kinase activity is inhibited in prefrontal cortex and hippocampus of rats 12 h after renal ischemia. The treatment with antioxidants prevents such effect
Manually annotated by BRENDA team
Q7ZYQ9, Q8AVH2
-
Manually annotated by BRENDA team
-
psoas myofibril, study of creatine kinase exchange rates between the myofibrillar M-band and its surroundings. In presence of substrates, the exchange rate of the enzyme slows down indicating an increase in the strength of the bond between creatine kinase and the M-band
Manually annotated by BRENDA team
-
patient with ovarian hepatoid yolk sac tumor, an atypical ubiquitous mitochondrial enzyme form
Manually annotated by BRENDA team
Q7ZYQ9, Q8AVH2
;
Manually annotated by BRENDA team
-
isoforms CK1, CK2 are characteristic for spermatozoa
Manually annotated by BRENDA team
Q7ZYQ9, Q8AVH2
-
Manually annotated by BRENDA team
-
of immature animals
Manually annotated by BRENDA team
additional information
-
overview tissue distribution of mitochondrial enzyme
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoforms M1, M2, B
Manually annotated by BRENDA team
-
isoforms M, B
Manually annotated by BRENDA team
-
isozymes CK-MM, CK-BB, and CK-MB
Manually annotated by BRENDA team
-
muscle-type cytosolic isozyme MM-CK, and brain-type cytosolic isozyme BB-CK
Manually annotated by BRENDA team
P06732
HaCaT cells express low levels of cytoplasmic creatine kinase (BB-CK) and high levels of mitochondrial creatine kinase (uMiCK). HeLa-S3 cells express high levels of cytoplasmic creatine kinase (BB-CK) and low levels of mitochondrial creatine kinase (uMiCK)
Manually annotated by BRENDA team
-
cytoplasmic, muscle-type isoform MCK
Manually annotated by BRENDA team
-
acetylcholine receptor membrane
Manually annotated by BRENDA team
-
accumulated in contact sites between inner and outer mitochondrial membrane
Manually annotated by BRENDA team
-
accumulated in contact sites between inner and outer mitochondrial membrane
Manually annotated by BRENDA team
-
overview on intramitochondrial localization
Manually annotated by BRENDA team
-
mitochondrial isozyme MtCK
Manually annotated by BRENDA team
-
simulation of hyperglycemic conditions induces H2O2 production in a creatine sensitive manner
Manually annotated by BRENDA team
P06732
HaCaT cells express low levels of cytoplasmic creatine kinase (BB-CK) and high levels of mitochondrial creatine kinase (uMiCK). HeLa-S3 cells express high levels of cytoplasmic creatine kinase (BB-CK) and low levels of mitochondrial creatine kinase (uMiCK). The mitochondrial CK isoform plays the most crucial role in maintaining cell viability by stabilizing contact sites between inner and outer mitochondrial membranes and maintaining local metabolite channeling, thus avoiding transition pore opening which eventually results in activation of caspase cell-death pathways; mitochondrial isoform plays the most crucial role in maintaining cell viability by stabilizing contact sites between inner and outer mitochondrial membranse and maintaining local metabolic channeling
Manually annotated by BRENDA team
-
sarcomeric, mitochondrial isoform sMiCK
Manually annotated by BRENDA team
-
in mitochondria from intact animals, mCK exists as a mixture of two oligomeric forms (dimer and octamer: 68 and 32%, respectively)
Manually annotated by BRENDA team
-
under energy-compromised conditions, CKM is recruited to the plasma membrane and co-localizes with NCX1
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42000
-
P00563
recombinant mutant R147A, analytical ultracentrifugation
43000
-
-
monomer
45000
-
P00563
recombinant mutant R147A/R151A, gel filtration and analytical ultracentrifugation
46000
-
P00563
recombinant mutant R147A, gel filtration
61500
-
-
dimeric enzyme form, gel filtration
64000
-
-
gel filtration
67000
-
P00563
recombinant mutant R151A, analytical ultracentrifugation
71000
-
P00563
recombinant mutant D209A, analytical ultracentrifugation
74000
-
P00563
recombinant mutant D209A, gel filtration
76000
78000
-
gel filtration
78000
80000
-
-
78000
-
-
isozyme Mi-CK, dimeric form, scanning transmission electron microscopy
78500
85100
-
cytosolic muscle isozyme
78500
85100
P11009
cytosolic muscle isozyme
78500
85100
-
cytosolic muscle isozyme
79700
-
-
and also 371000, gel filtration
80000
-
-
low speed sedimentation equilibrium centrifugation
81000
-
P00563
recombinant mutant R151A, gel filtration
82000
-
-
sedimentation equilibrium centrifugation
82600
-
-
cytosolic muscle isozyme, gel filtration
84000
85000
-
isozyme MiMi-CK, sedimentation equilibrium centrifugation, gel filtration
84000
-
-
isozyme MiMi-CK, equilibrium centrifugation
84000
-
-
gel filtration
84500
-
-
high speed and low speed sedimentation equilibrium centrifugation
85000
-
-
isozyme Mia-CK, dimeric form, gel permeation chromatography, analytical ultracentrifugation
85000
-
P00563
recombinant wild-type enzyme, gel filtration
85100
-
-
sedimentation equilibrium centrifugation
85300
-
-
wild-type hMMCK
86000
-
-
gel filtration, also 346000
86000
-
P00563
recombinant wild-type enzyme, analytical ultracentrifugation
86000
-
-
cytosolic isozyme, gel filtration
86000
-
-
homodimer
86200
-
-
wild-type hMMCK
89000
-
-
isozyme Mia-CK, dimeric form, scanning transmission electron microscopy
90000
-
-
gel filtration, isoform CK2
100000
-
-
gel filtration
126000
145000
-
flagellar isozyme, sucrose density gradient centrifugation, SDS-PAGE
240000
-
-
head isozyme, calculation from Stokes radius and partial specific volume
306000
352000
-
isozyme Mia-CK, octameric form, gel permeation chromatography, scanning transmission electron microscopy
328000
340000
-
isoenzyme Mi-CK, octameric form, sedimentation velocity analysis, sedimentation equilibrium centrifugation, scanning transmission electron microscopy
330000
-
-
gel filtration, isoform CK1
345000
-
-
mitochondrial isozyme, gel filtration
346000
-
-
gel filtration, also 86000
347000
-
-
octameric enzyme form, gel filtration
360000
-
-
isozyme Mia-CK, octameric form, gel filtration
371000
-
-
and also 79700, gel filtration
additional information
-
-
structural properties, sulfhydryl groups
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 40000-44000, mature enzyme
?
-
x * 43000, SDS-PAGE
dimer
-
crystallization data, absence of ATP
dimer
-
2 * 41500, SDS-PAGE
dimer
-
2 * 42000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
dimer
-
2 * 40000-43000, SDS-PAGE
dimer
-
2 * 41000, SDS-PAGE
dimer
-
2 * 42000, SDS-PAGE
dimer
-
2 * 43000-44000, SDS-PAGE, presence of 2-mercaptoethanol
dimer
-
2 * 49000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 44000, SDS-PAGE, presence of 2-mercaptoethanol, high speed sedimentation equilibrium centrifugation of urea-treated enzyme
dimer
-
2 * 41000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
-
2 * 43195, calculated from sequence of cDNA
dimer
-
1 * 41000 + 1 * 42000, isozyme CK-II; 2 * 41000, isozyme CK-IV; 2 * 42000, isozyme CK-III
dimer
-
2 * 42500
dimer
-
2 * 43600, SDS-PAGE, but also octamer, electron microscopy
dimer
-
2 * 43000, SDS-PAGE, but also octamer
dimer
P00563
2 * 47000, about, recombinant wild-type enzyme and recombinant mutant enzymes D209A and R151A, SDS-PAGE
dimer
-
2 * 43000, recombinant enzyme, SDS-PAGE, dimer formation after dissociation of the octamer
dimer
-
2 * 41000, muscle cytosolic isozyme, SDS-PAGE
dimer
-
2 * 40000-44000, mature cytosolic isozymes
dimer
P11009
2 * 40000-44000, mature cytosolic isozymes
dimer
-
2 * 40000-44000, mature cytosolic isozymes
dimer
-
muscle creatine kinase is only enzymatically active as a dimer
dimer
-
2 * 45000, SDS-PAGE, isoform CK2
homodimer
-
-
homodimer
-
2 * 43000, using NMR chemical-shift perturbation and relaxation experiments designed to study the active site 320s flexible loop of muscle creatine kinase it is shown that each subunit can bind substrates independently
monomer
-
1 * 145000, flagellar isozyme, SDS-PAGE
octamer
-
crystallization data
octamer
-
crystallization data, presence of ATP
octamer
-
8 * 42000, SDS-PAGE, octameric structure dissociates during storage at -20C, pH above 8.5, protein concentration below 0.3 mg/ml to dimeric form
octamer
-
8 * 43600, SDS-PAGE, but also dimer, electron microscopy
octamer
-
8 * 43000, SDS-PAGE, also as dimer
octamer
-
8 * 43000, recombinant enzyme, SDS-PAGE, enzyme primarily forms octamers
octamer
-
8 * 43000, muscle mitochondrial isozyme, SDS-PAGE
octamer
-
8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
octamer
P11009
8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
octamer
-
8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
octamer
-
8 * 41000, SDS-PAGE, isoform CK1
oligomer
-
in mitochondria from intact animals, mCK exists as a mixture of two oligomeric forms (dimer and octamer: 68 and 32%, respectively). Cerebral ischemia changes the dimer/octamer ratio. This ratio is shifted toward the formation of dimers after 30-min ischemia
polymer
-
x * 47000, head mitochondrial isozyme, SDS-PAGE
monomer
P00563
1 * 47000, about, recombinant mutant enzymes D209A, R147A, and R147A/R151A, SDS-PAGE
additional information
-
hydrolytic cleaveage is responsible for conversion of isoform MM1 to MM2 and MM3
additional information
-
overview on isoforms
additional information
-
the isozymes form monomers upon freeze-drying due to loss of subunit interactions
additional information
P00563
dimerization is no prerequisite for activity but is required for stability and quarternary structure, subunit interface structure and interacting side chains of Glu17, Tyr19, sp53, Gln57, Asp61, Asp209, Arg147, and Arg151, overview
additional information
-
the octamer-dimer equilibrium highly depends on protein concentration and dilution, respectively, and on temperature, highest percentage of octamer occurs at 28C, the lowest at 2C, overview
additional information
P11009
analysis of the structure of cardiac sarcomeric mitochondrial isozyme, free or bound to MgATP or transition state analogue complex
additional information
-
structure-function analysis, the monomeric enzyme is active, the subunits act independently
additional information
-
mutants L110D, L115D, L121D are faster on SDS-PAGE than wild-type protein
additional information
-
tertiary structure of oxidized form of enzyme is more easily disturbed than reduced form. The oxidized form, unlike reduced form, cannot interact with the M-line protein myomesin and therefore might have no role in muscle contraction. Oxidized creatine kinase can be rapidly ubiquitinated by muscle ring finger protein I and may be substrate of the ATP-ubiquitin-proteasome pathway
additional information
P00563
study on adsorption of creatine kinase onto silicon wafers. At pH 4, enzyme monomers in solution adsorb, forming a very thin layer indicating creatine kinase unfolding. At pH 6.8, the adsorbed layer is composed of a mixture of enzyme dimers in native structure and film thickness is increased. At pH 9, creatine kinase dimers form monolayers with the higest thickness. In comparison to free enzyme in solution, adsorbed enzyme presents a shift of the optimal pH value from 6.8 toward alkaline pH
additional information
-
recurrent interaction of brain-type enzyme isoform with cis-Golgi matrix protein GM130. GM130 and creatine kinase co-localize specifically in a transient fashion during early prophase of mitosis, when GM130 plays an important role in Golgi apparatus fragmentation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
soluble creatine kinase from euthermic squirrels is a mix of phosphorylated and dephosphorylated forms. In hibernating animals only phospho-enzyme is detected. High and low phosphate enzyme forms show different affinities for ATP and creatine substrates, but do not differ in stability to urea denaturation
additional information
-
enzyme activity depends on free sulfhydryl groups
additional information
-
enzyme activity depends on free sulfhydryl groups
additional information
-
enzyme activity depends on free sulfhydryl groups
side-chain modification
-
intrachain disulfide bond in oxidized form of enzyme is formed between C74 and C146
additional information
-
titration of two thiol groups leads to almost complete loss of activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure analysis of muscle cytosolic isozyme
-
isozyme MM-CK
-
overview: electron microscopy, X-ray crystallography
-
isozyme MM-CK
-
a dimeric and a octameric isoform
-
brain-type isoform
-
crystal structure analysis of the cytosolic brain isozyme, and of the cardiac sarcomeric mitochondrial crystallized free or bound to MgATP or transition state analogue complex
P11009
overview: electron microscopy, X-ray crystallography
-
crystal structure analysis of muscle-type cytosolic isozyme, and of ubiquitous mitochondrial isozyme, and of cytosolic brain type isozyme
-
crystallized at 22C using PEG 4000 as a precipitant. X-ray diffraction data are collected to 2.2 A resolution using synchrotron radiation. The crystals belong to the tetragonal space group P4(3)2(1)2, with cell parameters of a = b = 97.963, c = 164.312 A, and alpha = beta = gamma = 90. The symmetric unit contains two molecules of creatine kinase
-
isozyme MiMi-CK
-
muscle isoform
-
overview: electron microscopy, X-ray crystallography
-
ubiquituos mitochondrial isoform
-
crystal structure analysis of muscle cytosolic isozyme
-
crystals of the mutant G268N are successfully raised to study the fine structural change around the active site. Results show that one residue mutation in can cause the mutant G268N to exhibit cold-adapted enzyme properties comparable to those of Cyprinus carpio M1-creatine kinase
-
muscle isoform
-
NMR screening of inhibitors docked to the crystal structure of enzyme. A phenylfuroic acid may enter into a pocket adjacent to the nucleotide binding site
-
overview: electron microscopy, X-ray crystallography
-
structure of mutant R134K in a transition-state analogue complex. The functional enzyme dimer shows significant structural asymmetry with one monomer in a closed conformation with the active site occupied by the transition-state analogue components craetine, MgADP and nitrate. The other monomer has the two loops that control access to the active site in an open conformation and only MgADP is bound
-
overview: electron microscopy, X-ray crystallography
-
crystal structure analysis of muscle-type cytosolic isozyme crystallized with transition state analogue complex
-
in complex with a transistion-state analog
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
10.5
-
rapid inactivation above and below
6
8
-
calf brain enzyme stable, stability can be extended to pH 5.5-9 by addition of 0.01 M 2-mercaptoethanol
additional information
-
-
comparison of various enzymes of various sources
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
-
isozyme MiMi-CK: 1 h, 15% loss of activity, 2 h, 34% loss of activity, 3 h, 66% loss of activity, isozyme BB-CK: 6 h, 32% loss of activity, isozyme MM-CK: no loss of activity
35
-
-
calf brain: 0.01 M 2-mercaptoethanol enhances stability in pH-range 6-8
36
-
-
mutant D54G, melting temperature
37
-
-
isozyme MiMi-CK: 10 min, 30% loss of activity, 20 min, 62% loss of activity, 80 min, 75% loss of activity, isozyme MM-CK: 80 min, 75% loss of activity
37
-
P00563
inactivation of recombinant mutant R147A/R151A
37
-
-
midpoint temperature of thermal inactivation of mutant enzyme D54G is 36.5C
40
43
P00563
inactivation of recombinant mutant R151A
41
-
P00563
inactivation of recombinant mutant R147A
42.2
-
-
T0.5: 42.2C wild-type hBBCK
45
-
-
soluble enzyme: half-life 4 min, immobilized enzyme: half-life 35 min
45
-
-
20 min, 80% residual activity for sarcomeric isoform, 90% residual activity for ubiquotous isoform
45
-
-
20 min, 88.1% remaining activity of the atypical ubiquitous mitochondrial enzyme, 89.6% remaining activity of the typical ubiquitous mitochondrial enzyme
45
-
-
mutant G73A, inactivation
45
-
-
10 min, mutant enzyme D54G is completely inactivated
48
-
-
wild-type, stable up to 48C, mutant V75A, inactivation
48
-
-
10 min, the activity of wild-type enzyme has no significant changes after heat treatment at temperatures below 48C; wild-type, stable up to 48C
48
-
-
wild-type hBBCK gets completely inactivated above 48C
48
-
Q90X19
muscle-type creatine kinase of Danio rerio is less stable compared to human muscle-type creatine kinase, T0.5: 48C
51
-
-
inactivation above
51.9
-
-
melting temperature of mutant L110D
52
-
-
wild-type, melting temperature
52
-
-
T0.5: 52C hybrid form consisting of muscle and brain creatine kinase isoforms
52.3
-
-
melting temperature of wild-type
52.9
-
-
melting temperature of mutant L121D
53
55
P00563
inactivation of recombinant wild-type enzyme
53
-
-
midpoint temperature of thermal inactivation of wild-type enzyme is 52.5C
53.6
-
-
melting temperature of mutant L115D
56.9
-
-
muscle-type creatine kinase of Danio rerio is less stable compared to human muscle-type creatine kinase, T0.5: 56.9C
57.2
-
-
T0.5: 57.2C wild-type hMMCK
58
-
-
wild-type, inactivation
58
-
-
10 min, complete loss of activity above; wild-type, complete loss of activity
62
-
-
wild-type hMMCK gets completely inactivated above 62C
additional information
-
-
comparison of various enzymes of various sources
additional information
-
-
enzymes from marine fishes are less thermostable than that of carp, the latter being more labile than the rabbit enzyme
additional information
-
-
shark muscle isozyme marginally more resistant to temperature inactivation than brain isozyme
additional information
-
-
temperature stability profile of the isozymes CK-MM, CK-BB, and CK-MB, overview
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-mercaptoethanol enhances pH-stability
-
dimeric enzyme stable to 1-2 M urea
-
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
-
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 25C and pH 8.0
-
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
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freeze drying leads to oxidation of isozyme CK-BB
-
660931
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 20 mM sodium phosphate buffer, pH 8.0, 10% loss of activity in 2 weeks, faster inactivation in presence of dithiothreitol
-
-70C, 0.05 M Tris/barbital buffer, pH 7.8, 0.01 M 2-mercaptoethanol, 17% loss of activity in 6 weeks
-
4C, 10 mM MOPS buffer, pH 7.2, 2% v/v glycerol, 25 mM 2-mercaptoethanol, 0.1 mM EDTA, stable for more than 4 months
-
4C, octameric enzyme, protein concentration above 1 mg/ml, 1 mM 2-mercaptoethanol, 0.2 mM EDTA, 0.26 M NaCl, 25 mM sodium phosphate buffer, pH 7.0
-
liquid N2 preserves octameric stucture, dissociation to dimer at higher temperatures
-
4C, pH 7.0, 1 mM dithiothreitol or 14 mM 2-mercaptoethanol, at least 3 months
-
-17C, inactivation in presence of chloride or nitrate
-
freeze drying leads to oxidation of isozyme CK-BB and rearrangement of isozyme CK-MB
-
4C, several weeks
-
-10C, 5 mM Tris/HCl buffer, pH 8.7, 1 mM 2-mercaptoethanol, saturated ammonium sulfate solution
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 interconvertible forms of enzyme formed by reversible oxidation of sulfhydryl groups
-
overview
-
preparation of catalytically active hybrids of brain and muscle enzymes
-
isozyme MM-CK
-
recombinant full length enzyme and mature enzyme from Escherichia colito near homogeneity by affinity and cation exchange chromatography
-
cytosolic and mitochondrial isozymes from skeletal muscle by affinity chromatography
-
overview
-
partially preparation of mitochondria
-
isozyme Mia-CK
-
overview
-
5 varieties of isozyme MM-CK
-
overview
-
preparation of catalytically active hybrids of brain and muscle enzymes
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
typical ubiquitous mitochondrial enzyme from heart muscle tissue, atypical ubiquitous mitochondrial from serum
-
partially preparation of mitochondria
-
DEAE Sepharose column chromatography and Sephadex G-200 gel filtration
-
recombinant soluble monomeric or dimeric mutant enzymes by affinity chromatography, native enzyme from skeletal muscle, at high ionic strength, low temperature, and by fractionation with ethanol, or by affinity and ion exchange chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
isozyme MM-CK
-
overview
-
recombinant enzyme, inclusion bodies
-
partially preparation of mitochondria
-
isozyme CK-II, CK-III, CK-IV
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DNA and amino acid sequence determination and analysis, optimization of overexpression of full length enzyme and mature enzyme lacking the mitochondrial targeting sequence in Escherichia coli
-
expressed in Escherichia coli
Q90X19
brain isoform
-
expressed in Escherichia coli
-
expression in Escherichia coli, mostly in insoluble form, after optimization of the conditions the enzyme does not aggregate and shows multi-kinetic phases
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
overexpressed as a soluble form in Escherichia coli
-
expression of soluble monomeric or dimeric mutants
-
expression of soluble wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
overexpression of soluble wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), triple mutant enzyme R147A/R151A/D209A is expressed as insoluble, aggregated protein
P00563
expressed in Escherichia coli as a fusion protein with maltose-binding protein, mitochondrial isoform sMiCK; expressed in Escherichia coli as a fusion protein with maltose-binding protein, muscle-type isoform MCK
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
CKB mRNA and protein levels are significantly higher in probands affected with autosomal dominant inherited anomaly CKBE
-
high expression patterns at gastrulation and neurulation in ectoderm, high expression in somites from beginning of the tail-bud stage; high expression patterns at neurulation in somites
Q7ZYQ9, Q8AVH2
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A189D
Q90X19
Km and kcat values similar to wild-type, T0.5 (C): 46.2 (wild-type: 48.0C)
A205S
Q90X19
Km and kcat values similar to wild-type, T0.5 (C): 46.6 (wild-type: 48.0C)
E185Q
Q90X19
Km (ATP) and (creatine) significantly higher compared to wild-type, kcat value 74% of wild-type, T0.5 (C): 47.4 (wild-type: 48.0C)
H267A
Q90X19
Km and kcat values similar to wild-type, T0.5 (C): 47.6 (wild-type: 48.0C)
K36L
Q90X19
Km and kcat values similar to wild-type, T0.5 (C): 46.7 (wild-type: 48.0C)
N146C
Q90X19
Km and kcat values similar to wild-type, T0.5 (C): 51 (wild-type: 48.0C)
Q46E
Q90X19
Km and kcat values similar to wild-type, T0.5 (C): 50.9 (wild-type: 48.0C)
S329A
Q90X19
Km and kcat values similar to wild-type, T0.5 (C): 48.3 (wild-type: 48.0C)
T304K
Q90X19
Km and kcat values similar to wild-type, T0.5 (C): 47.6 (wild-type: 48.0C)
W264C
-
absoluteley conserved residue involved in octamer stability in most organisms, mutant forms dimers instead of octamers
W264Y
-
absoluteley conserved residue involved in octamer stability in most organisms, mutant forms dimers instead of octamers
A267H
-
Km and kcat values similar to wild-type, T0.5 (C): 56.9 (wild-type: 56.9C)
A329S
-
Km and kcat values similar to wild-type, T0.5 (C): 56.6 (wild-type: 56.9C)
C146N
-
Km and kcat values similar to wild-type, T0.5 (C): 52.4 (wild-type: 56.9C)
C283S/S285C
P12532
pKa value of active site cysteine increase by 1 pH unit
D189A
-
Km values 2-3fold decreased compared to wild-type, kcat 30% decreased compared to wild-type, T0.5 (C): 57 (wild-type: 56.9C)
D54G
-
mutation identified in acute myocardial infarction patient, mutant shows substantially decreased activity, substrate binding affinity and stability; the mutant enzyme has substantially decreased activity, substrate binding affinity and stability. Spectroscopic experiments indicate that the mutation impairs the structure of creatine kinase, which results in a partially unfolded state with more hydrophobic exposure and exposed Trp residues. The inability to fold to the functional compact state makes the mutant be prone to aggregate upon microenvironmental stresses, and might gradually decrease the creatine kinase level of the acute myocardial infarction patient
DeltaH65
-
affinity to substrates almost like wild type enzyme, very little stability
DeltaH65P66
-
8-fold decreased affinity for creatine phosphate
E226Q
-
catalytic site mutants which show no detectable creatine kinase activity demonstrate that enzymatic activity is not required for the regulation of NCX1 activity
E227L
-
catalytic site mutants which show no detectable creatine kinase activity demonstrate that enzymatic activity is not required for the regulation of NCX1 activity
E231Q
-
catalytic site mutants which show no detectable creatine kinase activity demonstrate that enzymatic activity is not required for the regulation of NCX1 activity
E232L
-
catalytic site mutants which show no detectable creatine kinase activity demonstrate that enzymatic activity is not required for the regulation of NCX1 activity
E46Q
-
Km values 2-3fold decreased compared to wild-type, kcat 30% decreased compared to wild-type, T0.5 (C): 50.1 (wild-type: 56.9C)
I69A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
I69L
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
I69V
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K304T
-
Km and kcat values similar to wild-type, T0.5 (C): 57.1 (wild-type: 56.9C)
P284A
P12532
pKa value of active site cysteine increase by 1.2 pH units
Q185E
-
Km values 2-3fold decreased compared to wild-type, kcat 30% decreased compared to wild-type, T0.5 (C): 56.4 (wild-type: 56.9C)
S123A
-
mutation analysis show that a putative PKC phosphorylation site on sMiCK and CKM is required for the regulation of NCX1 activity: S123A mutant fails to produce a recovery in the decreased NCX1 activity under energy-compromised conditions
S128A
-
mutation analysis show that a putative PKC phosphorylation site on sMiCK and CKM is required for the regulation of NCX1 activity: S123A mutant fails to produce a recovery in the decreased NCX1 activity under energy-compromised conditions
S205A
-
Km and kcat values similar to wild-type, T0.5 (C): 58.1 (wild-type: 56.9C)
S285A
P12532
pKa value of active site cysteine increase by 1 pH unit
T277V
-
autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity
T282V
-
autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity
T284V
-
autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity
T289V
-
autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity
T322V
-
autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity
T327V
-
autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity
V325A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme, mutant shows a slight preference for cyclocreatine, i.e. 1-carboxymethy-2-iminoimidazolidine, as substrate
A267H
-
at pH 7.1 mutant shows 30% higher specific activity than the wild-type at 35C, in contrast to mutant G268N this mutant shows no cold-adapted characteristics
A76G
-
mutation in the intra-subunit domain-domain interface, similar to wild-type in kinetics and thermal inactivation
C146S
-
enzyme preparation contains only reduced form
C254S
-
enzyme preparation contains both oxidized and reduced forms
C283S
-
enzyme preparation contains both oxidized and reduced forms
C74A
-
mutation in the intra-subunit domain-domain interface, no significant effect on activity and structure, decrease in stability and reactivation
C74L
-
mutation in the intra-subunit domain-domain interface, no significant effect on activity and structure, decrease in stability and reactivation
C74M
-
mutation in the intra-subunit domain-domain interface, no significant effect on activity and structure, decrease in stability and reactivation
C74S
-
mutation in the intra-subunit domain-domain interface, no significant effect on activity and structure, decrease in stability and reactivation
C74S
-
enzyme preparation contains only reduced form
D209A
P00563
site-directed mutagenesis, mutant enzyme appears as a mixture of monomeric and dimeric forms, the monomer shows higher thermolability and sensitivity aginst unfolding by 1-anilinonaphthalene-8-sulfonate due to a higher surface area
G286N
-
Km values of the rabbit creatine kinase G268N mutant are similar to those of the wild-type rabbit enzyme, circular dichroism spectra show that the overall secondary structures of the mutant enzyme, at pH 8.0 and 5 C, are almost identical to the carp M1-creatine kinase enzyme. At pH 7.4-8.0 and 35-10 C, with a smaller substrate, dADP, specific activities of the mutant enzyme are consistently higher than the wild-type rabbit enzyme. At pH 7.1 mutant shows 23% higher specific activity than the wild-type at 35C. At pH 7.7 and pH 8.0 at 10C mutant G268N exhibits 2 to 2.5fold higher specific activity than the wild-type, comparable to Cyprinus carpio M1-creatine kinase. Km and kcat values similar to wild-type
G73A
-
mutation in the intra-subunit domain-domain interface, decrease in activity and stability
L115D
-
gradual decrease in enzyme activity and secondary structures, mutation does not affect enzyme inactivation by heat or guanidine hydrochloride. Inactivated mutant cannot recover activity by dilution-initiated refolding
N285A
-
severe loss of activity
N285D
-
severe loss of activity, ordered binding mechanism
N285Q
-
severe loss of activity, random order mechanism, reduced affinity for second substrate
P20G
-
disruption of subunit cohesion, causing dissociation of the functional homodimer into monomers with reduced catalytic activity
P270G
-
at pH 7.1 mutant shows 30% higher specific activity than the wild-type at 35C, in contrast to mutant G268N this mutant shows no cold-adapted characteristics
R129A
-
site-directed mutagenesis, inactive mutant
R129K
-
site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme
R131A
-
site-directed mutagenesis, inactive mutant
R131K
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
R134K
-
highly soluble mutant, crystallization data
R147A
P00563
site-directed mutagenesis, mutant enzyme is a monomer showing higher thermolability and sensitivity aginst unfolding by 1-anilinonaphthalene-8-sulfonate due to a higher surface area, reduced activity and 89% reduced kcat compared to the wild-type enzyme, the mutant enzyme does not follow a random-order rapid-equilibrium mechanism like the wild-type enzyme, but to an ordered mechanism with creatine binding first
R147A/R151A
P00563
site-directed mutagenesis, double mutant enzyme is a monomer showing higher thermolability and sensitivity aginst unfolding by 1-anilinonaphthalene-8-sulfonate due to a higher surface area, 10fold reduced substrate binding and 40% reduced kcat compared to the wild-type enzyme, the mutant enzyme follows a random-order rapid-equilibrium mechanism like the wild-type enzyme
R147A/R151A/D209A
P00563
site-directed mutagenesis, the triple mutant enzyme is expressed as insoluble, aggregated protein
R151A
P00563
site-directed mutagenesis, mutant enzyme is a dimer, reduced activity compared to the wild-type enzyme
R235A
-
site-directed mutagenesis, inactive mutant
R235K
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
R291K
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
R319K
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
R340A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
R340K
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
R340Q
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
V72A
-
mutation in the intra-subunit domain-domain interface, decrease in activity and stability
V75A
-
mutation in the intra-subunit domain-domain interface, no significant effect on activity and structure, decrease in stability and reactivation
additional information
-
the Trp residue corresponding to Trp264 in chicken sarcomeric enzyme is absoluteley conserved in most organisms and involved in octamer stability. Mutation of this Trp residue to Cys, Tyr, His, Asn, or Phe produces only dimers
L36K
-
Km and kcat values similar to wild-type, T0.5 (C): 47.3 (wild-type: 56.9C)
additional information
-
expression of enzyme in Escherichia coli results in four different isoforms having similar kinetic parameters and identical bands on SDS-PAGE but different anodal mobility on non-denaturing gels. Cause of isoform formation may be deamidation of asparagine or glutamine residues
additional information
-
using chimeric mutants it is shown that C terminus of mitochondrial creatine kinase (sMiCK) and muscle creatine kinase (CKM) is required for the regulation of NCX1 activity
V325E
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme, mutant shows a more than 100fold higher preference for N-ethylglycocyamine as substrate compared to creatine, highly reduced activity with other substrates compared to the wild-type enzyme
additional information
-
transgenic mice lacking mitochondrial enzyme or both mitochondrial and cytoplasmic enzyme
additional information
-
enzyme knockout results in loss of hearing
L121D
-
gradual decrease in enzyme activity and secondary structures, mutation does not affect enzyme inactivation by heat or guanidine hydrochloride. Inactivated mutant cannot recover activity by dilution-initiated refolding
additional information
-
deletion of N-terminal 15 amino acids causes dissociation of the functional homodimer into monomers with reduced catalytic activity
additional information
-
fusion proteins of Stichopus japonicus arginine kinase and rabbit muscle creatine kinase in direction arginine kinase-creatine kinase, AK-CK and creatine kinase-arginine kinase, CK-AK. In both fusion proteins, both of the enzymes show about 50% decrease in activity and about 2fold Km values. Fused proteins have similar secondary structure, tertiary structure, molecular size, and thermodynamic stability
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
additional information
-
the enzyme from Tethya aurantia lacks the absoluteley conserved Trp residue, Trp264 in chicken sarcomeric enzyme, involved in octamer stability in most organisms and consequently forms dimers. Mutation of Tyr residue in the site corresponding to the conserved Trp in other organisms to Trp, His or Asn also yields dimers
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
reactivators are thiols, like N-acetylcysteine, beta-mercaptoethanol, dithiothreitol, monothioglycerol, glutathione
-
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
-
reactivation of 5,5'-dithiobis-(2-nitrobenzoic acid)-modified enzyme by excess of dithiothreitol, kinetics
-
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 17C. 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
-
dose- and time-dependent inhibition by cystine, cysteamine prevents and reverses this inhibition
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
possible roles in pathology
medicine
-
role of enzyme in severe left ventricular hypertrophy
biotechnology
-
use as biomarker of sperm cell membrane degradation
medicine
-
possible roles in pathology
diagnostics
-
enzyme is clinically important as an indicator of myocardial and skeletal muscle disorders and for the diagnosis of acute myocardial infarction
medicine
-
possible roles in pathology
medicine
-
enzyme properties relevant for analysis
medicine
-
levels of both free and protein-bound 4-hydroxy-2-nonenal are increased in alzheimers disease brain. 4-Hydroxy-2-nonenal inhibitis creatine kinase dose-dependently and forms adducts with specific amino acids including the active site residues H66, H191, C283, and H296
medicine
-
ethylmalonic acid accumulates in patients affected by short-chain acyl-CoA dehydrogenase deficiency and other diseases. Ethylmalonic acid inhibits the activity of respiratory chain complexes and also inhibits creatine kinase at concentrations o 1 mM and 5 mM and may therefore compromise energy metabolism in skeletal muscle
medicine
-
increased troponin I levels in the presence of rest pain and normal creatine kinase is not a spurious finding, but may actually be a marker of advanced coronary artery disease. However, some of these patients may also have nonsignificant coronary artery disease
medicine
-
mutations in the dysferlin gene cause several muscular dystrophy phenotypes including limb girdle 2B, Miyoshi myopathy, and distal anterior compartment myopathy. These disorders are characterized by autosomal recessive inheritance, early adult onset, and elevated levels of serum creatine kinase
medicine
-
transgenic mice lacking mitochondrial enzyme or both mitochondrial and cytoplasmic enzyme, myocardial energy-recruiting mechanims
biotechnology
-
stability of immobilized enzyme
medicine
-
possible roles in pathology
medicine
-
study on the effect of antipsychotics haloperidol, clozapine, olanzapine or aripiprazole chronic administration on creatine kinase in rat brain
medicine
-
neurotoxicitiy of L-arginine in hyperargininemia may in part be due to inhibition of creatine kinase
medicine
-
possible roles in pathology