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(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
alpha-P-borano substituted ADP Sp isomer
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strong competitive inhibitor
bovine serum albumin
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no influence on enzyme activity
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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
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-
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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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
guanidine hydrochloride
in the absence of added guanidine hydrochloride, MM-CK activity slightly decreases with NaCl concentration up to 4 M, but a dramatic decline is observed above that value, with full inactivation at 4.5 M. When guanidine is added, curves with similar shapes are obtained but NaCl concentrations needed to inactivate the enzyme are shifted towards lower values
Guanidinium chloride
inhibitory, in presence of NaCl, increased inhibitory activity. Inactivation by NaCl is due to dissociation of dimeric creatine kinase into its constitutive subunits, and upon monomerization, the protein becomes more susceptible to guanidinium denaturing effect
guanidinium hydrochloride
Guanidinoacetate
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vitamins E and C prevent the effects of intrastriatal administration of guanidinoacetate on the inhibition of creatine kinase
H2O2
irreversible inhibition. H2O2 interacts with the ADP binding region of the active site of the enzyme. Enzymatic activity is rapidly abolished with less than 1 mM H2O2. Any residual activity is completely lost at an H2O2 concentration of 2-10 mM; irreversible inhibition. The enzyme activity rapidly abolishes with less than 1 mM H2O2. Any residual activity is completely lost at an H2O2 concentration of 2-10 mM. Adding reducing agents such as 2 mM dithiothreitol, 4 mM N-acetyl-l-cysteine, or 4 mM reduced L-glutathione before H2O2 treatment prevents against inactivation caused by 0.5 mM H2O2. However, if antioxidants are added 1 h after addition of 0.5 mM H2O2, no recovery is observed compared with the H2O2-treated group
L-arginine
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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
MOPS buffer
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i.e. 3-(N-morpholino)propane sulfonate
morphine
0.00001-0.1 mM morphine significantly reduces recombinant enzymatic activity (27% inhibition at 0.001 mM, 80% inhibition at more than 0.05 mM); 27% inhibition at 0.001 m, 80% inhibition at more than 0.05 mM
p-hydroxymercuribenzoate
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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
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
thiosulfate
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0.5 mM thiosulfate administration decreases the enzyme activity 30 min after administration. Thiosulfate also decreases the activity of the enzyme in vitro in striatum of rats, which is prevented by the thiol reducing agents dithiothreitol, the antioxidants glutathione, melatonin, trolox, and lipoic acid; thiosulfate (1 M) inhibits creatine kinase activity in rat striatum via thiol group oxidation is prevented by the thiol reducing agents dithiothreitol GSH, melatonin, trolox and lipoic acid
trans-[RuCl2(3-pyridinecarboxylic acid)4]
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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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4-hydroxymercuribenzoic acid
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complete inhibition at 0.01 mM
4-hydroxymercuribenzoic acid
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5,5'-dithiobis(2-nitrobenzoate)
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5,5'-dithiobis(2-nitrobenzoate)
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5,5'-dithiobis(2-nitrobenzoate)
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5,5'-dithiobis(2-nitrobenzoate)
less than 5% residual activity at 0.1 mM
Acrylamide
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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
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CK-BB is kinetically reversibly inactivated by acrylamide accompanied by the disruption of the hydrophobic surface, complete inhibition at 800 mM
Cl-
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Cl-
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inactivation at -17°C
Co2+
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Creatinine phosphate
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competitive to phosphocreatine
Creatinine phosphate
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competitive to MgATP2-
cystine
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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
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cystine inhibited the enzyme activity in a dose- and time-dependent manner and cysteamine prevents and reverses the inhibition caused by cystine, suggesting that cystine inhibits creatine kinase activity by oxidation of the sulfhydryl groups of the enzyme; dose- and time-dependent inhibition, cysteamine prevents and reverses this inhibition
formate
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mimics the phosphoryl group in the transition state
formate
mimics the phosphoryl group in the transition state
formate
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mimics the phosphoryl group in the transition state
formate
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mimics the phosphoryl group in the transition state
formate
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mimics the phosphoryl group in the transition state
guanidinium hydrochloride
0.1-3.0 M, under both conditions, the tag-free enzyme shows the lowest degree of aggregation, followed by His-tagged CK, and Fc-III-tagged CK has the highest degree of aggregation
guanidinium hydrochloride
inactivation mechanism of wild-type and mutant enzymes, overview
guanidinium hydrochloride
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first dissociation of subunits, then unfolding into random coil
iodoacetamide
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substrates can protect against alkylation
iodoacetamide
substrates can protect against alkylation
iodoacetamide
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substrates can protect against alkylation
iodoacetamide
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70.9% inhibition of the atypical ubiquitous mitochondrial enzyme, 74.6% inhibition of the typical ubiquitous mitochondrial enzyme
iodoacetamide
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substrates can protect against alkylation
iodoacetamide
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protection by MgATP2-, MgADP-, urea
iodoacetamide
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substrates can protect against alkylation
iodoacetic acid
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jujubogenin
16.9% inhibition at 0.005 mM
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NaCl
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inactivation due to subunit dissociation, mechanism
NaCl
enzyme activity slightly decreases with NaCl concentration up to 4 M, and a dramatic decline is observed above that value, with full inactivation at 4.5 M. In presence of guanidinium chloride, inactivation occurs much earlier. Inactivation by NaCl is due to dissociation of dimeric creatine kinase into its constitutive subunits, and upon monomerization, the protein becomes more susceptible to guanidinium denaturing effect; in the absence of added guanidine hydrochloride, MM-CK activity slightly decreases with NaCl concentration up to 4 M, but a dramatic decline is observed above that value, with full inactivation at 4.5 M. When guanidine is added, curves with similar shapes are obtained but NaCl concentrations needed to inactivate the enzyme are shifted towards lower values
nitrate
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mimics the phosphoryl group in the transition state
nitrate
mimics the phosphoryl group in the transition state
nitrate
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mimics the phosphoryl group in the transition state
nitrate
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mimics the phosphoryl group in the transition state
nitrate
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mimics the phosphoryl group in the transition state
nitrite
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mimics the phosphoryl group in the transition state
nitrite
mimics the phosphoryl group in the transition state
nitrite
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mimics the phosphoryl group in the transition state
nitrite
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mimics the phosphoryl group in the transition state
nitrite
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mimics the phosphoryl group in the transition state
NO3-
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NO3-
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inactivation at -17°C
SDS
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strongly inhibits the CK-BB activity in a noncompetitive manner, although almost all the activity is eliminated by SDS CK-BB is never completely inactivated (4% to 5% activity is still sustained), regardless of increased incubation time or SDS concentration
SDS
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dissociation of subunits, no unfolding
transition state analogue complex
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consists of creatine, MgADP, and planar ions such as nitrate, nitrite, and formate, binding structure
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transition state analogue complex
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creatine, MgADP-, and planar ions such as nitrate, nitrite, and formate
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Zn2+
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Zn2+
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Zn2+ may induce CK-BB inactivation and misfolding, when the Zn2+ concentration is 0.4 mM, CK-BB activity is completely abolished
additional information
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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
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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
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additional information
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lansoprazole at 0.003 mg/ml does not alter DNA integrity of human spermatozoa or activity of seminal creatine kinase after 1 h incubation period; there is no significant change in the activity of seminal creatine kinase by the effect of lansoprazole (0.003 mg/ml, 1 h incubation)
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additional information
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haloperidol, no effect on enzyme. Aripiprazole, no effect on enzyme in hippocampus, cerebellum and prefrontal cortex
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additional information
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no effect: trans-[RuCl2(4-pyridinecarboxylic acid)4]
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additional information
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cysteamine, glutathione, and sodium acetate does not affect cytosolic and mitochondrial creatine kinase activity
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additional information
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brain creatine kinase activity is lower on days 14 and 21 post-feeding in animals that receive aflatoxin B1-contaminated diet compared to the control group. The inhibition of brain enzyme activity appears to be mediated by the oxidation of lipids, proteins, and thiol group, as well as by a reduction in the antioxidant capacity
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