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ADP + phosphocreatine
ATP + creatine
alpha-(RP)-borano-ADP + phosphocreatine
alpha-(RP)-borano-ATP + creatine
-
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
-
the SP-ADPalphaB isomer is a 70fold better substrate for creatine kinase than the RP isomer
-
-
?
ATP + creatine
ADP + creatine phosphate
ATP + creatine
ADP + phosphocreatine
ATP + cyclocreatine
ADP + phospho-cyclocreatine
ATP + glycocyamine
ADP + glycocyamine phosphate
ATP + glycocyamine
ADP + phosphoglycocyamine
ATP + N-ethylglycocyamine
ADP + N-ethylglycocyamine phosphate
dADP + phosphocreatine
?
-
-
-
-
?
additional information
?
-
ADP + phosphocreatine
ATP + creatine
-
-
-
-
r
ADP + phosphocreatine
ATP + creatine
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
-
-
-
-
r
ADP + phosphocreatine
ATP + creatine
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
-
-
-
-
r
ADP + phosphocreatine
ATP + creatine
-
-
-
r
ADP + phosphocreatine
ATP + creatine
-
-
-
r
ADP + phosphocreatine
ATP + creatine
-
-
-
r
ADP + phosphocreatine
ATP + creatine
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
-
synergistic substrate binding, mitochondrial isoform sMiCK
-
-
?
ADP + phosphocreatine
ATP + creatine
-
synergistic substrate binding, muscle-type isoform MCK
-
-
?
ADP + phosphocreatine
ATP + creatine
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
-
-
-
-
r
ADP + phosphocreatine
ATP + creatine
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
-
-
-
-
r
ADP + phosphocreatine
ATP + creatine
-
-
-
-
?
ADP + phosphocreatine
ATP + creatine
-
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
r
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
r
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
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
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
642382, 642394, 642397, 642398, 642399, 642402, 642406, 642407, 672307, 674788, 702414, 704042, 704051 -
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
r
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
creatine cannot be replaced by creatinine
-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
r
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
Mg-complexes of ATP and ADP are the true substrates for the mitochondrial enzymes
-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
r
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
r
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
-
?
ATP + creatine
ADP + creatine phosphate
trout
-
ATP required as MgATP2-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
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
-
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
the enzyme is involved in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
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
-
overview on physiological roles
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
?
ATP + creatine
ADP + phosphocreatine
the enzyme has a 20fold greater preference for creatine compared to glycocyamine
-
-
?
ATP + creatine
ADP + phosphocreatine
the enzyme shows a 20fold greater preference for creatine than glycocyamine
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
evolution of enzyme, phylogenetics
-
-
?
ATP + creatine
ADP + phosphocreatine
Frog
-
overview on physiological roles
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
mitochondrial model of CK in energy transport
-
-
r
ATP + creatine
ADP + phosphocreatine
-
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
-
overview on physiological roles
-
-
?
ATP + creatine
ADP + phosphocreatine
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
?, r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
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
-
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
-
the reaction equilibrium lies towards ATP production
-
-
r
ATP + creatine
ADP + phosphocreatine
-
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 + creatine
ADP + phosphocreatine
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
regeneration of ATP as primary energy source
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
?, r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
overview on physiological roles
-
-
?
ATP + creatine
ADP + phosphocreatine
the mitochondrial isozyme MtCK catalyzes the almost complete transphosphorylation of mitochondrial ATP and cytosolic creatine into ADP and phophocreatine. ADP locally generated by MtCK is transferred into the matrix for rephosphorylation and phosphocreatine is released from mitochondria into the cytosol, direct channelling of ATP and ADP between mitochondrial matrix and MtCK via adenine nucleotide transporter
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
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
-
overview on physiological roles
-
-
?
ATP + creatine
ADP + phosphocreatine
-
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
coupled to (Na+,K+)ATPase system
-
-
r
ATP + creatine
ADP + phosphocreatine
-
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
-
overview on physiological roles
-
-
?
ATP + creatine
ADP + phosphocreatine
-
key enzyme of energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
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
-
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
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + creatine
ADP + phosphocreatine
-
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
-
role in anaerobic metabolism
-
-
?
ATP + creatine
ADP + phosphocreatine
-
-
-
-
r
ATP + cyclocreatine
ADP + phospho-cyclocreatine
-
i.e. 1-carboxymethyl-2-iminoimidazolidine
-
-
?
ATP + cyclocreatine
ADP + phospho-cyclocreatine
i.e. 1-carboxymethyl-2-iminoimidazolidine
-
-
?
ATP + cyclocreatine
ADP + phospho-cyclocreatine
-
i.e. 1-carboxymethy-2-iminoimidazolidine
-
-
?
ATP + glycocyamine
ADP + glycocyamine phosphate
-
very low activity
-
-
?
ATP + glycocyamine
ADP + glycocyamine phosphate
very low activity
-
-
?
ATP + glycocyamine
ADP + glycocyamine phosphate
-
very low activity
-
-
?
ATP + glycocyamine
ADP + phosphoglycocyamine
-
-
-
?
ATP + glycocyamine
ADP + phosphoglycocyamine
-
-
-
?
ATP + N-ethylglycocyamine
ADP + N-ethylglycocyamine phosphate
-
-
-
-
?
ATP + N-ethylglycocyamine
ADP + N-ethylglycocyamine phosphate
-
-
-
?
ATP + N-ethylglycocyamine
ADP + N-ethylglycocyamine phosphate
-
-
-
-
?
additional information
?
-
-
probable enzyme evolution, overview
-
-
?
additional information
?
-
-
substrate binding structure, reaction equilibrium is highly influenced by pH and Mg2+ concentration, substrate specificity of isozymes
-
-
?
additional information
?
-
probable enzyme evolution, overview
-
-
?
additional information
?
-
substrate binding structure, reaction equilibrium is highly influenced by pH and Mg2+ concentration, substrate specificity of isozymes
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
membrane proteins VAMP2/3 and JWA are putative BCK interaction partners. At the plasma membrane, BCK interacts with at least two members of the family of cation-coupled chloride transporters (solute carrier family 12): the K+/Cl- cotransporters 2 (KCC2 or SLC12A5) and 3 (KCC3 or SLC12A6), BCK may be required for maximal phosphorylation efficiency
-
-
?
additional information
?
-
membrane proteins VAMP2/3 and JWA are putative BCK interaction partners. At the plasma membrane, BCK interacts with at least two members of the family of cation-coupled chloride transporters (solute carrier family 12): the K+/Cl- cotransporters 2 (KCC2 or SLC12A5) and 3 (KCC3 or SLC12A6), BCK may be required for maximal phosphorylation efficiency
-
-
?
additional information
?
-
the enzyme binds to 1,2-dipalmitoyl-sn-glycero-3-phosphate with the highest affinity (dissociation constant: 0.002 mM)
-
-
-
additional information
?
-
-
the enzyme binds to 1,2-dipalmitoyl-sn-glycero-3-phosphate with the highest affinity (dissociation constant: 0.002 mM)
-
-
-
additional information
?
-
the enzyme binds to 1,2-dipalmitoyl-snglycero-3-phosphate with the highest affinity (dissociation constant 0.002 mM). The enzyme preferentially interacts with saturated fatty acid- and/or monounsaturated fatty acid-containing phosphatidic acids, but not with polyunsaturated fatty acid-containing phosphatidic acids
-
-
-
additional information
?
-
-
the enzyme binds to 1,2-dipalmitoyl-snglycero-3-phosphate with the highest affinity (dissociation constant 0.002 mM). The enzyme preferentially interacts with saturated fatty acid- and/or monounsaturated fatty acid-containing phosphatidic acids, but not with polyunsaturated fatty acid-containing phosphatidic acids
-
-
-
additional information
?
-
-
probable enzyme evolution, overview
-
-
?
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
?
-
-
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
?
-
-
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
?
-
synaptical vesicle protein VAMP2/3 and membrane protein and JWA are BCK interaction partners, by Y2H assays. VAMP3 interacts with both, wild-type BCK and truncated DELTABCK mutant. The common and characteristic SNARE domain of VAMPs (amino acids 14-74 in VAMP3) is not sufficient for BCK interaction. JWA and VAMP both link BCK to energy-requiring intracellular vesicle transport
-
-
?
additional information
?
-
synaptical vesicle protein VAMP2/3 and membrane protein and JWA are BCK interaction partners, by Y2H assays. VAMP3 interacts with both, wild-type BCK and truncated DELTABCK mutant. The common and characteristic SNARE domain of VAMPs (amino acids 14-74 in VAMP3) is not sufficient for BCK interaction. JWA and VAMP both link BCK to energy-requiring intracellular vesicle transport
-
-
?
additional information
?
-
-
probable enzyme evolution, overview
-
-
?
additional information
?
-
-
substrate binding structure, substrate binding at both subunits
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-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
1-anilinonaphthalene-8-sulfonate
unfolding agent
2,3-butadiene
-
complete inhibition, MgATP2- or MgADP- protect the enzyme from inactivation
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-(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
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
Cd2+
-
Cd2+ conspicuously inactivates the activity of the muscle-type enzyme in a first-order kinetic process and exhibits non-competitive inhibition with creatine and ATP. Cd2+ induces tertiary structure changes in enzyme PSCKM with exposure of hydrophobic surfaces. The addition of osmolytes, such as glycine and proline, partially reactivates the enzyme. Molecular dynamics and docking simulations between PSCKM and Cd2+ show that Cd2+ blocks the entrance of ATP to the active site of the enzyme, computational modeling, overview
Chromium ADP
-
competitive to MgADP-
Chromium ATP
-
competitive to MgATP2-
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
-
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
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
Guanidinoacetate
-
vitamins E and C prevent the effects of intrastriatal administration of guanidinoacetate on the inhibition of creatine kinase
H2O2
irreversible inhibition. H2O2 interacts with the ADP binding region of the active site of the enzyme. Enzymatic activity is rapidly abolished with less than 1 mM H2O2. Any residual activity is completely lost at an H2O2 concentration of 2-10 mM; irreversible inhibition. The enzyme activity rapidly abolishes with less than 1 mM H2O2. Any residual activity is completely lost at an H2O2 concentration of 2-10 mM. Adding reducing agents such as 2 mM dithiothreitol, 4 mM N-acetyl-l-cysteine, or 4 mM reduced L-glutathione before H2O2 treatment prevents against inactivation caused by 0.5 mM H2O2. However, if antioxidants are added 1 h after addition of 0.5 mM H2O2, no recovery is observed compared with the H2O2-treated group
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 25°C or 40°C even at high protein concentrations, inactivation kinetics
LiCl
-
inactivation due to subunit dissociation, mechanism
MOPS buffer
-
i.e. 3-(N-morpholino)propane sulfonate
morphine
0.00001-0.1 mM morphine significantly reduces recombinant enzymatic activity (27% inhibition at 0.001 mM, 80% inhibition at more than 0.05 mM); 27% inhibition at 0.001 m, 80% inhibition at more than 0.05 mM
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
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
thiosulfate
-
0.5 mM thiosulfate administration decreases the enzyme activity 30 min after administration. Thiosulfate also decreases the activity of the enzyme in vitro in striatum of rats, which is prevented by the thiol reducing agents dithiothreitol, the antioxidants glutathione, melatonin, trolox, and lipoic acid; thiosulfate (1 M) inhibits creatine kinase activity in rat striatum via thiol group oxidation is prevented by the thiol reducing agents dithiothreitol GSH, melatonin, trolox and lipoic acid
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
-
4-hydroxymercuribenzoic acid
-
complete inhibition at 0.01 mM
4-hydroxymercuribenzoic acid
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
less than 5% residual activity at 0.1 mM
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
Cl-
-
-
Cl-
-
inactivation at -17°C
Co2+
-
-
Creatinine phosphate
-
competitive to phosphocreatine
Creatinine phosphate
-
competitive to MgATP2-
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
-
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
formate
-
mimics the phosphoryl group in the transition state
formate
mimics the phosphoryl group in the transition state
formate
-
mimics the phosphoryl group in the transition state
formate
-
mimics the phosphoryl group in the transition state
formate
-
mimics the phosphoryl group in the transition state
guanidinium hydrochloride
0.1-3.0 M, under both conditions, the tag-free enzyme shows the lowest degree of aggregation, followed by His-tagged CK, and Fc-III-tagged CK has the highest degree of aggregation
guanidinium hydrochloride
inactivation mechanism of wild-type and mutant enzymes, overview
guanidinium hydrochloride
-
first dissociation of subunits, then unfolding into random coil
iodoacetamide
-
substrates can protect against alkylation
iodoacetamide
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
-
substrates can protect against alkylation
iodoacetamide
-
protection by MgATP2-, MgADP-, urea
iodoacetamide
-
substrates can protect against alkylation
iodoacetic acid
-
-
jujubogenin
16.9% inhibition at 0.005 mM
-
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
mimics the phosphoryl group in the transition state
nitrate
-
mimics the phosphoryl group in the transition state
nitrate
-
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
mimics the phosphoryl group in the transition state
nitrite
-
mimics the phosphoryl group in the transition state
nitrite
-
mimics the phosphoryl group in the transition state
nitrite
-
mimics the phosphoryl group in the transition state
NO3-
-
-
NO3-
-
inactivation at -17°C
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
SDS
-
dissociation of subunits, no unfolding
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+
-
Zn2+ may induce CK-BB inactivation and misfolding, when the Zn2+ concentration is 0.4 mM, CK-BB activity is completely abolished
additional information
-
transition state analogue complex substrates inhibit the dimeric but not the octameric enzyme; transition state analogue complex substrates inhibit the dimeric but not the octameric enzyme
-
additional information
transition state analogue complex substrates inhibit the dimeric but not the octameric enzyme; transition state analogue complex substrates inhibit the dimeric but not the octameric enzyme
-
additional information
-
lansoprazole at 0.003 mg/ml does not alter DNA integrity of human spermatozoa or activity of seminal creatine kinase after 1 h incubation period; there is no significant change in the activity of seminal creatine kinase by the effect of lansoprazole (0.003 mg/ml, 1 h incubation)
-
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
-
additional information
-
brain creatine kinase activity is lower on days 14 and 21 post-feeding in animals that receive aflatoxin B1-contaminated diet compared to the control group. The inhibition of brain enzyme activity appears to be mediated by the oxidation of lipids, proteins, and thiol group, as well as by a reduction in the antioxidant capacity
-
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1
alpha-(RP)-borano substituted ADP
-
-
0.008
alpha-(SP)-borano substituted ADP
-
-
0.23 - 50
creatine phosphate
6.7
glycocyamine
at pH 8.5 and 25°C
0.51 - 8.97
phosphocreatine
additional information
additional information
-
0.015
ADP
-
30°C
0.015
ADP
-
ADP in form of MgADP-
0.017
ADP
-
pH 7.4, dimeric form
0.017
ADP
-
ADP in form of MgADP-
0.03
ADP
-
pH 7.0, muscle-type cytosolic isozyme
0.04
ADP
-
pH 7.0, brain-type cytosolic isozyme
0.043
ADP
-
pH 7.4, octameric form
0.043
ADP
-
ADP in form of MgADP-
0.051 - 0.052
ADP
-
30°C, pH 7.4
0.051 - 0.052
ADP
-
ADP in form of MgADP-
0.13
ADP
-
pH 7.0, ubiquitous mitochondrial isozyme
0.15
ADP
-
pH 7.0, ubiquitous mitochondrial isozyme
0.15
ADP
-
ADP in form of MgADP-
0.22
ADP
-
acetylcholine receptor membrane-asscociated enzyme
0.22
ADP
-
ADP in form of MgADP-
0.54
ADP
-
soluble enzyme from muscle
0.54
ADP
-
ADP in form of MgADP-
1.2
ADP
-
ADP in form of MgADP-
0.042
ATP
-
pH 7.4, dimeric form
0.042
ATP
-
ATP in form of MgATP2-
0.056
ATP
-
ATP in form of MgATP2-
0.082
ATP
-
pH 7.4, octameric form
0.082
ATP
-
ATP in form of MgATP2-
0.11
ATP
-
25°C, pH 8.0, ubiquitous mitochondrial isoform
0.11
ATP
-
pH 8.0, ubiquitous mitochondrial isozyme
0.2
ATP
-
cytoplasmic isoform M1, 25°C
0.22
ATP
pH 9.0, 30°C, recombinant wild-type enzyme, with substrate creatine
0.22
ATP
ATP in form of MgATP2-
0.29
ATP
pH 9.0, 30°C, recombinant wild-type enzyme, with substrate cyclocreatine
0.29
ATP
ATP in form of MgATP2-
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, 25°C
0.34
ATP
-
isoform III isolated after expression in Escherichia coli, pH 8.0, 30°C
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, 30°C
0.36
ATP
25°C, 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 and isoform I isolated after expression in Escherichia coli, pH 8.0, 30°C
0.42
ATP
25°C, pH not specified in the publication, mutant S329A
0.43
ATP
-
isoform IV isolated after expression in Escherichia coli, pH 8.0, 30°C
0.43
ATP
mutant C74A, 25°C
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
25°C, pH not specified in the publication, mutant N146C
0.46
ATP
-
wild-type enzyme
0.46
ATP
mutant A76G, 25°C
0.47
ATP
mutant C74S, 25°C
0.49
ATP
25°C, pH not specified in the publication, wild-type
0.51
ATP
mutant V72A, 25°C
0.56
ATP
wild type enzyme, at pH 8.0 and 25°C
0.56
ATP
recombinant wild type enzyme, at 25°C, pH not specified in the publication
0.57
ATP
mutant V75A, 25°C
0.58
ATP
25°C, pH not specified in the publication, mutant A205S
0.58
ATP
25°C, pH not specified in the publication, mutant Q46E
0.62
ATP
pH 9.0, 30°C, recombinant wild-type enzyme, with substrate N-ethylglycocyamine
0.62
ATP
25°C, pH not specified in the publication, mutant H267A
0.62
ATP
-
25°C, pH not specified in the publication, wild-type
0.62
ATP
ATP in form of MgATP2-
0.65
ATP
-
cytoplasmic isoform B, 25°C
0.65
ATP
-
25°C, pH not specified in the publication, mutant S205A
0.66
ATP
mutant C74M, 25°C
0.68
ATP
-
25°C, pH 8.0, sarcomeric mitochondrial isoform
0.68
ATP
-
pH 8.0, ubiquitous mitochondrial isozyme
0.68
ATP
-
25°C, euthermic squirrel
0.68
ATP
mutant G73A, 25°C
0.7
ATP
-
pH 9.0, 30°C, recombinant wild-type enzyme
0.7
ATP
-
cytoplasmic isoform M1, 25°C
0.7
ATP
mutant C74L, 25°C
0.7
ATP
-
ATP in form of MgATP2-
0.73
ATP
-
fusion protein CK-AK
0.73
ATP
-
25°C, pH not specified in the publication, mutant A267H
0.73
ATP
-
ATP in form of MgATP2-
0.74
ATP
-
25°C, pH not specified in the publication, mutant K304T
0.74
ATP
-
25°C, pH not specified in the publication, mutant L36K
0.75
ATP
-
cytoplasmic isoform M, 25°C
0.79
ATP
-
25°C, myosin bound enzyme
0.8
ATP
-
cytoplasmic isoform M1, 25°C
0.8
ATP
-
cytoplasmic isoform M2, 25°C
0.8
ATP
in form of Mg-ATP, at pH 8.5 and 25°C
0.81
ATP
-
pH 9.0, brain-type cytosolic isozyme
0.82
ATP
25°C, pH not specified in the publication, mutant A189D
0.84
ATP
-
25°C, pH not specified in the publication, mutant D189A
0.85
ATP
25°C, 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, 25°C
0.91
ATP
-
25°C, pH not specified in the publication, mutant C146N
0.92
ATP
25°C, pH not specified in the publication, mutant E185Q
1
ATP
-
cytoplasmic isoform B, 25°C
1
ATP
-
cytoplasmic isoform M2, 25°C
1.09
ATP
-
25°C, pH not specified in the publication, mutant E46Q
1.1
ATP
-
pH 9.0, 30°C, recombinant mutant R340K
1.1
ATP
-
ATP in form of MgATP2-
1.14
ATP
recombinant mutant enzyme D326E, at 25°C, pH not specified in the publication
1.14
ATP
mutant enzyme D326E, at pH 8.0 and 25°C
1.18
ATP
-
25°C, hibernating squirrel
1.24
ATP
-
25°C, pH not specified in the publication, mutant Q185E
1.35
ATP
-
mitochondrial isoform M2, 25°C
1.37
ATP
-
0.020 mM organotellurium, preincubation time 5 min, mitochondrial fraction, pH 7.5, 37°C
1.38
ATP
-
0.005 mM organotellurium, preincubation time 5 min, mitochondrial fraction, pH 7.5, 37°C
1.38
ATP
-
25°C, pH not specified in the publication, mutant A329S
1.4
ATP
recombinant mutant enzyme H66R, at 25°C, pH not specified in the publication
1.4
ATP
mutant enzyme H66R, at pH 8.0 and 25°C
1.6
ATP
-
pH 9.0, 30°C, recombinant mutant R291K
1.6
ATP
-
pH 9.0, 30°C, recombinant mutant R340A
1.6
ATP
-
ATP in form of MgATP2-
1.6
ATP
-
ATP in form of MgATP2-
1.7
ATP
-
ATP in form of MgATP2-
1.7
ATP
in form of Mg-ATP, at pH 8.5 and 25°C
1.75
ATP
-
no organotellurium, preincubation time 30 min, cytosolic fraction, pH 7.5, 37°C
1.94
ATP
-
0.005 mM organotellurium, preincubation time 30 min, mitochondrial fraction, pH 7.5, 37°C
2.03
ATP
-
0.020 mM organotellurium, preincubation time 30 min, cytosolic fraction, pH 7.5, 37°C
2.1
ATP
-
0.005 mM organotellurium, preincubation time 30 min, cytosolic fraction, pH 7.5, 37°C
2.1
ATP
-
no organotellurium, preincubation time 5 min, mitochondrial fraction, including reduced glutathione (GSH), pH 7.5, 37°C
2.2
ATP
-
mutant enzyme D54G
2.49
ATP
-
0.020 mM organotellurium, preincubation time 30 min, mitochondrial fraction, pH 7.5, 37°C
2.82
ATP
-
no organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37°C
2.84
ATP
-
0.005 mM organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37°C
3.15
ATP
-
no organotellurium, preincubation time 30 min, mitochondrial fraction, pH 7.5, 37°C
3.19
ATP
-
no organotellurium, preincubation time 5 min, cytosolic fraction, including reduced glutathione (GSH), pH 7.5, 37°C
3.55
ATP
-
no organotellurium, preincubation time 5 min, mitochondrial fraction, pH 7.5, 37°C
3.6
ATP
-
pH 9.0, 30°C, recombinant mutant R235K
3.6
ATP
-
ATP in form of MgATP2-
3.92
ATP
-
0.020 mM organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37°C
3.98
ATP
recombinant mutant enzyme D326A, at 25°C, pH not specified in the publication
3.98
ATP
mutant enzyme D326A, at pH 8.0 and 25°C
4.98
ATP
recombinant mutant enzyme H66P, at 25°C, pH not specified in the publication
4.98
ATP
mutant enzyme H66P, at pH 8.0 and 25°C
5.3 - 6
ATP
-
0.005 mM organotellurium, preincubation time 5 min, mitochondrial fraction, including reduced glutathione (GSH), pH 7.5, 37°C
6.68
ATP
-
0.005 mM organotellurium, preincubation time 5 min, cytosolic fraction, including reduced glutathione (GSH), pH 7.5, 37°C
7.3
ATP
-
pH 9.0, 30°C, recombinant mutant R340Q
7.3
ATP
-
ATP in form of MgATP2-
8.96
ATP
recombinant mutant enzyme H66P/D326A, at 25°C, pH not specified in the publication
8.96
ATP
mutant enzyme H66P/D326A, at pH 8.0 and 25°C
9.38
ATP
-
mitochondrial isoform sMiCK
10.3
ATP
-
pH 9.0, 30°C, recombinant mutant R129A
10.3
ATP
-
ATP in form of MgATP2-
17.52
ATP
-
0.020 mM organotellurium, preincubation time 5 min, cytosolic fraction, including reduced glutathione (GSH), pH 7.5, 37°C
20
ATP
-
0.020 mM organotellurium, preincubation time 5 min, mitochondrial fraction, including reduced glutathione (GSH), pH 7.5, 37°C
0.35
Creatine
-
mitochondrial isoform, 25°C
0.69
Creatine
-
37°C, atypical ubiquitous mitochondrial enzyme
0.74
Creatine
-
37°C, typical ubiquitous mitochondrial enzyme
1.01
Creatine
-
25°C, pH 8.0, ubiquitous mitochondrial isoform
1.01
Creatine
-
pH 8.0, ubiquitous mitochondrial isozyme
1.2
Creatine
-
25°C, myosin bound enzyme
1.5
Creatine
-
cytoplasmic isoform B, 25°C
1.62
Creatine
-
25°C, euthermic squirrel
2
Creatine
at pH 8.5 and 25°C
2 - 3
Creatine
-
isoform I isolated after expression in Escherichia coli, pH 8.0, 30°C
2 - 3.4
Creatine
-
25°C, pH not specified in the publication, mutant A329S
2.06
Creatine
-
25°C, hibernating squirrel
2.5
Creatine
-
soluble enzyme from muscle
2.7
Creatine
-
cytoplasmic isoform B, 25°C
2.8
Creatine
mutant L110D
3.1
Creatine
mutant L115D
3.26
Creatine
-
enzyme from embryonic stem cell-derived cardiomyocytes, pH 6.5, 37°C
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
4.7
Creatine
-
cytoplasmic isoform M, 25°C
4.9
Creatine
-
pH 9.0, brain-type cytosolic isozyme
4.9 - 5
Creatine
-
30°C, pH 7.4
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, 37°C
5.9
Creatine
-
25°C, pH not specified in the publication, wild-type
6.2
Creatine
-
wild-type hMMCK, pH and temperature not specified in the publication
6.6
Creatine
-
25°C, pH not specified in the publication, mutant S205A
7.1
Creatine
-
25°C, pH not specified in the publication, mutant L36K
7.31
Creatine
-
25°C, pH 8.0, sarcomeric mitochondrial isoform
7.31
Creatine
-
pH 8.0, ubiquitous mitochondrial isozyme
8.1
Creatine
-
pH 7.4, octameric form
8.2
Creatine
-
pH 9.0, 30°C, 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, 25°C
8.7
Creatine
-
25°C, pH not specified in the publication, mutant A267H
8.9
Creatine
mutant A76G, 25°C
8.9
Creatine
-
25°C, pH not specified in the publication, mutant K304T
9
Creatine
-
pH 9.0, 30°C, recombinant wild-type enzyme
9
Creatine
mutant C74S, 25°C
9.1
Creatine
wild-type, 25°C
9.15
Creatine
wild type enzyme, at pH 8.0 and 25°C
9.15
Creatine
recombinant wild type enzyme, at 25°C, pH not specified in the publication
9.5
Creatine
-
pH 9.0, muscle-type cytosolic isozyme
9.6
Creatine
-
wild-type enzyme
10.5
Creatine
25°C, pH not specified in the publication, mutant S329A
10.8
Creatine
-
cytoplasmic isoform M1, 25°C
11
Creatine
25°C, pH not specified in the publication, mutant N146C
11.1
Creatine
-
25°C, pH not specified in the publication, mutant Q185E
11.2
Creatine
-
cytoplasmic isoform M2, 25°C
12.9
Creatine
-
25°C, pH not specified in the publication, mutant C146N
13
Creatine
-
fusion protein CK-AK
13.8
Creatine
mutant V75A, 25°C
14
Creatine
-
fusion protein AK-CK
14.2
Creatine
25°C, pH not specified in the publication, wild-type
14.5
Creatine
-
cytoplasmic isoform M1, 25°C
14.8
Creatine
-
25°C, pH not specified in the publication, mutant E46Q
16.7
Creatine
25°C, pH not specified in the publication, mutant H267A
17.1
Creatine
25°C, pH not specified in the publication, mutant Q46E
17.8
Creatine
25°C, pH not specified in the publication, mutant T304K
18.3
Creatine
mutant C74M, 25°C
18.6
Creatine
mutant C74L, 25°C
19
Creatine
-
pH 9.0, 30°C, recombinant mutant R340K
19
Creatine
-
isoform II isolated after expression in Escherichia coli, pH 8.0, 30°C
19.28
Creatine
recombinant mutant enzyme D326E, at 25°C, pH not specified in the publication
19.28
Creatine
mutant enzyme D326E, at pH 8.0 and 25°C
20
Creatine
-
isoform III isolated after expression in Escherichia coli, pH 8.0, 30°C
20.2
Creatine
-
mitochondrial isoform M2, 25°C
20.6
Creatine
-
25°C, pH not specified in the publication, mutant D189A
20.8
Creatine
25°C, pH not specified in the publication, mutant A205S
21
Creatine
-
wild-type and isoform IV isolated after expression in Escherichia coli, pH 8.0, 30°C
21.4
Creatine
mutant V72A, 25°C
21.6
Creatine
25°C, pH not specified in the publication, mutant K36L
23.5
Creatine
-
cytoplasmic isoform M1, 25°C
24.11
Creatine
recombinant mutant enzyme H66R, at 25°C, pH not specified in the publication
24.11
Creatine
mutant enzyme H66R, at pH 8.0 and 25°C
25
Creatine
mutant G73A, 25°C
25.5
Creatine
-
mitochondrial isoform M2, 25°C
26.38
Creatine
-
pH 9.0, 20°C
26.4
Creatine
-
cytoplasmic isoform M2, 25°C
28.5
Creatine
25°C, pH not specified in the publication, mutant A189D
34
Creatine
-
mutant D54G
34
Creatine
-
mutant enzyme D54G
44.1
Creatine
25°C, pH not specified in the publication, mutant E185Q
72
Creatine
-
pH 9.0, 30°C, recombinant mutant R235K
76
Creatine
-
pH 9.0, 30°C, recombinant mutant R291K
79.88
Creatine
recombinant mutant enzyme D326A, at 25°C, pH not specified in the publication
79.88
Creatine
mutant enzyme D326A, at pH 8.0 and 25°C
87.12
Creatine
recombinant mutant enzyme H66P, at 25°C, pH not specified in the publication
87.12
Creatine
mutant enzyme H66P, at pH 8.0 and 25°C
156.44
Creatine
recombinant mutant enzyme H66P/D326A, at 25°C, pH not specified in the publication
156.44
Creatine
mutant enzyme H66P/D326A, at pH 8.0 and 25°C
163
Creatine
-
pH 9.0, 30°C, recombinant mutant R340Q
167
Creatine
-
pH 9.0, 30°C, recombinant mutant R129A
0.23
creatine phosphate
-
pH 7.4, dimeric form
0.31
creatine phosphate
-
30°C
0.4
creatine phosphate
-
-
0.4
creatine phosphate
-
pH 7.0, 25°C
0.49 - 0.5
creatine phosphate
-
30°C, pH 7.4
0.68
creatine phosphate
-
pH 7.4, octameric form
1.07
creatine phosphate
-
37°C, ubiquitous isoform
1.19
creatine phosphate
-
37°C, sarcomeric isoform
1.9 - 2.2
creatine phosphate
-
-
1.9 - 2.2
creatine phosphate
-
acetylcholine receptor membrane-associated enzyme
2 - 10.6
creatine phosphate
-
-
2 - 10.6
creatine phosphate
-
-
2 - 10.6
creatine phosphate
-
-
3.7
creatine phosphate
-
30°C
17
creatine phosphate
-
0.5°C, pH 7.6
50
creatine phosphate
-
-
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, 37°C
0.67
phosphocreatine
-
no organotellurium, preincubation time 5 min, mitochondrial fraction, including reduced glutathione (GSH), pH 7.5, 37°C
0.7
phosphocreatine
-
0.020 mM organotellurium, preincubation time 5 min, mitochondrial fraction, including reduced glutathione (GSH), pH 7.5, 37°C
0.8
phosphocreatine
-
pH 7.5, 37°C
0.87
phosphocreatine
-
no organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37°C
1.11
phosphocreatine
-
no organotellurium, preincubation time 5 min, cytosolic fraction, including reduced glutathione (GSH), pH 7.5, 37°C
1.15
phosphocreatine
-
0.005 mM organotellurium, preincubation time 5 min, cytosolic fraction, including reduced glutathione (GSH), pH 7.5, 37°C
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, 37°C
1.33
phosphocreatine
-
pH 7.0, muscle-type cytosolic isozyme
1.34
phosphocreatine
-
no organotellurium, preincubation time 5 min, mitochondrial fraction, pH 7.5, 37°C
1.41
phosphocreatine
-
0.020 mM organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37°C
1.72
phosphocreatine
-
0.020 mM organotellurium, preincubation time 5 min, cytosolic fraction, including reduced glutathione (GSH), pH 7.5, 37°C
1.73
phosphocreatine
-
0.005 mM organotellurium, preincubation time 5 min, mitochondrial fraction, pH 7.5, 37°C
2.04
phosphocreatine
-
0.020 mM organotellurium, preincubation time 5 min, mitochondrial fraction, pH 7.5, 37°C
3.26
phosphocreatine
-
0.005 mM organotellurium, preincubation time 30 min, cytosolic fraction, pH 7.5, 37°C
3.34
phosphocreatine
-
0.020 mM organotellurium, preincubation time 30 min, cytosolic fraction, pH 7.5, 37°C
3.54
phosphocreatine
-
no organotellurium, preincubation time 30 min, cytosolic fraction, pH 7.5, 37°C
5.77
phosphocreatine
-
0.005 mM organotellurium, preincubation time 30 min, mitochondrial fraction, pH 7.5, 37°C
6.43
phosphocreatine
-
0.020 mM organotellurium, preincubation time 30 min, mitochondrial fraction, pH 7.5, 37°C
8.97
phosphocreatine
-
no organotellurium, preincubation time 30 min, mitochondrial fraction, pH 7.5, 37°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
overview
-
additional information
additional information
-
overview
-
additional information
additional information
-
overview
-
additional information
additional information
-
overview
-
additional information
additional information
-
overview
-
additional information
additional information
-
overview
-
additional information
additional information
-
overview
-
additional information
additional information
-
overview
-
additional information
additional information
-
effect of temperature on values for MgATP2- and creatine
-
additional information
additional information
-
dextran strongly increases Km
-
additional information
additional information
-
temperature dependence of reaction, in vivo measurements
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetic mechanism, 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 for ADP in mitochondria, enhancing effect of creatine, overview
-
additional information
additional information
-
kinetics for ADP in mitochondria, enhancing effect of creatine, overview
-
additional information
additional information
-
kinetics for ADP in mitochondria, enhancing effect of creatine, overview
-
additional information
additional information
-
kinetics, negative cooperativity
-
additional information
additional information
kinetics, recombinant wild-type and mutant enzymes
-
additional information
additional information
-
kinetics, recombinant wild-type and mutant enzymes
-
additional information
additional information
-
kinetics, 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, the enzyme shows negative cooperativity and nonidentical active sites
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.06
alpha-(RP)-borano substituted ADP
-
-
0.03
alpha-(SP)-borano substituted ADP
-
-
0.5
glycocyamine
at pH 8.5 and 25°C
0.55 - 14.5
N-ethylglycocyamine
78.3 - 483.3
phosphocreatine
additional information
additional information
-
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
0.08
ATP
-
pH 9.0, 30°C, recombinant mutant R129A
0.08
ATP
-
ATP in form of MgATP2-
0.54
ATP
-
pH 9.0, 30°C, recombinant mutant R235K
0.54
ATP
-
ATP in form of MgATP2-
1.33
ATP
-
pH 9.0, 30°C, recombinant mutant R340Q
1.33
ATP
-
ATP in form of MgATP2-
2.14
ATP
-
pH 9.0, 30°C, recombinant mutant R340A
2.14
ATP
-
ATP in form of MgATP2-
2.18
ATP
-
pH 9.0, 30°C, recombinant mutant R291K
2.18
ATP
-
ATP in form of MgATP2-
28.99
ATP
recombinant mutant enzyme H66P/D326A, at 25°C, pH not specified in the publication
36.4
ATP
-
muscle-type isoform MCK
38.4
ATP
-
mitochondrial isoform sMiCK
50.1
ATP
-
pH 9.0, 30°C, recombinant mutant R340K
50.1
ATP
-
ATP in form of MgATP2-
51.7
ATP
-
pH 8.0, ubiquitous mitochondrial isozyme
62.15
ATP
recombinant mutant enzyme H66P, at 25°C, pH not specified in the publication
67.78
ATP
recombinant mutant enzyme D326A, at 25°C, pH not specified in the publication
75
ATP
-
pH 8.0, ubiquitous mitochondrial isozyme
76
ATP
-
isoform II isolated after expression in Escherichia coli, pH 8.0, 30°C
88
ATP
-
isoform IV isolated after expression in Escherichia coli, pH 8.0, 30°C
115
ATP
-
isoform III isolated after expression in Escherichia coli, pH 8.0, 30°C
136.21
ATP
recombinant mutant enzyme H66R, at 25°C, pH not specified in the publication
143
ATP
-
wild-type, pH 8.0, 30°C
148
ATP
-
pH 9.0, 30°C, recombinant wild-type enzyme
148
ATP
-
ATP in form of MgATP2-
153.5
ATP
-
pH 9.0, muscle-type cytosolic isozyme
155
ATP
-
isoform I isolated after expression in Escherichia coli, pH 8.0, 30°C
157.66
ATP
recombinant mutant enzyme D326E, at 25°C, pH not specified in the publication
177.66
ATP
recombinant wild type enzyme, at 25°C, pH not specified in the publication
215
ATP
-
pH 9.0, brain-type cytosolic isozyme
0.08
Creatine
-
pH 9.0, 30°C, recombinant mutant R129A
0.54
Creatine
-
pH 9.0, 30°C, recombinant mutant R235K
1.33
Creatine
-
pH 9.0, 30°C, recombinant mutant R340Q
2.14
Creatine
-
pH 9.0, 30°C, recombinant mutant R340A
2.18
Creatine
-
pH 9.0, 30°C, recombinant mutant R291K
4.2
Creatine
pH 9.0, 30°C, recombinant mutant I69A
4.5
Creatine
-
mitochondrial isoform, 25°C
12.5
Creatine
-
cytoplasmic isoform M2, 25°C
13.1
Creatine
-
cytoplasmic isoform B, 25°C
14.7
Creatine
-
cytoplasmic isoform M1, 25°C
15
Creatine
-
mitochondrial isoform, 25°C
15.4
Creatine
pH 9.0, 30°C, recombinant mutant V325A
16.3
Creatine
-
cytoplasmic isoform M, 25°C
19.9
Creatine
-
cytoplasmic isoform M2, 25°C
20.3
Creatine
-
cytoplasmic isoform B, 25°C
25.2
Creatine
-
cytoplasmic isoform M1, 25°C
27.9
Creatine
-
cytoplasmic isoform, 25°C
28.99
Creatine
recombinant mutant enzyme H66P/D326A, at 25°C, pH not specified in the publication
28.99
Creatine
mutant enzyme H66P/D326A, at pH 8.0 and 25°C
30
Creatine
pH and temperature not specified in the publication
30
Creatine
at pH 8.5 and 25°C
36.4
Creatine
-
muscle-type isoform MCK
38.4
Creatine
-
mitochondrial isoform sMiCK
41.3
Creatine
-
mitochondrial isoform, 25°C
45
Creatine
pH 9.0, 30°C, recombinant mutant I69L
50.1
Creatine
-
pH 9.0, 30°C, recombinant mutant R340K
51.7
Creatine
-
pH 8.0, ubiquitous mitochondrial isozyme
62.15
Creatine
recombinant mutant enzyme H66P, at 25°C, pH not specified in the publication
62.15
Creatine
mutant enzyme H66P, at pH 8.0 and 25°C
67.78
Creatine
recombinant mutant enzyme D326A, at 25°C, pH not specified in the publication
67.78
Creatine
mutant enzyme D326A, at pH 8.0 and 25°C
75
Creatine
-
pH 8.0, ubiquitous mitochondrial isozyme
82.7
Creatine
pH 9.0, 30°C, recombinant mutant I69V
85.3
Creatine
pH 9.0, 30°C, recombinant wild-type enzyme
106
Creatine
-
co-substrate: ATP, 25°C, pH not specified in the publication, mutant Q185E
112
Creatine
-
co-substrate: ATP, 25°C, pH not specified in the publication, mutant A329S
115
Creatine
-
co-substrate: ATP, 25°C, pH not specified in the publication, mutant E46Q
117
Creatine
-
co-substrate: ATP, 25°C, pH not specified in the publication, mutant D189A
119
Creatine
co-substrate: ATP, 25°C, pH not specified in the publication, mutant E185Q
122
Creatine
-
co-substrate: ATP, 25°C, pH not specified in the publication, mutant K304T
126
Creatine
co-substrate: ATP, 25°C, pH not specified in the publication, mutant K36L
128
Creatine
co-substrate: ATP, 25°C, pH not specified in the publication, mutant T304K
132
Creatine
co-substrate: ATP, 25°C, pH not specified in the publication, mutant Q46E
136.21
Creatine
recombinant mutant enzyme H66R, at 25°C, pH not specified in the publication
136.21
Creatine
mutant enzyme H66R, at pH 8.0 and 25°C
138
Creatine
-
co-substrate: ATP, wild-type hMMCK, pH and temperature not specified in the publication
140
Creatine
co-substrate: ATP, 25°C, pH not specified in the publication, mutant N146C
142
Creatine
co-substrate: ATP, 25°C, pH not specified in the publication, mutant H267A
142
Creatine
co-substrate: ATP, 25°C, pH not specified in the publication, mutant S329A
148
Creatine
-
pH 9.0, 30°C, recombinant wild-type enzyme
153.5
Creatine
-
pH 9.0, muscle-type cytosolic isozyme
157.66
Creatine
recombinant mutant enzyme D326E, at 25°C, pH not specified in the publication
157.66
Creatine
mutant enzyme D326E, at pH 8.0 and 25°C
159
Creatine
co-substrate: ATP, 25°C, pH not specified in the publication, wild-type
163
Creatine
co-substrate: ATP, 25°C, pH not specified in the publication, mutant A189D
170
Creatine
-
co-substrate: ATP, 25°C, pH not specified in the publication, wild-type
173
Creatine
co-substrate: ATP, 25°C, pH not specified in the publication, mutant A205S
173
Creatine
-
co-substrate: ATP, 25°C, pH not specified in the publication, mutant C146N
175
Creatine
-
co-substrate: ATP, 25°C, pH not specified in the publication, mutant L36K
177.66
Creatine
wild type enzyme, at pH 8.0 and 25°C
177.66
Creatine
recombinant wild type enzyme, at 25°C, pH not specified in the publication
178
Creatine
-
co-substrate: ATP, 25°C, pH not specified in the publication, mutant S205A
196
Creatine
-
co-substrate: ATP, 25°C, 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, 30°C, recombinant mutant I69L
4.4
cyclocreatine
pH 9.0, 30°C, recombinant mutant I69V
18
cyclocreatine
pH 9.0, 30°C, recombinant mutant V325A
35.2
cyclocreatine
pH 9.0, 30°C, recombinant wild-type enzyme
0.55
N-ethylglycocyamine
pH 9.0, 30°C, recombinant mutant I69L
4.3
N-ethylglycocyamine
pH 9.0, 30°C, recombinant mutant V325A
12
N-ethylglycocyamine
pH 9.0, 30°C, recombinant mutant I69V
14.5
N-ethylglycocyamine
pH 9.0, 30°C, 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
additional information
additional information
-
comparison of kinetic constants with enzymes from Danio rerio, Lampetra japonica, Neanthes diversicolor, Dendronephthya gigantea
-
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, Lampetra japonica, Neanthes diversicolor
-
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 Mus musculus, Lampetra japonica, Neanthes diversicolor, Dendronephthya gigantea
-
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2.37 - 16.46
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
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
-
-
0.33
Creatine
at pH 8.5 and 25°C
1.2
glycocyamine
at pH 8.5 and 25°C
1.22
SDS
-
in 5 mM glycine-NaOH (pH 9.0), at 25°C
additional information
additional information
-
2.37
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min, ADP variable, mitochondrial fraction, pH 7.5, 37°C
2.53
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), ADP variable, mitochondrial fraction, pH 7.5, 37°C
5.02
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), ADP variable, cytosolic fraction, pH 7.5, 37°C
5.46
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min, phosphocreatine variable, mitochondrial fraction, pH 7.5, 37°C
5.67
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.020 mM organotellurium, preincubation time 5 min, ADP variable, mitochondrial fraction, pH 7.5, 37°C
5.78
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.020 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), ADP variable, mitochondrial fraction, pH 7.5, 37°C
6.49
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.005 mM organotellurium, preincubation time 5 min, phosphocreatine variable, cytosolic fraction, pH 7.5, 37°C
7.1
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.020 mM organotellurium, preincubation time 30 min, ADP variable, cytosolic fraction, pH 7.5, 37°C
7.18
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.020 mM organotellurium, preincubation time 30 min, phosphocreatine variable, mitochondrial fraction, pH 7.5, 37°C
7.5
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.020 mM organotellurium, preincubation time 30 min, ADP variable, mitochondrial fraction, pH 7.5, 37°C
7.56
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.020 mM organotellurium, preincubation time 30 min, phosphocreatine variable, cytosolic fraction, pH 7.5, 37°C
8
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.005 mM organotellurium, preincubation time 30 min, phosphocreatine variable, mitochondrial fraction, pH 7.5, 37°C
8.12
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.005 mM organotellurium, preincubation time 30 min, ADP variable, cytosolic fraction, pH 7.5, 37°C
8.2
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.005 mM organotellurium, preincubation time 30 min, phosphocreatine variable, cytosolic fraction, pH 7.5, 37°C
8.22
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
-
0.005 mM organotellurium, preincubation time 30 min, ADP variable, mitochondrial fraction, pH 7.5, 37°C
8.69
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
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0.005 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), phosphocreatine variable, cytosolic fraction, pH 7.5, 37°C
8.76
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
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0.005 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), phosphocreatine variable, mitochondrial fraction, pH 7.5, 37°C
9.65
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
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0.020 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), ADP variable, cytosolic fraction, pH 7.5, 37°C
10.25
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
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0.020 mM organotellurium, preincubation time 5 min, phosphocreatine variable, mitochondrial fraction, pH 7.5, 37°C
10.55
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
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0.005 mM organotellurium, preincubation time 5 min, ADP variable, cytosolic fraction, pH 7.5, 37°C
15.45
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
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0.020 mM organotellurium, preincubation time 5 min, ADP variable, cytosolic fraction, pH 7.5, 37°C
16
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
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0.020 mM organotellurium, preincubation time 5 min, phosphocreatine variable, cytosolic fraction, pH 7.5, 37°C
16.15
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
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0.020 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), phosphocreatine variable, mitochondrial fraction, pH 7.5, 37°C
16.46
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
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0.020 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), phosphocreatine variable, cytosolic fraction, pH 7.5, 37°C
0.13
ATP
in form of Mg-ATP, with creatine as substrate, at pH 8.5 and 25°C
0.3
ATP
in form of Mg-ATP, with glycocyamine as substrate, at pH 8.5 and 25°C
0.423
Cd2+
-
versus ATP, pH 9.0, 20°C
0.549
Cd2+
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versus creatine, pH 9.0, 20°C
10
L-isoleucine
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versus phosphocreatine, pH 7.5, 37°C
21
L-isoleucine
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versus ADP, pH 7.5, 37°C
16
L-leucine
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versus phosphocreatine, pH 7.5, 37°C
22
L-leucine
-
versus ADP, pH 7.5, 37°C
14
L-valine
-
versus phosphocreatine, pH 7.5, 37°C
23
L-valine
-
versus ADP, pH 7.5, 37°C
additional information
additional information
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inhibition kinetics with 4-hydroxy-3-nitrophenylglyoxal, overview
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additional information
additional information
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inactivation rate constants for enzyme PSCKM by Cd2+., overview
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embryonic stem cell- and neonatal-derived cardiomyocytes
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embryonic stem cell-derived cardiomyocytes
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four CK isoforms: one mitochondrial MtCK and three cytosolic isoforms: muscle-type CK (cyt-MM-CK), brain-type CK (cyt-BB-CK) and muscle-brain-type CK (cyt-MB-CK). The mitochondrial s-type, rather than u-type, is predominantly expressed in herring eye
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CKB mRNA and protein levels are significantly higher in probands affected with autosomal dominant inherited anomaly CKBE
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leptin decreases creatibe kinase
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in cultured mouse myotubes, BCK localizes near the endings of the cells, interaction with skeletal and cardiac alpha-actin
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CKB mRNA and protein levels are significantly higher in probands affected with autosomal dominant inherited anomaly CKBE
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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
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patient with ovarian hepatoid yolk sac tumor, an atypical ubiquitous mitochondrial enzyme form
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isoforms CK1, CK2 are characteristic for spermatozoa
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parietal cells of the stomach, BCK is co-localizing with and fueling the gastric H+/K+-ATPase pump at the apical membrane and the membranes of the tubulovesicular system
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of immature animals
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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
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the inter-individual variation in creatine kinase activity in the general population is wide, ranging from below 25 to up to 5000 IU/L5, with particularly high levels in men and in persons of African ancestry
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phenylbutyrate greatly decreases the adriamycin-associated elevations of serum lactate dehydrogenase and creatine kinase activities, two nonspecific widely used cardiac injury markers
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642371, 642388, 642391, 642436, 642439, 673067, 675955, 688324, 701768, 721310, 722398 brenda
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cytosolic brain-type cratine kinase
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cytosolic brain-type creatine kinase, the CK energy buffering and shuttle system seems to operate in many brain cells, in particular in the polarized large cells like neurons or hair bundle and photoreceptor cells in the sensory organs
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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
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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
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inhibition of creatine kinase blunts high extracellular Ca2+-induced increases in cardiomyocyte contractile response
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creatine kinase activity is not altered if rats are submitted to renal ischemia
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creatine kinase activity is not altered if rats are submitted to renal ischemia
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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
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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
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creatine kinase activity is not altered if rats are submitted to renal ischemia
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creatine kinase activity is not altered if rats are submitted to renal ischemia
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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
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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)
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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
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creatine kinase circuit is essential for high-sensitivity hearing
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642371, 642383, 642385, 642388, 642391, 642405, 642414, 642422, 642436, 662511, 762027 brenda
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enzyme variants IIV
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human heart cDNA library is used
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trout
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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
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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)
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creatine kinase activity is inhibited in prefrontal cortex and hippocampus of rats 12 h after renal ischemia. The treatment with antioxidants prevents such effect
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creatine kinase activity is inhibited in prefrontal cortex and hippocampus of rats 12 h after renal ischemia. The treatment with antioxidants prevents such effect
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skeletal
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skeletal
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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
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two muscle-specific isoforms
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skeletal
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skeletal
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skeletal
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skeletal
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enzyme variants I-IV
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skeletal
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skeletal
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commercial preparation
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oxidized form of enzyme
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muscle-type creatine kinase
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skeletal
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skinned psoas muscle
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skeletal
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skeletal
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hypaxial
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primary cortical neurons from mutant R6/2 mice and wild-type B6CBAFI/J mice
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primary cortical neurons from mutant R6/2 mice and wild-type B6CBAFI/J mice
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creatine kinase activity is inhibited in prefrontal cortex and hippocampus of rats 12 h after renal ischemia. The treatment with antioxidants prevents such effect
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MM isoform
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sMiCK
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additional information
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overview tissue distribution of mitochondrial enzyme
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additional information
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overview tissue distribution of mitochondrial enzyme
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additional information
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overview tissue distribution of mitochondrial enzyme
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additional information
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overview tissue distribution of mitochondrial enzyme
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additional information
high creatine kinase activity commonly occurs after exercise and in patients with damage of CK-rich tissue, including cardiac muscle, brain, and skeletal muscle
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additional information
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high creatine kinase activity commonly occurs after exercise and in patients with damage of CK-rich tissue, including cardiac muscle, brain, and skeletal muscle
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additional information
in a given cell type, at least one dimeric cytosolic isoform is always co-expressed with a predominantly octameric mitochondrial isoform (MtCK), generally cytosolic muscle-type CK (MCK) with sarcomeric MtCK (sMtCK), or cytosolic brain-type CK (BCK) with ubiquitous MtCK
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additional information
in a given cell type, at least one dimeric cytosolic isoform is always co-expressed with a predominantly octameric mitochondrial isoform (MtCK), generally cytosolic muscle-type CK (MCK) with sarcomeric MtCK (sMtCK), or cytosolic brain-type CK (BCK) with ubiquitous MtCK
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additional information
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overview tissue distribution of mitochondrial enzyme
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additional information
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overview tissue distribution of mitochondrial enzyme
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additional information
no expression of BCK in liver
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additional information
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no expression of BCK in liver
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additional information
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overview tissue distribution of mitochondrial enzyme
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additional information
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overview tissue distribution of mitochondrial enzyme
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recruitment of BCK to submembrane domains, formation of dynamic actin-based protrusions
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isoforms M1, M2, B
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isoforms M1, M2, B
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isoforms M, B
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muscle-type cytosolic isozyme MM-CK, and brain-type cytosolic isozyme BB-CK
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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)
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cytosolic brain-type creatine kinase
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isozymes CK-MM, CK-BB, and CK-MB
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cytoplasmic, muscle-type isoform MCK
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cytosolic brain-type creatine kinase, mainly soluble brain BCK
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cytosolic brain-type creatine kinase, mainly soluble brain BCK
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isozyme BCK localization at the endoplasmic reticulum calcium pump is regulated by phosphorylation via AMPK
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isozyme BCK localization at the endoplasmic reticulum calcium pump is regulated by phosphorylation via AMPK
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acetylcholine receptor membrane
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association of brain-type creatine kinase with membrane structures such as synaptic vesicles and mitochondria, involving hydrophobic and electrostatic interactions, respectively. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Recruitment of BCK to submembrane domains also supports formation of dynamic actin-based protrusions
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association of brain-type creatine kinase with membrane structures such as synaptic vesicles and mitochondria, involving hydrophobic and electrostatic interactions, respectively. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Recruitment of BCK to submembrane domains also supports formation of dynamic actin-based protrusions. Hypothetical model of BCK localization at cellular membranes, overview
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association of brain-type creatine kinase with membrane structures such as synaptic vesicles and mitochondria, involving hydrophobic and electrostatic interactions, respectively. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Recruitment of BCK to submembrane domains also supports formation of dynamic actin-based protrusions. Hypothetical model of BCK localization at cellular membranes, overview
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acetylcholine receptor membrane
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overview on intramitochondrial localization
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accumulated in contact sites between inner and outer mitochondrial membrane
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mitochondrial isozyme MtCK
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there are two mitochondrial isoforms of CK: s-type (sarcomeric, expressed in skeletal and heart muscles only) and u-type (ubiquitous, expressed in many other tissues), which both exist as octamers in fish as well as in higher vertebrates and invertebrates. The mitochondrial s-type, rather than u-type, is predominantly expressed in herring eye
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overview on intramitochondrial localization
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accumulated in contact sites between inner and outer mitochondrial membrane
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respiration rate at 10-20°C, pH 7.1-7.3
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accumulated in contact sites between inner and outer mitochondrial membrane
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accumulated in contact sites between inner and outer mitochondrial membrane
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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
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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
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association with by brain-type creatine kinase
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octameric MtCK is situated in the mitochondrial intermembrane space, binding simultaneously to both mitochondrial inner and outer membranes, as well as in the cristae space bound to inner membrane
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respiration rate at 10-20°C, pH 7.1-7.3
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accumulated in contact sites between inner and outer mitochondrial membrane
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sarcomeric, mitochondrial isoform sMiCK
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accumulated in contact sites between inner and outer mitochondrial membrane
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simulation of hyperglycemic conditions induces H2O2 production in a creatine sensitive manner
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in mitochondria from intact animals, mCK exists as a mixture of two oligomeric forms (dimer and octamer: 68 and 32%, respectively)
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head isozyme
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accumulated in contact sites between inner and outer mitochondrial membrane
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accumulated in contact sites between inner and outer mitochondrial membrane
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respiration rate at 10-20°C, pH 7.1-7.3
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under energy-compromised conditions, CKM is recruited to the plasma membrane and co-localizes with NCX1
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association with by brain-type creatine kinase
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association with by brain-type creatine kinase, isolated from rat forebrains by separation from nerve-ending particles (synaptosomes). Synaptic vesicle BCK is indeed firmly anchored in the vesicle membrane and not just interacting electrostatically with the lipid headgroups or simply enclosed within the vesicles
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additional information
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overview
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additional information
Frog
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overview
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additional information
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overview
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additional information
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overview
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additional information
the BCK isoform is mostly soluble but partially associates with cellular structures, subcellular localizations and cellular interaction partners of BCK, overview
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additional information
the BCK isoform is mostly soluble but partially associates with cellular structures, subcellular localizations and cellular interaction partners of BCK, overview
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additional information
the mitochondrial enzyme participates in large complexes that include the voltage-dependent anion channel in the mitochondrial outer membrane as well as cardiolipin and adenine nucleotide transporter in the mitochondrial inner membrane, localization and complex formation of MtCK, overview
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brenda
additional information
the mitochondrial enzyme participates in large complexes that include the voltage-dependent anion channel in the mitochondrial outer membrane as well as cardiolipin and adenine nucleotide transporter in the mitochondrial inner membrane, localization and complex formation of MtCK, overview
-
brenda
additional information
-
overview
-
brenda
additional information
-
overview
-
brenda
additional information
as compared to total, mainly soluble brain BCK, the BCK bound to mitochondria and synaptic vesicles appears to be heterogeneous. Appreciable amounts of cytosolic BCK are bound to synaptic vesicles and mitochondrial membranes, and these interactions are governed by different mechanisms and possibly linked to secondary BCK modifications. Two different mechanisms are possible involving either the membrane or the BCK binding partner: (1) A specific mitochondrial receptor is required, which is absent in liver and removed by the high pH treatment in brain, or (2) BCK requires posttranslational modifications which are missing on the recombinant enzyme
-
brenda
additional information
-
as compared to total, mainly soluble brain BCK, the BCK bound to mitochondria and synaptic vesicles appears to be heterogeneous. Appreciable amounts of cytosolic BCK are bound to synaptic vesicles and mitochondrial membranes, and these interactions are governed by different mechanisms and possibly linked to secondary BCK modifications. Two different mechanisms are possible involving either the membrane or the BCK binding partner: (1) A specific mitochondrial receptor is required, which is absent in liver and removed by the high pH treatment in brain, or (2) BCK requires posttranslational modifications which are missing on the recombinant enzyme
-
-
brenda
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evolution
the MtCK gene is likely basal and ancestral and has evolved very early in metazoan evolution
malfunction
-
absence of creatine kinase in muscle cells leads to morphological and functional adaptations towards preservation of muscle contractile abilities
malfunction
-
complete brain-type creatine kinase deficiency in mice blocks seizure activity and affects intracellular calcium kinetics
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
malfunction
-
24 h after trauma brain injury (TBI) of mice preconditioned with N-methyl-D-aspartate, creatine kinase activity is augmented in the cerebral cortex. Eventhough N-methyl-D-aspartate preconditioning and TBI have similar effects on the enzyme activity, each manages its response via opposite mechanisms because the protective effects of preconditioning are unambiguous
malfunction
downregulation of brain-type creatine kinase in brain of a Huntington's disease mouse model. Huntington's disease is a hereditary neurodegenerative disorder caused by a CAG repeat expansion in the huntingtin (HTT) gene. Mutant HTT (mHTT) suppresses the activity of the CKB gene promoter, which contributes to the lowered CKB expression in Huntington's disease. Exogenous expression of wild-type CKB, but not a dominant negative CKB mutant, rescues the ATP depletion, aggregate formation, impaired proteasome activity, and shortened neurites induced by mHTT. Negative regulation of isozyme CKB by mHTT is a key event in the pathogenesis of Huntington's disease and contributes to the neuronal dysfunction associated with Huntington's disease
malfunction
downregulation of brain-type creatine kinase in brains of Huntington's disease patients. Huntington's disease is a hereditary neurodegenerative disorder caused by a CAG repeat expansion in the huntingtin (HTT) gene
malfunction
knockout mice that lack the brain CK isoforms, i.e. BCK and/or ubiquitous MtCK, uMtCK, show defects in spatial memory acquisition and behavior, development of the hippocampus, correct functioning of hair bundle cells in the auditory system, and energy distribution within photoreceptor cells, transgenic models of creatine deficiency, overview
malfunction
-
impairment of enzyme activity leads to a downregulation of renal Na+, K+-ATPase activity during an Aeromonas caviae infection, contributing to energy depletion
malfunction
-
downregulation of brain-type creatine kinase in brain of a Huntington's disease mouse model. Huntington's disease is a hereditary neurodegenerative disorder caused by a CAG repeat expansion in the huntingtin (HTT) gene. Mutant HTT (mHTT) suppresses the activity of the CKB gene promoter, which contributes to the lowered CKB expression in Huntington's disease. Exogenous expression of wild-type CKB, but not a dominant negative CKB mutant, rescues the ATP depletion, aggregate formation, impaired proteasome activity, and shortened neurites induced by mHTT. Negative regulation of isozyme CKB by mHTT is a key event in the pathogenesis of Huntington's disease and contributes to the neuronal dysfunction associated with Huntington's disease
-
malfunction
-
24 h after trauma brain injury (TBI) of mice preconditioned with N-methyl-D-aspartate, creatine kinase activity is augmented in the cerebral cortex. Eventhough N-methyl-D-aspartate preconditioning and TBI have similar effects on the enzyme activity, each manages its response via opposite mechanisms because the protective effects of preconditioning are unambiguous
-
metabolism
co-localization and functional coupling of creatine kinase isoforms with ATP-producing and ATP-consuming reactions, a non-equilibrium state of the creatine kinase reaction, and restricted intracellular diffusion of adenine nucleotides support the concept of a cellular CK/PCr phosphoryl transfer network. spatial organization of the CK/PCr shuttle in brain, in particular the association of BCK to subcellular components as well as to specific, interacting proteins, overview
metabolism
co-localization and functional coupling of creatine kinase isoforms with ATP-producing and ATP-consuming reactions, a non-equilibrium state of the creatine kinase reaction, and restricted intracellular diffusion of adenine nucleotides support the concept of a cellular CK/PCr phosphoryl transfer network. The reactions catalyzed by different isoforms of compartmentalized creatine kinase, organized in intracellular energetic units tend to maintain the intracellular metabolic stability
metabolism
importance of functional coupling between MtCK, ANT and respiration/ATP synthesis provided by the close co-localization of MtCK and ANT in proteolipid complexes. Co-localization and functional coupling of creatine kinase isoforms with ATP-producing and ATP-consuming reactions, a non-equilibrium state of the creatine kinase reaction, and restricted intracellular diffusion of adenine nucleotides support the concept of a cellular CK/PCr phosphoryl transfer network. The reactions catalyzed by different isoforms of compartmentalized creatine kinase, organized in intracellular energetic units tend to maintain the intracellular metabolic stability
metabolism
the enzyme preferentially interacts with saturated fatty acid- and/or monounsaturated fatty acid-containing phosphatidic acids, but not with polyunsaturated fatty acid-containing phosphatidic acids. Notably, the enzyme exclusively interacts with phosphatidic acid, whereas the protein does not bind to other lipids such as diacylglycerol, phosphatidylserine, phosphatidylglycerol, phosphatidylinositol, phosphatidylinositol (3,4,5)-triphosphate and cardiolipin
metabolism
-
co-localization and functional coupling of creatine kinase isoforms with ATP-producing and ATP-consuming reactions, a non-equilibrium state of the creatine kinase reaction, and restricted intracellular diffusion of adenine nucleotides support the concept of a cellular CK/PCr phosphoryl transfer network. spatial organization of the CK/PCr shuttle in brain, in particular the association of BCK to subcellular components as well as to specific, interacting proteins, overview
-
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
physiological function
brain-type creatine kinase is an enzyme involved in energy homeostasis via the phosphocreatine-creatine kinase system, the CK system plays a critical role in energy homeostasis and ATP distribution
physiological function
brain-type creatine kinase is an enzyme involved in energy homeostasis via the phosphocreatine-creatine kinase system, the CK system plays a critical role in energy homeostasis and ATP distribution. Creatine kinase activity is critical for the beneficial effects of isozyme CKB of enhancing proteasome activity and reducing aggregate formation
physiological function
-
creatine kinase catalyzes the reversible transfer of the phosphoryl group from phosphocreatine to ADP, regenerating ATP, and it is a major enzyme of higher eukaryotes that manages high, fluctuating energy demands to maintain cellular energy homeostasis and guarantee stable, locally buffered ATP/ADP ratios
physiological function
creatine kinase inhibits ADP-induced platelet aggregation. Inter-individual differences in plasma creatine kinase activity modulate the bleeding risk. Proposed mode of action of creatine kinase in main inhibitory pathways of platelet activation and the potential role of plasma creatine kinase herein, overview. The enzyme might attenuate platelet activation through scavenging plasma ADP as a binding protein, or via its catalytic activity converting ADP to ATP, leading to a reduced activation of the P2Y12 ADP receptor and attenuated platelet aggregation
physiological function
creatine kinase is a key player in maintaining cellular energy homeostasis using creatine for reversible phosphoryl transfer between ATP and phosphocreatine. The cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at Ser6 to trigger BCK localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. Recruitment of BCK into the surface layer of a membrane, close to ATPases, and the resulting two-dimensional ATP diffusion along the membrane are sufficient to provide an energetic advantage. BCK may fuel the endoplasmic reticulum Ca2+ ATPase pump
physiological function
creatine kinase is a key player in maintaining cellular energy homeostasis using creatine for reversible phosphoryl transfer between ATP and phosphocreatine. The cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at serine 6 to trigger BCK localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Creatine kinase microcompartments play a role in the energy metabolism. At the cellular level, creatine kinase acts mainly via two different mechanisms. Firstly, the enzyme enables the building-up of a global cellular energy buffer in the form of a large phosphocreatine pool that can be used to regenerate ATP during a temporal mismatch between ATP generation and consumption. Secondly, cytosolic and mitochondrial isozymes, together with highly concentrated and diffusible phosphocreatine, facilitate the so-called CK/PCr shuttle to correct for a spatial mismatch between ATP generation and -consumption within a cell. The CK/PCr shuttle is particularly important for large and polar cells with high and/or fluctuating energy demands such as skeletal and heart muscle cells, or many cell types in the brain, but may occur in any cell type expressing creatine kinase. BCK may fuel the endoplasmic reticulum Ca2+ ATPase pump. In retina photoreceptor cells, BCK may play an equally important role, but rather in synaptic transmission at the synaptic terminal or for cGMP resynthesis in the rod outer segments. In astrocytes and fibroblasts, BCK in peripheral cellular structures facilitates actin-driven cell spreading and migration
physiological function
creatine kinase is a key player in maintaining cellular energy homeostasis using creatine for reversible phosphoryl transfer between ATP and phosphocreatine. The cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at serine 6 to trigger BCK localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. Membrane localization of BCK seems to be an important and regulated feature for the fueling of membrane-located, ATP-dependent processes, stressing again the importance of local rather than global ATP concentrations. Creatine kinase microcompartments play a role in the energy metabolism. At the cellular level, creatine kinase acts mainly via two different mechanisms. Firstly, the enzyme enables the building-up of a global cellular energy buffer in the form of a large phosphocreatine pool that can be used to regenerate ATP during a temporal mismatch between ATP generation and consumption. Secondly, cytosolic and mitochondrial isozymes, together with highly concentrated and diffusible phosphocreatine, facilitate the so-called CK/PCr shuttle to correct for a spatial mismatch between ATP generation and -consumption within a cell. The CK/PCr shuttle is particularly important for large and polar cells with high and/or fluctuating energy demands such as skeletal and heart muscle cells, or many cell types in the brain, but may occur in any cell type expressing creatine kinase. The role of MtCK within the mitochondrial interactosome is to separate energy fluxes from the intracellular energy signals and to amplify these signals due to the intramitochondrial recycling of ADP
physiological function
-
the essential enzyme plays an important role in brain energy homeostasis
physiological function
-
the enzyme plays an important role in brain energy homeostasis
physiological function
-
brain-type creatine kinase is an enzyme involved in energy homeostasis via the phosphocreatine-creatine kinase system, the CK system plays a critical role in energy homeostasis and ATP distribution. Creatine kinase activity is critical for the beneficial effects of isozyme CKB of enhancing proteasome activity and reducing aggregate formation
-
physiological function
-
creatine kinase catalyzes the reversible transfer of the phosphoryl group from phosphocreatine to ADP, regenerating ATP, and it is a major enzyme of higher eukaryotes that manages high, fluctuating energy demands to maintain cellular energy homeostasis and guarantee stable, locally buffered ATP/ADP ratios
-
physiological function
-
creatine kinase is a key player in maintaining cellular energy homeostasis using creatine for reversible phosphoryl transfer between ATP and phosphocreatine. The cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at Ser6 to trigger BCK localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. Recruitment of BCK into the surface layer of a membrane, close to ATPases, and the resulting two-dimensional ATP diffusion along the membrane are sufficient to provide an energetic advantage. BCK may fuel the endoplasmic reticulum Ca2+ ATPase pump
-
additional information
dual active-site cysteine 283 residues
additional information
-
dual active-site cysteine 283 residues
additional information
formation of the disulfide bond between the C74 and the C146 residues in the oxidized form
additional information
-
formation of the disulfide bond between the C74 and the C146 residues in the oxidized form
additional information
phosphocreatine is an alternative energy carrier that compared to ATP is metabolically inert (except for the creatine kinase reaction), much smaller in molecular size and less charged over the physiological pH range, and is thus significantly more diffusible than ATP
additional information
phosphocreatine is an alternative energy carrier that compared to ATP is metabolically inert (except for the creatine kinase reaction), much smaller in molecular size and less charged over the physiological pH range, and is thus significantly more diffusible than ATP
additional information
phosphocreatine is an alternative energy carrier that compared to ATP is metabolically inert (except for the creatine kinase reaction), much smaller in molecular size and less charged over the physiological pH range, and is thus significantly more diffusible than ATP
additional information
-
phosphocreatine is an alternative energy carrier that compared to ATP is metabolically inert (except for the creatine kinase reaction), much smaller in molecular size and less charged over the physiological pH range, and is thus significantly more diffusible than ATP
-
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126000 - 145000
-
flagellar isozyme, sucrose density gradient centrifugation, SDS-PAGE
145000
-
1 * 145000, flagellar isozyme, 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
335000
octameric enzyme form of isozyme MtCK, gel filtration
345000
-
mitochondrial isozyme, gel filtration
346000
-
gel filtration, also 86000
347000
-
octameric enzyme form, gel filtration
35000
-
2 * 35000, SDS-PAGE
360000
-
isozyme Mia-CK, octameric form, gel filtration
371000
-
and also 79700, gel filtration
40000
-
2 * 40000, SDS-PAGE
41500
-
2 * 41500, SDS-PAGE
43195
-
2 * 43195, calculated from sequence of cDNA
44000
-
2 * 44000, SDS-PAGE, presence of 2-mercaptoethanol, high speed sedimentation equilibrium centrifugation of urea-treated enzyme
46000
recombinant mutant R147A, gel filtration
49000
-
2 * 49000, SDS-PAGE
50000
-
2 * 50000, SDS-PAGE
61500
-
dimeric enzyme form, gel filtration
67000
recombinant mutant R151A, analytical ultracentrifugation
71000
recombinant mutant D209A, analytical ultracentrifugation
74000
recombinant mutant D209A, gel filtration
76000 - 78000
-
gel filtration
78000
-
isozyme Mi-CK, dimeric form, scanning transmission electron microscopy
79700
-
and also 371000, gel filtration
81000
recombinant mutant R151A, gel filtration
82600
-
cytosolic muscle isozyme, gel filtration
84000 - 85000
-
isozyme MiMi-CK, sedimentation equilibrium centrifugation, gel filtration
84500
-
high speed and low speed sedimentation equilibrium centrifugation
85100
-
sedimentation equilibrium centrifugation
89000
-
isozyme Mia-CK, dimeric form, scanning transmission electron microscopy
41000
-
2 * 41000, SDS-PAGE
41000
-
2 * 41000, SDS-PAGE
41000
-
2 * 41000, isozyme CK-IV
41000
-
1 * 41000 + 1 * 42000, isozyme CK-II
41000
-
2 * 41000, muscle cytosolic isozyme, SDS-PAGE
41000
-
8 * 41000, SDS-PAGE, isoform CK1
42000
recombinant mutant R147A, analytical ultracentrifugation
42000
-
2 * 42000, SDS-PAGE
42000
-
2 * 42000, SDS-PAGE
42000
-
8 * 42000, SDS-PAGE, octameric structure dissociates during storage at -20°C, pH above 8.5, protein concentration below 0.3 mg/ml to dimeric form
42000
-
2 * 42000, isozyme CK-III
42000
-
1 * 41000 + 1 * 42000, isozyme CK-II
43000
gel filtration
43000
-
x * 43000, SDS-PAGE
43000
-
2 * 43000, SDS-PAGE
43000
-
8 * 43000, SDS-PAGE, also as dimer
43000
-
2 * 43000, SDS-PAGE, but also octamer
43000
-
2 * 43000, recombinant enzyme, SDS-PAGE, dimer formation after dissociation of the octamer
43000
-
8 * 43000, muscle mitochondrial isozyme, SDS-PAGE
43000
-
8 * 43000, recombinant enzyme, SDS-PAGE, enzyme primarily forms octamers
43600
-
8 * 43600, SDS-PAGE, but also dimer, electron microscopy
43600
-
2 * 43600, SDS-PAGE, but also octamer, electron microscopy
45000
recombinant mutant R147A/R151A, gel filtration and analytical ultracentrifugation
45000
-
2 * 45000, SDS-PAGE, isoform CK2
47000
-
x * 47000, head mitochondrial isozyme, SDS-PAGE
47000
1 * 47000, about, recombinant mutant enzymes D209A, R147A, and R147A/R151A, SDS-PAGE
47000
2 * 47000, about, recombinant wild-type enzyme and recombinant mutant enzymes D209A and R151A, SDS-PAGE
78500 - 85100
-
cytosolic muscle isozyme
78500 - 85100
-
cytosolic muscle isozyme
78500 - 85100
cytosolic muscle isozyme
80000
gel filtration
80000
-
low speed sedimentation equilibrium centrifugation
82000
-
sedimentation equilibrium centrifugation
82000
dimeric enzyme form, gel filtration
84000
-
gel filtration
84000
-
isozyme MiMi-CK, equilibrium centrifugation
85000
-
isozyme Mia-CK, dimeric form, gel permeation chromatography, analytical ultracentrifugation
85000
recombinant wild-type enzyme, gel filtration
86000
gel filtration
86000
-
cytosolic isozyme, gel filtration
86000
-
gel filtration, also 346000
86000
recombinant wild-type enzyme, analytical ultracentrifugation
90000
gel filtration
90000
-
gel filtration, isoform CK2
additional information
-
overview
additional information
-
overview
additional information
-
overview
additional information
-
overview
additional information
-
overview
additional information
-
overview
additional information
-
overview
additional information
-
overview
additional information
-
structural properties, sulfhydryl groups
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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
?
x * 44000, His6-tagged enzyme, SDS-PAGE
?
x * 43000, His6-tagged enzyme, SDS-PAGE
?
x * 43264, calculated from amino acid sequence
?
-
x * 40000-44000, mature enzyme
dimer
-
-
dimer
-
2 * 35000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
-
2 * 40000-44000, mature cytosolic isozymes
dimer
-
2 * 41000, 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 * 45000, SDS-PAGE, isoform CK2
dimer
-
2 * 40000-43000, SDS-PAGE
dimer
-
2 * 44000, SDS-PAGE, presence of 2-mercaptoethanol, high speed sedimentation equilibrium centrifugation of urea-treated enzyme
dimer
-
2 * 42000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
dimer
-
2 * 41500, SDS-PAGE
dimer
-
crystallization data, absence of ATP
dimer
-
2 * 43195, calculated from sequence of cDNA
dimer
2 * 40000-44000, mature cytosolic isozymes
dimer
-
2 * 41000, SDS-PAGE
dimer
-
2 * 42000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE, but also octamer
dimer
-
2 * 43600, SDS-PAGE, but also octamer, electron microscopy
dimer
-
2 * 40000-44000, mature cytosolic isozymes
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 40000-44000, mature cytosolic isozymes
dimer
2 * 47000, about, recombinant wild-type enzyme and recombinant mutant enzymes D209A and R151A, SDS-PAGE
dimer
muscle creatine kinase is only enzymatically active as a dimer
dimer
dual active-site cysteine 283 residues, spectral observations localized at the active-site cysteines indicate an intrinsic, dynamic asymmetry between the two subunits that exists already in the apo form of the dimeric creatine kinase enzyme, rather than being induced by the substrate. Unmodified and Cys283-modified enzymes are investigated in the apo and transition state analogue forms of the enzyme. The narrow and invariant S-H vibrational bands report a homogeneous environment for the unmodified active-site cysteines, indicating that their thiols are hydrogen bonded to the same H-bond acceptor in the presence and absence of the substrate. The S-H peak persists at all physiologically relevant pH's, indicating that Cys283 is protonated at all pH's relevant to enzymatic activity. The S-H hydrogen bond acceptor is a single, long-resident water molecule and the role of the conserved yet catalytically unnecessary thiol may be to dynamically rigidify that part of the active site through specific H-bonding to water. The asymmetric and broad CN stretching bands from the CN-modified Cys283 suggest an asymmetric structure in the apo form of the enzyme in which there is a dynamic exchange between spectral subpopulations associated with water-exposed and water-excluded probe environments, homogeneous orientation of the SCN probe group in the active site. Molecular dynamics simulations, overview
dimer
-
2 * 49000, SDS-PAGE
dimer
-
2 * 43000-44000, SDS-PAGE, presence of 2-mercaptoethanol
dimer
-
2 * 40000-43000, SDS-PAGE
dimer
-
2 * 42000, isozyme CK-III
dimer
-
2 * 41000, isozyme CK-IV
dimer
-
1 * 41000 + 1 * 42000, isozyme CK-II
heterodimer
-
heterodimer
1 * 47200 + 1 * 43600, calculated from amino acid sequence
homodimer
2 * 45000, SDS-PAGE
homodimer
2 * 42000, SDS-PAGE
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 * 47000, about, recombinant mutant enzymes D209A, R147A, and R147A/R151A, SDS-PAGE
monomer
-
1 * 145000, flagellar isozyme, SDS-PAGE
octamer
-
8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
octamer
-
8 * 43000, recombinant enzyme, SDS-PAGE, enzyme primarily forms octamers
octamer
-
8 * 43000, muscle mitochondrial isozyme, SDS-PAGE
octamer
-
8 * 41000, SDS-PAGE, isoform CK1
octamer
mitochondrial isozyme MtCK
octamer
-
crystallization data
octamer
-
8 * 42000, SDS-PAGE, octameric structure dissociates during storage at -20°C, pH above 8.5, protein concentration below 0.3 mg/ml to dimeric form
octamer
-
crystallization data, presence of ATP
octamer
8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
octamer
-
8 * 43600, SDS-PAGE, but also dimer, electron microscopy
octamer
-
8 * 43000, SDS-PAGE, also as dimer
octamer
-
8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
octamer
mitochondrial isozyme
octamer
-
8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
octamer
mitochondrial isozyme
octamer
-
mitochondrial isozyme
-
additional information
-
hydrolytic cleaveage is responsible for conversion of isoform MM1 to MM2 and MM3
additional information
-
the octamer-dimer equilibrium highly depends on protein concentration and dilution, respectively, and on temperature, highest percentage of octamer occurs at 28°C, the lowest at 2°C, overview
additional information
-
MtCK generally exists as an octamer, but a dynamic octamer/dimer equilibrium exists in vitro depending on various parameters like MtCK concentration, temperatures and pH. Enzyme activity and temperature stability /sensitivity are higher for the octameric enzyme than for the dimeric enzyme. MtCK dimers are very sensitive and inactivate after exposure to temperatures above 30°C
additional information
MtCK generally exists as an octamer, but a dynamic octamer/dimer equilibrium exists in vitro depending on various parameters like MtCK concentration, temperatures and pH. Enzyme activity and temperature stability /sensitivity are higher for the octameric enzyme than for the dimeric enzyme. MtCK dimers are very sensitive and inactivate after exposure to temperatures above 30°C
additional information
-
overview on isoforms
additional information
Frog
-
overview on isoforms
additional information
-
overview on isoforms
additional information
analysis of the structure of cardiac sarcomeric mitochondrial isozyme, free or bound to MgATP or transition state analogue complex
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
additional information
formation of the disulfide bond between the C74 and the C146 residues in the oxidized form
additional information
-
formation of the disulfide bond between the C74 and the C146 residues in the oxidized form
additional information
-
overview on isoforms
additional information
-
overview on isoforms
additional information
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
-
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
-
structure-function analysis, the monomeric enzyme is active, the subunits act independently
additional information
-
the isozymes form monomers upon freeze-drying due to loss of subunit interactions
additional information
mutants L110D, L115D, L121D are faster on SDS-PAGE than wild-type protein
additional information
-
mutants L110D, L115D, L121D are faster on SDS-PAGE than wild-type protein
additional information
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
-
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
-
overview on isoforms
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G268D
site-directed mutagenesis, the mutant shows increased activity at 10°C and pH 8.0 compared to the wild-type
G268K
site-directed mutagenesis, the mutant shows increased activity at 10°C and pH 8.0 compared to the wild-type
G268L
site-directed mutagenesis, the mutant does not show altered activity at 10°C and pH 8.0 compared to the wild-type
A189D
Km and kcat values similar to wild-type, T0.5 (°C): 46.2 (wild-type: 48.0°C)
A205S
Km and kcat values similar to wild-type, T0.5 (°C): 46.6 (wild-type: 48.0°C)
E185Q
Km (ATP) and (creatine) significantly higher compared to wild-type, kcat value 74% of wild-type, T0.5 (°C): 47.4 (wild-type: 48.0°C)
H267A
Km and kcat values similar to wild-type, T0.5 (°C): 47.6 (wild-type: 48.0°C)
K36L
Km and kcat values similar to wild-type, T0.5 (°C): 46.7 (wild-type: 48.0°C)
N146C
Km and kcat values similar to wild-type, T0.5 (°C): 51 (wild-type: 48.0°C)
Q46E
Km and kcat values similar to wild-type, T0.5 (°C): 50.9 (wild-type: 48.0°C)
S329A
Km and kcat values similar to wild-type, T0.5 (°C): 48.3 (wild-type: 48.0°C)
T304K
Km and kcat values similar to wild-type, T0.5 (°C): 47.6 (wild-type: 48.0°C)
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: 56.9°C)
A329S
-
Km and kcat values similar to wild-type, T0.5 (°C): 56.6 (wild-type: 56.9°C)
C146N
-
Km and kcat values similar to wild-type, T0.5 (°C): 52.4 (wild-type: 56.9°C)
C283S/S285C
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: 56.9°C)
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: 56.9°C)
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: 56.9°C)
L36K
-
Km and kcat values similar to wild-type, T0.5 (°C): 47.3 (wild-type: 56.9°C)
P284A
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: 56.9°C)
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: 56.9°C)
S285A
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
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
A267H
-
at pH 7.1 mutant shows 30% higher specific activity than the wild-type at 35°C, 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
D209A
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
G268D
site-directed mutagenesis, the mutant shows increased activity at 10°C and pH 8.0 compared to the wild-type
G268K
site-directed mutagenesis, the mutant shows increased activity at 10°C and pH 8.0 compared to the wild-type
G268L
site-directed mutagenesis, the mutant does not show altered activity at 10°C and pH 8.0 compared to the wild-type
G268N
site-directed mutagenesis, the mutant shows increased activity at 10°C compared to the wild-type
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 35°C. At pH 7.7 and pH 8.0 at 10°C 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
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
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 35°C, 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
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
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
site-directed mutagenesis, the triple mutant enzyme is expressed as insoluble, aggregated protein
R151A
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
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
D326A
the mutant displays obviously loss of activity, substrate synergism and stability as compared to the wild type enzyme
D326A
the mutant enzyme displays strong loss of activity, substrate synergism and stability with partially unfolded state and aggregation
D326E
the mutant displays obviously loss of activity, substrate synergism and stability as compared to the wild type enzyme
D326E
the mutant enzyme displays loss of activity
D54G
-
mutation identified in acute myocardial infarction patient, mutant shows substantially decreased activity, substrate binding affinity and stability
D54G
-
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
H66P
the mutant displays obviously loss of activity, substrate synergism and stability as compared to the wild type enzyme
H66P
the mutant enzyme displays strong loss of activity, substrate synergism and stability with partially unfolded state and aggregation
H66P/D326A
the mutant displays obviously loss of activity, substrate synergism and stability as compared to the wild type enzyme
H66P/D326A
the mutant enzyme displays severe loss of activity, substrate synergism and stability
H66R
the mutant displays obviously loss of activity, substrate synergism and stability as compared to the wild type enzyme
H66R
the mutant enzyme displays loss of activity
C74S
-
enzyme preparation contains only reduced form
C74S
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
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
additional information
construction of a Fc-III-tagged GFP fusion muscle creatine kinase (CK) as a model system to investigate effects of the Fc-III tag on activities and stabilities of recombinantly expressed multicysteine-containing proteins. The Fc-III tag has no adverse effects on the fluorescence of GFP and reduces the occurrence of GFP misfolding due to incorrect Cys oxidation compared with the His-tagged protein. Activity and stability of the Fc-III-tagged creatine kinase is slightly lower than that of the tag-free creatine kinase, but is higher than that of the His-tagged creatine kinase as determined by the ratio of the oxidized versus reduced CK. A major portion of His-tagged CK is in its oxidized form, while that of the Fc-III-tagged CK is in its reduced form. A folding model of CK with different tags is proposed, overview. The decrease of the activity of CK may attribute to the tag-induced changes of the tertiary structures of the targeted proteins
additional information
-
construction of a Fc-III-tagged GFP fusion muscle creatine kinase (CK) as a model system to investigate effects of the Fc-III tag on activities and stabilities of recombinantly expressed multicysteine-containing proteins. The Fc-III tag has no adverse effects on the fluorescence of GFP and reduces the occurrence of GFP misfolding due to incorrect Cys oxidation compared with the His-tagged protein. Activity and stability of the Fc-III-tagged creatine kinase is slightly lower than that of the tag-free creatine kinase, but is higher than that of the His-tagged creatine kinase as determined by the ratio of the oxidized versus reduced CK. A major portion of His-tagged CK is in its oxidized form, while that of the Fc-III-tagged CK is in its reduced form. A folding model of CK with different tags is proposed, overview. The decrease of the activity of CK may attribute to the tag-induced changes of the tertiary structures of the targeted proteins
additional information
-
transgenic mice lacking mitochondrial enzyme or both mitochondrial and cytoplasmic enzyme
additional information
-
enzyme knockout results in loss of hearing
additional information
deletion of N-terminal 15 amino acids causes dissociation of the functional homodimer into monomers with reduced catalytic activity
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
additional information
construction of an N-terminally trucated isozyme BCK
additional information
-
construction of an N-terminally trucated isozyme BCK
-
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
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0 - 60
the enzyme acctivity is stable from 0°C up to 45°C, inactivation at 65°C
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
25 - 60
the wild type enzyme remains stable after 10 min at 25-45°C. The activity drops to about 70% and after 10 min at 50°C. The enzyme is almost completely inactive after 10 min at 60°C
25 - 65
the activity of the wild type enzyme has few changes after heat treatment for 10 min at temperatures below 48°C. A steep decrease of activity is observed between 48°C and 60°C
35
-
calf brain: 0.01 M 2-mercaptoethanol enhances stability in pH-range 6-8
36
-
mutant D54G, melting temperature
40 - 43
inactivation of recombinant mutant R151A
41
inactivation of recombinant mutant R147A
42.2
-
T0.5: 42.2°C wild-type hBBCK
51.9
melting temperature of mutant L110D
52.3
melting temperature of wild-type
52.9
melting temperature of mutant L121D
53
-
midpoint temperature of thermal inactivation of wild-type enzyme is 52.5°C
53 - 55
inactivation of recombinant wild-type enzyme
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: 56.9°C
57.2
-
T0.5: 57.2°C wild-type hMMCK
62
-
wild-type hMMCK gets completely inactivated above 62°C
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
-
midpoint temperature of thermal inactivation of mutant enzyme D54G is 36.5°C
37
inactivation of recombinant mutant R147A/R151A
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
-
10 min, mutant enzyme D54G is completely inactivated
45
mutant G73A, inactivation
45
-
soluble enzyme: half-life 4 min, immobilized enzyme: half-life 35 min
48
muscle-type creatine kinase of Danio rerio is less stable compared to human muscle-type creatine kinase, T0.5: 48°C
48
-
wild-type, stable up to 48°C
48
-
10 min, the activity of wild-type enzyme has no significant changes after heat treatment at temperatures below 48°C
48
-
wild-type hBBCK gets completely inactivated above 48°C
48
wild-type, stable up to 48°C, mutant V75A, inactivation
52
-
wild-type, melting temperature
52
-
T0.5: 52°C hybrid form consisting of muscle and brain creatine kinase isoforms
52
the recombinant enzymes are stable upto 50°C, the recombinant His-tagged and Fc-III-tagged enzymes show similar heat-resistance and are less stable than that of the tag-free enzyme. They start to lose their activities at 52°C and are relatively less active at the same denaturing temperature than tag-free enzyme. The DELTAT0.5 value of the tag-free enzyme is about 58°C and that of the tagged enzyme is around 57°C
58
-
wild-type, complete loss of activity
58
-
10 min, complete loss of activity above
58
wild-type, inactivation
additional information
-
comparison of various enzymes of various sources
additional information
-
enzyme activity and temperature stability /sensitivity are higher for the octameric enzyme than for the dimeric enzyme. MtCK dimers are very sensitive and inactivate after exposure to temperatures above 30°C
additional information
enzyme activity and temperature stability /sensitivity are higher for the octameric enzyme than for the dimeric enzyme. MtCK dimers are very sensitive and inactivate after exposure to temperatures above 30°C
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
-
comparison of various enzymes of various sources
additional information
-
comparison of various enzymes of various sources
additional information
-
temperature stability profile of the isozymes CK-MM, CK-BB, and CK-MB, overview
additional information
-
enzymes from marine fishes are less thermostable than that of carp, the latter being more labile than the rabbit enzyme
additional information
-
enzymes from marine fishes are less thermostable than that of carp, the latter being more labile than the rabbit enzyme
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