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Enzyme Nomenclature
Information on EC 2.7.3.2 - creatine kinase
for references in articles please use BRENDA:EC2.7.3.2
Word Map on EC 2.7.3.2
- 2.7.3.2
- myocardial
- cardiac
- infarct
- coronary
- lactate
- injury
- artery
- ventricular
-
reperfusion
- muscular
- ischemia
-
troponins
- myopathy
- pain
- renal
-
myoglobin
-
admission
- dystrophy
- rhabdomyolysis
- anterior
- chest
-
postoperative
-
cytokeratins
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admitted
-
cardioprotective
- angina
-
duchenne
-
ejection
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percutaneous
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contractile
-
fatigue
-
cardiopulmonary
-
reperfused
-
angiographic
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isometric
-
c-reactive
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thrombolysis
-
athlete
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angioplasty
- tachycardia
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perioperative
-
revascularization
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langendorff
-
eccentric
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electrocardiograph
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in-hospital
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hemodynamic
- arrhythmia
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exercise-induced
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echocardiography
- biotechnology
- medicine
- diagnostics
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.7.3.2
-
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RECOMMENDED NAME
GeneOntology No.
creatine kinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + creatine = ADP + phosphocreatine
; N-ethylglycocyamine can also act as acceptor
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-
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ATP + creatine = ADP + phosphocreatine
mitochondrial enzymes, mechanism, overview
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ATP + creatine = ADP + phosphocreatine
mitochondrial enzymes, mechanism, overview
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ATP + creatine = ADP + phosphocreatine
mitochondrial enzymes, mechanism, overview
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ATP + creatine = ADP + phosphocreatine
mitochondrial enzymes, mechanism, overview
-
ATP + creatine = ADP + phosphocreatine
mitochondrial enzymes, mechanism, overview
-
ATP + creatine = ADP + phosphocreatine
mitochondrial enzymes, mechanism, overview
-
ATP + creatine = ADP + phosphocreatine
mitochondrial enzymes, mechanism, overview
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ATP + creatine = ADP + phosphocreatine
mitochondrial enzymes, mechanism, overview
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ATP + creatine = ADP + phosphocreatine
enzyme is functionally coupled to ouabain-inhibited (Na+,K+)-ATPase
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ATP + creatine = ADP + phosphocreatine
random-order rapid-equilibrium mechanism
ATP + creatine = ADP + phosphocreatine
catalytic mechanism and substrate binding involving 2 flexible loops and a specificity pocket formed by Ile69 and Val325 determining substrate specificity, active site structure
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ATP + creatine = ADP + phosphocreatine
bireactant catalytic mechanism, transition state stabilization by six arginines clustered in the active site of the enzyme
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ATP + creatine = ADP + phosphocreatine
catalytic cysteine, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview
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ATP + creatine = ADP + phosphocreatine
catalytic cysteine, active site residues are Glu226, Glu227, and Asp228, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview
ATP + creatine = ADP + phosphocreatine
catalytic cysteine, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview
-
ATP + creatine = ADP + phosphocreatine
catalytic cysteine, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview
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ATP + creatine = ADP + phosphocreatine
catalytic cysteine, active site structure involving His66 and Asp326, overview, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
ATP:creatine N-phosphotransferase
N-Ethylglycocyamine can also act as acceptor.
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CAS REGISTRY NUMBER
COMMENTARY
9001-15-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
creatine kinase activity and protein are 20% lower during hibernation than in euthermia, whereas enzyme mRNA is reduced by 70%. Hibernator creatine kinase shows reduced affinity for ATP and creatine. Soluble enzyme from euthermic squirrels is a mix of phosphorylated and dephosphorylated forms. in hibernating animals only phospho-enzyme is detected
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4 isozymes encoded by 4 different genes: 2 cytosolic isozymes, a muscle-type MM-CK and a brain-type BB-CK or a heterodimer MB-CK, and 2 mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK
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two isoforms, interconversion by reversible oxidation of protein sulfhydryl groups
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642371, 642372, 642373, 642374, 642375, 642376, 642377, 642385, 642410, 642427, 642444, 672391, 676173, 687322
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4 isozymes encoded by 4 different genes: 2 cytosolic isozymes, a muscle-type MM-CK and a brain-type BB-CK or a heterodimer MB-CK, and 2 mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK
Uniprot
-
642371, 642380, 642383, 642385, 642388, 642391, 642407, 642414, 642422, 642430, 642436, 642439, 642442, 642443, 662723, 675781, 675955, 675957, 688203, 688324, 689192, 697687, 701768, 721310, 721916, 722398, 722399, 722684
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2 typical mitochondrial enzyme types, the sarcomeric and the ubiquitous, encoded by 2 different genes
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4 isozymes encoded by 4 different genes: 2 cytosolic isozymes, a muscle-type MM-CK and a brain-type BB-CK or a heterodimer MB-CK, and 2 mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK
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computational approach to study the contribution of side chain residues to the very low pKa value of active site cysteine
Uniprot
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642371, 642378, 642382, 642385, 642394, 642397, 642398, 642399, 642402, 642404, 642406, 642407, 642425, 642427, 642428, 642434, 642445, 642446, 660930, 661270, 671814, 672307, 674788, 674947, 675316, 675415, 675956, 685504, 701761, 702414, 704042, 704051, 722077, 722245
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4 isozymes encoded by 4 different genes: 2 cytosolic isozymes, a muscle-type MM-CK and a brain-type BB-CK or a heterodimer MB-CK, and 2 mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK
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-
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642371, 642385, 642389, 642400, 642403, 642420, 642421, 642423, 642427, 642435, 642440, 671679, 674713, 675240, 685344, 686183, 705501, 705502, 706831, 721956, 722307
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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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the MtCK gene is likely basal and ancestral and has evolved very early in metazoan evolution; the MtCK gene is likely basal and ancestral and has evolved very early in metazoan evolution
malfunction
metabolism
physiological function
additional information
malfunction
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complete brain-type creatine kinase deficiency in mice blocks seizure activity and affects intracellular calcium kinetics
malfunction
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absence of creatine kinase in muscle cells leads to morphological and functional adaptations towards preservation of muscle contractile abilities
malfunction
-
oxygen consumption dynamics during electrical stimulation in superfused fast-twitch hindlimb muscles isolated from wild-type and transgenic mice deficient in the myoplasmic and mitochondrial creatine isoforms (MiM CK-/-), respectively. Transgenic mice deficient in the mitochondrial creatinine isoforms (MiM CK-/-) show muscle oxygen consumption activation kinetics 30% faster than wild-type. MiM CK-/- muscle oxygen consumption deactivation kinetics are 380% faster than wild-type
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; 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
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
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
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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
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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
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malfunction
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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
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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; 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
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
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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
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physiological function
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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
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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
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; 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
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
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
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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
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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
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physiological function
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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
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physiological function
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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
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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; 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; 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
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formation of the disulfide bond between the C74 and the C146 residues in the oxidized form
additional information
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
ADP + phosphocreatine
ATP + creatine
-
synergistic substrate binding, mitochondrial isoform sMiCK
-
-
?
ADP + phosphocreatine
ATP + creatine
-
synergistic substrate binding, muscle-type isoform MCK
-
-
?
ATP + creatine
ADP + creatine phosphate
-
-
-
-
-
ATP + creatine
ADP + creatine phosphate
-
ATP required as MgATP2-
-
-
?
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 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 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 + 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
-
the enzyme is involved in energy homeostasis
-
-
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
-
evolution of enzyme, phylogenetics
-
-
?
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
key enzyme in energy homeostasis
-
-
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
-
the reaction equilibrium lies towards ATP production
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-
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
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regeneration of ATP as primary energy source
-
-
?
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
-
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
-
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
-
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
-
key enzyme in energy homeostasis
-
-
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 + N-ethylglycocyamine
ADP + N-ethylglycocyamine phosphate
-
-
-
-
?
additional information
?
-
-
substrate binding structure, reaction equilibrium is highly influenced by pH and Mg2+ concentration, substrate specificity of isozymes
-
-
-
additional information
?
-
substrate binding structure, reaction equilibrium is highly influenced by pH and Mg2+ concentration, substrate specificity of isozymes
-
-
-
additional information
?
-
-
substrate binding structure, 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
?
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
the enzyme is involved in energy homeostasis
-
-
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
-
evolution of enzyme, phylogenetics
-
-
?
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
P11009
key enzyme in energy homeostasis
-
-
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
-
regeneration of ATP as primary energy source
-
-
?
ATP + creatine
ADP + phosphocreatine
P30275, Q04447
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
-
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
-
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
-
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
-
key enzyme in energy homeostasis
-
-
r
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
?
-
P30275
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
?
-
Q04447
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
?
-
-
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
?
-
P07335
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
?
-
P07335
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
NaCl
Mg2+
-
MgATP2- or MgADP- protect the enzyme from inactivation by 4-hydroxy-3-nitrophenylglyoxal or 2,3-butadiene
Mg2+
-
MgATP2-, at 1 mM, dissociation constants of wild-type and mutant enzymes
Mg2+
-
required as MgATP; required, regulatory effect of Mg2+-concentration
NaCl
-
prevents aggregation of the enzyme during recombinant expression in Escherichia coli
NaCl
-
induces folding of the enzyme unfolded by lactic acid, formation of the molten globule conformation with a compact structure
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
2,3-butadiene
-
complete inhibition, MgATP2- or MgADP- protect the enzyme from inactivation
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
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
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
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
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
-
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
Guanidinoacetate
-
vitamins E and C prevent the effects of intrastriatal administration of guanidinoacetate on the inhibition of creatine kinase
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
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
phosphate
-
competitive against ATP and phosphocreatine, noncompetitive against ADP and creatine
sodium barbital
-
slow inactivation of enzyme that can be reversed by dilution. Sodium barbital may compete mainly with creatine, but also with ATP, for inhibition
sulfate
-
competitive against ATP and phosphocreatine, noncompetitive against ADP and creatine
trans-[RuCl2(3-pyridinecarboxylic acid)4]
-
administration at 180.7 micromol/kg, inhibition of creatine kinase activity in hippocampus, striatum, cerebral cortex, heart and skeletal muscle. No effect on enzyme in vitro
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
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
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
-
70.9% inhibition of the atypical ubiquitous mitochondrial enzyme, 74.6% inhibition of the typical ubiquitous mitochondrial enzyme
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
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
transition state analogue complex
-
consists of creatine, MgADP, and planar ions such as nitrate, nitrite, and formate, binding structure
-
transition state analogue complex
-
creatine, MgADP-, and planar ions such as nitrate, nitrite, and formate
-
Zn2+
-
Zn2+ may induce CK-BB inactivation and misfolding, when the Zn2+ concentration is 0.4 mM, CK-BB activity is completely abolished
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
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
activation of creatine kinase and induction of a state 3-like respiration in isolated brain mitochondria, and prevention of H2O2 production obeys the steady-state kinetics of the enzyme to phosphorylate creatine
aripiprazole
-
activation of enzyme in striatum and cerebral cortex after chronic administration at 10 or 20 mg/kg. No effect on enzyme in hippocampus, cerebellum and prefrontal cortex
ATP
-
activation of creatine kinase and induction of a state 3-like respiration in isolated brain mitochondria, and prevention of H2O2 production obeys the steady-state kinetics of the enzyme to phosphorylate creatine
Creatine
-
activation of creatine kinase and induction of a state 3-like respiration in isolated brain mitochondria, and prevention of H2O2 production obeys the steady-state kinetics of the enzyme to phosphorylate creatine
olanzapine
-
activation of enzyme in striatum after chronic administration at 10 mg/kg
trans-[RuCl2(3,4-pyridinedicarboxylic acid)4]
-
administration at 180.7 micromol/kg, increase of creatine kinase activity in hippocampus, striatum, cerebral cortex and heart, but not in skeletal muscle. No effect on enzyme in vitro
trans-[RuCl2(3,5-pyridinedicarboxylic acid)4]
-
administration at 180.7 micromol/kg, increase of creatine kinase activity in hippocampus, striatum, cerebral cortex and heart, but not in skeletal muscle. No effect on enzyme in vitro
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
ATP
-
hybrid form consisting of muscle and brain creatine kinase isoforms, pH and temperature not specified in the publication
0.34
ATP
-
isoform III isolated after expression in Escherichia coli, pH 8.0, 30°C
0.36
ATP
-
isoform II isolated after expression in Escherichia coli, pH 8.0, 30°C
0.4
ATP
-
wild-type and isoform I isolated after expression in Escherichia coli, pH 8.0, 30°C
0.43
ATP
-
isoform IV isolated after expression in Escherichia coli, pH 8.0, 30°C
0.58
ATP
25°C, pH not specified in the publication, mutant A205S; 25°C, pH not specified in the publication, mutant Q46E
0.74
ATP
-
25°C, pH not specified in the publication, mutant K304T; 25°C, pH not specified in the publication, mutant L36K
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
1.75
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; no organotellurium, preincubation time 5 min, mitochondrial fraction, including reduced glutathione (GSH), pH 7.5, 37°C
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
3.92
ATP
-
0.020 mM organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37°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
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
2 - 3
Creatine
-
isoform I isolated after expression in Escherichia coli, pH 8.0, 30°C
3.26
Creatine
-
enzyme from embryonic stem cell-derived cardiomyocytes, pH 6.5, 37°C
3.9
Creatine
-
wild-type hBBCK, pH and temperature not specified in the publication
5
Creatine
-
hybrid form consisting of muscle and brain creatine kinase isoforms, pH and temperature not specified in the publication
6.2
Creatine
-
wild-type hMMCK, pH and temperature not specified in the publication
19
Creatine
-
isoform II isolated after expression in Escherichia coli, pH 8.0, 30°C
20
Creatine
-
isoform III isolated after expression in Escherichia coli, pH 8.0, 30°C
21
Creatine
-
wild-type and isoform IV isolated after expression in Escherichia coli, pH 8.0, 30°C
1.9 - 2.2
creatine phosphate
-
acetylcholine receptor membrane-associated enzyme
0.22
MgATP2-
-
pH 9.0, 30°C, recombinant wild-type enzyme, with substrate creatine
0.29
MgATP2-
-
pH 9.0, 30°C, recombinant wild-type enzyme, with substrate cyclocreatine
0.62
MgATP2-
-
pH 9.0, 30°C, recombinant wild-type enzyme, with substrate N-ethylglycocyamine
1.6
MgATP2-
-
pH 9.0, 30°C, recombinant mutant R291K; pH 9.0, 30°C, recombinant mutant R340A
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
0.87
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
1.32
phosphocreatine
-
0.005 mM organotellurium, preincubation time 5 min, cytosolic fraction, pH 7.5, 37°C
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
-
effect of temperature on values for MgATP2- and creatine
-
additional information
additional information
-
temperature dependence of reaction, in vivo measurements
-
additional information
additional information
-
dextran strongly increases Km
-
additional information
additional information
-
kinetics, recombinant wild-type and mutant enzymes
-
additional information
additional information
-
kinetics, negative cooperativity
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics, the enzyme shows negative cooperativity and nonidentical active sites
-
additional information
additional information
kinetics, the enzyme shows negative cooperativity and nonidentical active sites
-
additional information
additional information
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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, 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
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kinetics for ADP in mitochondria, enhancing effect of creatine, overview
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additional information
additional information
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kinetics for ADP in mitochondria, enhancing effect of creatine, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
115
ATP
-
isoform III isolated after expression in Escherichia coli, pH 8.0, 30°C