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Information on EC 2.7.3.2 - creatine kinase
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2.7.3.2 creatine kinaseIUBMB Comments
N-Ethylglycocyamine can also act as acceptor.
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Word Map
- 2.7.3.2
- myocardial
- cardiac
- infarct
- coronary
- artery
- ventricular
- troponins
-
reperfusion
- muscular
- pain
- ischemia
- necrosis
- aminotransferase
- myopathy
- myoglobin
- dystrophy
-
admission
- renal
- chest
- rhabdomyolysis
- anterior
-
cytokeratins
-
cardioprotective
-
postoperative
-
admitted
-
ejection
-
percutaneous
-
c-reactive
- angina
-
hemodynamic
-
angioplasty
-
exercise-induced
- tachycardia
-
st-segment
-
duchenne
- arrhythmia
-
isometric
-
fatigue
-
angiographic
-
perioperative
-
thrombolysis
-
echocardiography
-
athlete
-
electrocardiograph
-
cardiopulmonary
-
eccentric
-
revascularization
-
langendorff
-
in-hospital
- biotechnology
- diagnostics
- medicine
-
reperfused
The enzyme appears in viruses and cellular organisms
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
BCK
brain creatine kinase
brain-type CK
brain-type creatine kinase
CK
CK MM
CK-BB
CK-MB
-
-
-
-
CK-MM
-
-
-
-
ckb
CKMiMi
-
-
-
-
creatine kinase
creatine phosphokinase
-
-
-
-
creatine phosphotransferase
-
-
-
-
kinase, creatine (phosphorylating)
-
-
-
-
MB-CK
-
-
-
-
MCK
Mi-CK
-
-
-
-
MiMi-CK
-
-
-
-
mitochondrial creatine kinase
MM-CK
MtCK
muscle creatine kinase
muscle-type creatine kinase
phosphocreatine kinase
-
-
-
-
plasma creatine kinase
sMiCK
uMtCK
additional information
BB-CK
-
-
-
-
CK
-
-
-
-
CK-BB
-
-
-
-
MM-CK
-
-
-
-
additional information
-
the enzyme is a member of the phosphagen (guanidino) kinase family
additional information
-
the enzyme is a member of the phosphagen (guanidino) kinase family
additional information
-
the enzyme is a member of the phosphagen (guanidino) kinase family
additional information
-
the enzyme is a member of the phosphagen kinase superfamily of enzymes
additional information
-
the enzyme is a member of the phosphagen (guanidino) kinase family
additional information
-
the enzyme is a member of the phosphagen (guanidino) kinase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + creatine = ADP + phosphocreatine
; N-ethylglycocyamine can also act as acceptor
-
-
-
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
-
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
-
ATP + creatine = ADP + phosphocreatine
enzyme is functionally coupled to ouabain-inhibited (Na+,K+)-ATPase
-
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
-
ATP + creatine = ADP + phosphocreatine
bireactant catalytic mechanism, transition state stabilization by six arginines clustered in the active site of the enzyme
-
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
-
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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PATHWAY SOURCE
PATHWAYS
MetaCyc
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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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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
-
-
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
-
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
?
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-
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 SUBSTRATE
NATURAL 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
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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INHIBITOR
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
A0A0A1IVI8
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
kinetics for ADP in mitochondria, enhancing effect of creatine, overview
-
additional information
additional information
-
kinetics for ADP in mitochondria, enhancing effect of creatine, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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; co-substrate: ATP, 25°C, pH not specified in the publication, mutant S329A
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
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
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
additional information
additional information
-
comparison of kinetic constants with enzymes from Mus musculus, Lampetra japonica, Neanthes diversicolor, Dendronephthya gigantea
-
additional information
additional information
-
comparison of kinetic constants with enzymes from Mus musculus, Danio rerio, Lampetra japonica, Neanthes diversicolor
-
additional information
additional information
-
comparison of kinetic constants with enzymes from Mus musculus, Danio rerio, Lampetra japonica, Dendronephthya gigantea
-
additional information
additional information
-
comparison of kinetic constants with enzymes from Mus musculus, Danio rerio, Neanthes diversicolor, Dendronephthya gigantea
-
additional information
additional information
-
comparison of kinetic constants with enzymes from Danio rerio, Lampetra japonica, Neanthes diversicolor, Dendronephthya gigantea
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
0.020 mM organotellurium, preincubation time 5 min including reduced glutathione (GSH), phosphocreatine variable, cytosolic fraction, pH 7.5, 37°C
additional information
additional information
-
inhibition kinetics with 4-hydroxy-3-nitrophenylglyoxal, overview
-
additional information
additional information
-
inactivation rate constants for enzyme PSCKM by Cd2+., overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
181
A0A0A1IVI8
purified native octameric enzyme, pH and temperature not specified in the publication; purified native octameric enzyme, pH and temperature not specified in the publication
261