2.7.3.2: creatine kinase
This is an abbreviated version!
For detailed information about creatine kinase, go to the full flat file.
Word Map on EC 2.7.3.2
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2.7.3.2
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myocardial
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cardiac
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infarct
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coronary
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artery
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ventricular
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troponin
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ischemia
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muscular
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reperfusion
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pain
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myopathy
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aminotransferase
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necrosis
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myoglobin
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rhabdomyolysis
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admission
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admitted
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dystrophy
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chest
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cytokeratins
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postoperative
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cardioprotective
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alt
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hemodynamic
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ejection
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fatigue
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percutaneous
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c-reactive
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angina
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soreness
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thrombolysis
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angioplasty
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electrocardiograph
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myalgia
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st-segment
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arrhythmia
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exercise-induced
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echocardiography
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cardiopulmonary
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eccentric
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langendorff
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athlete
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duchenne
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electromyography
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angiographic
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perioperative
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in-hospital
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revascularization
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diagnostics
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biotechnology
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reperfused
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medicine
- 2.7.3.2
- myocardial
- cardiac
- infarct
- coronary
- artery
- ventricular
- troponin
- ischemia
- muscular
-
reperfusion
- pain
- myopathy
- aminotransferase
- necrosis
- myoglobin
- rhabdomyolysis
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admission
-
admitted
- dystrophy
- chest
-
cytokeratins
-
postoperative
-
cardioprotective
-
alt
-
hemodynamic
-
ejection
-
fatigue
-
percutaneous
-
c-reactive
- angina
- soreness
-
thrombolysis
-
angioplasty
-
electrocardiograph
- myalgia
-
st-segment
- arrhythmia
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exercise-induced
-
echocardiography
-
cardiopulmonary
-
eccentric
-
langendorff
-
athlete
-
duchenne
-
electromyography
-
angiographic
-
perioperative
-
in-hospital
-
revascularization
- diagnostics
- biotechnology
-
reperfused
- medicine
Reaction
Synonyms
adenosine triphosphate-creatine transphosphorylase, adenosine-5'-triphosphate: creatine phosphotransferase, ATP-creatine transphosphorylase, ATP: creatine N-phosphotransferase, ATP:creatine phosphotransferase, B-type creatine kinase, BB-CK, BB-type creatine kinase, BCK, brain creatine kinase, brain type creatine kinase, brain-type CK, brain-type creatine kinase, CK, CK MM, CK-B, CK-BB, CK-MB, CK-MM, ckb, CKM, CKMB, CKMBI, CKMiMi, creatine kinase, creatine kinase B, creatine kinase M-type, creatine kinase MB, creatine kinase muscle type, creatine kinase-MB, creatine N-phosphotransferase, creatine phosphokinase, creatine phosphotransferase, creatinine kinase, creatinine kinase MB, hBBCK, hMMCK, kinase, creatine (phosphorylating), M-CK, M1-CK, MB-CK, MCK, Mi-CK, MiMi-CK, mit-CK, mitochondrial creatine kinase, MM-CK, MM-type creatine kinase, More, MtCK, muscle creatine kinase, muscle type creatine kinase, muscle-type creatine kinase, phosphocreatine kinase, plasma creatine kinase, PSCKM, recombinant human brain-type creatine kinase, rHBCK, RM-CK, s-type CK, sarcomeric CK, sMiCK, sMtCK, u-type CK, ubiquitous CK, ubiquitous MtCK, uMiCK, uMtCK, zMMCK
ECTree
2.7.3.2 creatine kinaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.7.3.2 - creatine kinase
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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
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the SP-ADPalphaB isomer is a 70fold better substrate for creatine kinase than the RP isomer
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-
?
alpha-(SP)-borano-ADP + phosphocreatine
alpha-(SP)-borano-ATP + creatine
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the SP-ADPalphaB isomer is a 70fold better substrate for creatine kinase than the RP isomer
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-
?
ADP + phosphocreatine
ATP + creatine
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synergistic substrate binding, mitochondrial isoform sMiCK
-
-
?
ADP + phosphocreatine
ATP + creatine
-
synergistic substrate binding, muscle-type isoform MCK
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-
?
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 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
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642382, 642394, 642397, 642398, 642399, 642402, 642406, 642407, 672307, 674788, 702414, 704042, 704051
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-
?
ATP + creatine
ADP + creatine phosphate
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ATP required as MgATP2-
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r
ATP + creatine
ADP + creatine phosphate
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ATP required as MgATP2-
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-
r
ATP + creatine
ADP + creatine phosphate
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creatine cannot be replaced by creatinine
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-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + creatine phosphate
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ATP required as MgATP2-
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r
ATP + creatine
ADP + creatine phosphate
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Mg-complexes of ATP and ADP are the true substrates for the mitochondrial enzymes
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-
r
ATP + creatine
ADP + phosphocreatine
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physiological roles: 1. buffering of ADP/ATP ratio, 2. transport of high-energy phosphates from sites of ATP production to sites of ATP consumption
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-
r
ATP + creatine
ADP + phosphocreatine
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the enzyme is involved in energy homeostasis
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-
r
ATP + creatine
ADP + phosphocreatine
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physiological roles: 1. buffering of ADP/ATP ratio, 2. transport of high-energy phosphates from sites of ATP production to sites of ATP consumption
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-
r
ATP + creatine
ADP + phosphocreatine
the enzyme has a 20fold greater preference for creatine compared to glycocyamine
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-
?
ATP + creatine
ADP + phosphocreatine
the enzyme shows a 20fold greater preference for creatine than glycocyamine
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-
?
ATP + creatine
ADP + phosphocreatine
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evolution of enzyme, phylogenetics
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-
?
ATP + creatine
ADP + phosphocreatine
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mitochondrial model of CK in energy transport
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-
r
ATP + creatine
ADP + phosphocreatine
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physiological roles: 1. buffering of ADP/ATP ratio, 2. transport of high-energy phosphates from sites of ATP production to sites of ATP consumption
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-
r
ATP + creatine
ADP + phosphocreatine
key enzyme in energy homeostasis
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-
r
ATP + creatine
ADP + phosphocreatine
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physiological roles: 1. buffering of ADP/ATP ratio, 2. transport of high-energy phosphates from sites of ATP production to sites of ATP consumption
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-
r
ATP + creatine
ADP + phosphocreatine
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the reaction equilibrium lies towards ATP production
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-
r
ATP + creatine
ADP + phosphocreatine
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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
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-
?
ATP + creatine
ADP + phosphocreatine
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regeneration of ATP as primary energy source
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-
?
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
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-
r
ATP + creatine
ADP + phosphocreatine
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physiological roles: 1. buffering of ADP/ATP ratio, 2. transport of high-energy phosphates from sites of ATP production to sites of ATP consumption
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-
r
ATP + creatine
ADP + phosphocreatine
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overview on physiological roles
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-
?
ATP + creatine
ADP + phosphocreatine
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key enzyme in energy homeostasis
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-
r
ATP + creatine
ADP + phosphocreatine
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coupled to (Na+,K+)ATPase system
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-
r
ATP + creatine
ADP + phosphocreatine
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physiological roles: 1. buffering of ADP/ATP ratio, 2. transport of high-energy phosphates from sites of ATP production to sites of ATP consumption
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-
r
ATP + creatine
ADP + phosphocreatine
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overview on physiological roles
-
-
?
ATP + creatine
ADP + phosphocreatine
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key enzyme of energy homeostasis
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-
r
ATP + creatine
ADP + phosphocreatine
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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
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key enzyme in energy homeostasis
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-
r
ATP + cyclocreatine
ADP + phospho-cyclocreatine
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i.e. 1-carboxymethyl-2-iminoimidazolidine
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-
?
ATP + cyclocreatine
ADP + phospho-cyclocreatine
i.e. 1-carboxymethyl-2-iminoimidazolidine
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-
?
ATP + cyclocreatine
ADP + phospho-cyclocreatine
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i.e. 1-carboxymethy-2-iminoimidazolidine
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-
?
ATP + glycocyamine
ADP + glycocyamine phosphate
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very low activity
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-
?
ATP + N-ethylglycocyamine
ADP + N-ethylglycocyamine phosphate
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-
-
-
?
additional information
?
-
-
substrate binding structure, reaction equilibrium is highly influenced by pH and Mg2+ concentration, substrate specificity of isozymes
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-
?
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
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-
?
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
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
-
the enzyme binds to 1,2-dipalmitoyl-sn-glycero-3-phosphate with the highest affinity (dissociation constant: 0.002 mM)
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-
-
additional information
?
-
-
the enzyme binds to 1,2-dipalmitoyl-sn-glycero-3-phosphate with the highest affinity (dissociation constant: 0.002 mM)
-
-
-
additional information
?
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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
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-
-
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
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-
-
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
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-
?
additional information
?
-
-
ATP undergoes substrate channelling between enzyme and myosin ATPase
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-
?
additional information
?
-
-
enzyme inhibition, e.g. by branched chain alpha-amino acids, might contribute to the brain damage maple syrup urine disease MSUD
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-
?
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
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-
?
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
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-
?
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
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-
?
additional information
?
-
-
probable enzyme evolution, overview
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-
?
additional information
?
-
-
substrate binding structure, substrate binding at both subunits
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-
?
