Information on EC 2.7.3.2 - creatine kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.3.2
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RECOMMENDED NAME
GeneOntology No.
creatine kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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creatine-phosphate biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
ATP:creatine N-phosphotransferase
N-Ethylglycocyamine can also act as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-15-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Antarctic icefish
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Manually annotated by BRENDA team
recombinant mitochondrial isoform
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
tropical fruit bat
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Frog
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Manually annotated by BRENDA team
atlantic cod
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Manually annotated by BRENDA team
nurse shark
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Manually annotated by BRENDA team
recombinant cytoplasmic and mitochondrial isoforms
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-
Manually annotated by BRENDA team
green sunfish
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Manually annotated by BRENDA team
recombinant cytoplasmic isoforms M1, M2, and B
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
67 R6/2 mice and 31 wild-type B6CBAFI/J mice, gene Ckb
UniProt
Manually annotated by BRENDA team
rainbow trout
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Manually annotated by BRENDA team
red sea bream
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Manually annotated by BRENDA team
monkey
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
pacific mackerel
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Manually annotated by BRENDA team
dogfish
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
turtle
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Manually annotated by BRENDA team
syn. Pseudemys scripta elegans, freshwater turtle
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Manually annotated by BRENDA team
trout
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Manually annotated by BRENDA team
creatine kinase activity and protein are 20% lower during hibernation than in euthermia, whereas enzyme mRNA is reduced by 70%. Hibernator creatine kinase shows reduced affinity for ATP and creatine. Soluble enzyme from euthermic squirrels is a mix of phosphorylated and dephosphorylated forms. in hibernating animals only phospho-enzyme is detected
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
alpha-(RP)-borano-ADP + phosphocreatine
alpha-(RP)-borano-ATP + creatine
show the reaction diagram
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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
show the reaction diagram
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the SP-ADPalphaB isomer is a 70fold better substrate for creatine kinase than the RP isomer
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?
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
ATP + cyclocreatine
ADP + phospho-cyclocreatine
show the reaction diagram
ATP + glycocyamine
ADP + glycocyamine phosphate
show the reaction diagram
ATP + N-ethylglycocyamine
ADP + N-ethylglycocyamine phosphate
show the reaction diagram
dADP + phosphocreatine
?
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MgADP-
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MgATP2-
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NADH
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activation of cytosolic enzyme in the direction of ATP-formation
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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can substitute for Mg2+
Mn2+
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required
Zn2+
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can substitute for Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2Z)-3-butyl-1-phenyl-2-(phenyltellanyl)oct-2-en-1-one
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organotellurium inhibits creatine kinase activity by two different mechanisms: competition with ADP and oxidation of critical sulfhydryl groups for the functioning of the enzyme
1-anilinonaphthalene-8-sulfonate
unfolding agent
2,3-butadiene
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complete inhibition, MgATP2- or MgADP- protect the enzyme from inactivation
4,4'-dithiodipyridine
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4-hydroxy-2-nonenal
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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
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complete inactivation, modification of 2 arginine residues per enzyme subunit, inhibition kinetics at pH 8.7, MgATP2- or MgADP- protect the enzyme from inactivation
4-hydroxymercuribenzoic acid
5,5'-dithiobis(2-nitrobenzoate)
5-(4-([(benzoylphenyl)amino]carbonyl)phenyl)-2-furoic acid
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35% inhibition, docking energy -49.5 kcal/mol
5-(4-([(biphenyl-4-ylmethyl)amino]carbony)phenyl)-2-furoic acid
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63% inhibition, docking energy -51.8 kcal/mol
5-(4-benzoylbiphenyl-4-yl)-2-furoic acid
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; 63% inhibition, docking energy -46.3 kcal/mol
5-(4-[(benzylamino)carbonyl]phenyl)-2-furoic acid
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20% inhibition, docking energy -47.4 kcal/mol
5-(4-[[(benzoylphenyl)amino]carbonyl]phenyl)-2-furoic acid
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5-(4-[[(biphenyl-4-ylmethyl)amino]carbony]phenyl)-2-furoic acid
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5-[4-[(benzylamino)carbonyl]phenyl]-2-furoic acid
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acetaminophen
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inhibits creatine kinase in cerebellum and hippocampus, the administration of N-acetylcysteine plus deferoxamine reverses the inhibition of creatine kinase activity
Acrylamide
alpha-P-borano substituted ADP Sp isomer
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strong competitive inhibitor
Bis-Tris
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bovine serum albumin
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no influence on enzyme activity
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Ca2+
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carbon tetrachloride
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inhibits creatine kinase activity in cerebellum, the administration of N-acetylcysteine plus deferoxamine reverses the inhibition of creatine kinase activity
catechin
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Cd2+
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Cd2+ conspicuously inactivates the activity of the muscle-type enzyme in a first-order kinetic process and exhibits non-competitive inhibition with creatine and ATP. Cd2+ induces tertiary structure changes in enzyme PSCKM with exposure of hydrophobic surfaces. The addition of osmolytes, such as glycine and proline, partially reactivates the enzyme. Molecular dynamics and docking simulations between PSCKM and Cd2+ show that Cd2+ blocks the entrance of ATP to the active site of the enzyme, computational modeling, overview
Chromium ADP
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competitive to MgADP-
Chromium ATP
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competitive to MgATP2-
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clozapine
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inhibition of enzyme in cerebellum and prefrontal cortex after chronic administration
copper metabolism gene MURR1 domain 6
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0.006 mg is capable of inhibiting the activities of both the MM- and BB-type creatine kinases
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Creatinine phosphate
Cu2+
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cystine
cystine dimethylester
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ethylmalonic acid
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accumulation in patients affected by short-chain acyl-CoA dehydrogenase deficiency and other diseases. Ethylmalonic acid inhibits the activity of respiratory chain complexes and also inhibits creatine kinase at concentrations o 1 mM and 5 mM
Fe3+
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formate
guanidine hydrochloride
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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
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inhibitory, in presence of NaCl, increased inhibitory activity. Inactivation by NaCl is due to dissociation of dimeric creatine kinase into its constitutive subunits, and upon monomerization, the protein becomes more susceptible to guanidinium denaturing effect
guanidinium hydrochloride
Guanidinoacetate
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vitamins E and C prevent the effects of intrastriatal administration of guanidinoacetate on the inhibition of creatine kinase
imidazole
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iodoacetamide
iodoacetic acid
Iodoethane
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L-arginine
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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. 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
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branched chain alpha-amino acids bind at the active site, competitive inhibition mechanism against substrates phosphocreatine and ADP, inhibition kinetics
L-leucine
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branched chain alpha-amino acids bind at the active site, competitive inhibition mechanism against substrates phosphocreatine and ADP, inhibition kinetics
L-lysine
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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
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branched chain alpha-amino acids bind at the active site, competitive inhibition mechanism against substrates phosphocreatine and ADP, inhibition kinetics
Lactic acid
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induces dissociation of enzyme dimer and unfolding of the enzyme at 0.8 mM, but no aggregation at 25°C or 40°C even at high protein concentrations, inactivation kinetics
LiCl
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inactivation due to subunit dissociation, mechanism
luteolin
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MOPS buffer
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i.e. 3-(N-morpholino)propane sulfonate
N-ethylmaleimide
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nitrate
nitrite
NO2-
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p-hydroxymercuribenzoate
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Pb2+
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lead inhibits in vitro the cytosolic and mitochondrial creatine kinase activity at 0.2 mM and that this inhibition is prevented by addition cysteamine to the assay at 0.1 mM and 0.5 mM final concentration
Phenylglyoxal
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complete inactivation, reacts on arginine residues
phosphate
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competitive against ATP and phosphocreatine, noncompetitive against ADP and creatine
Pipes buffer
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i.e. 1,4-piperazine diethanesulfonic acid
quercetin
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mechanism, role of radicals
SO32-
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SO42-
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sodium barbital
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slow inactivation of enzyme that can be reversed by dilution. Sodium barbital may compete mainly with creatine, but also with ATP, for inhibition
sulfate
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competitive against ATP and phosphocreatine, noncompetitive against ADP and creatine
taxifolin
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trans-[RuCl2(3-pyridinecarboxylic acid)4]
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administration at 180.7 micromol/kg, inhibition of creatine kinase activity in hippocampus, striatum, cerebral cortex, heart and skeletal muscle. No effect on enzyme in vitro
transition state analogue complex
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Tris
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additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
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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
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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
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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
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activation of creatine kinase and induction of a state 3-like respiration in isolated brain mitochondria, and prevention of H2O2 production obeys the steady-state kinetics of the enzyme to phosphorylate creatine
NADH
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lowers Km for phosphocreatine 3fold
olanzapine
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activation of enzyme in striatum after chronic administration at 10 mg/kg
trans-[RuCl2(3,4-pyridinedicarboxylic acid)4]
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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]
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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
additional information
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increase of enzymatic activity post-exercise
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.027 - 0.33
ADP
1
alpha-(RP)-borano substituted ADP
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0.008
alpha-(SP)-borano substituted ADP
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-
0.11 - 20
ATP
0.35 - 167
Creatine
0.23 - 50
creatine phosphate
0.015 - 1.2
MgADP-
0.042 - 10.3
MgATP2-
0.51 - 8.97
phosphocreatine
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
78.3 - 483.3
ADP
0.06
alpha-(RP)-borano substituted ADP
Oryctolagus cuniculus
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0.03
alpha-(SP)-borano substituted ADP
Oryctolagus cuniculus
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-
36.4 - 215
ATP
0.08 - 417
Creatine
1.5 - 35.2
cyclocreatine
0.08 - 148
MgATP2-
0.55 - 14.5
N-ethylglycocyamine
78.3 - 483.3
phosphocreatine
additional information
additional information
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