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Information on EC 2.7.3.2 - creatine kinase and Organism(s) Oryctolagus cuniculus and UniProt Accession P00563

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EC Tree
IUBMB Comments
N-Ethylglycocyamine can also act as acceptor.
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This record set is specific for:
Oryctolagus cuniculus
UNIPROT: P00563
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Word Map
The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
ck, creatine kinase, ck-mb, creatine phosphokinase, creatine kinase-mb, creatinine kinase, creatine kinase mb, ck-bb, plasma creatine kinase, mitochondrial creatine kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
muscle creatine kinase
-
muscle-type creatine kinase
-
adenosine triphosphate-creatine transphosphorylase
-
-
-
-
ATP-creatine transphosphorylase
-
-
ATP: creatine N-phosphotransferase
-
-
ATP:creatine phosphotransferase
-
-
-
-
BB-CK
-
-
-
-
BB-type creatine kinase
-
-
brain creatine kinase
-
-
brain type creatine kinase
-
-
CK-BB
CK-MB
-
-
-
-
CK-MM
-
-
-
-
CKMiMi
-
-
-
-
creatine phosphokinase
-
-
-
-
creatine phosphotransferase
-
-
-
-
creatinine kinase
-
-
kinase, creatine (phosphorylating)
-
-
-
-
MB-CK
-
-
-
-
Mi-CK
-
-
-
-
MiMi-CK
-
-
-
-
MM-CK
-
-
-
-
MM-type creatine kinase
-
-
muscle creatine kinase
-
-
phosphocreatine kinase
-
-
-
-
additional information
-
the enzyme is a member of the phosphagen (guanidino) kinase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
random-order rapid-equilibrium mechanism
ATP + creatine = ADP + phosphocreatine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:creatine N-phosphotransferase
N-Ethylglycocyamine can also act as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-15-4
-
SUBSTRATE
PRODUCT                       
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
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
-
-
-
-
?
alpha-(RP)-borano-ADP + phosphocreatine
alpha-(RP)-borano-ATP + creatine
show the reaction diagram
-
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
show the reaction diagram
-
the SP-ADPalphaB isomer is a 70fold better substrate for creatine kinase than the RP isomer
-
-
?
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
-
i.e. 1-carboxymethy-2-iminoimidazolidine
-
-
?
ATP + glycocyamine
ADP + glycocyamine phosphate
show the reaction diagram
-
very low activity
-
-
?
ATP + N-ethylglycocyamine
ADP + N-ethylglycocyamine phosphate
show the reaction diagram
-
-
-
-
?
dADP + phosphocreatine
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
additional information
?
-
-
probable enzyme evolution, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
-
induces folding of the enzyme unfolded by lactic acid, formation of the molten globule conformation with a compact structure
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-anilinonaphthalene-8-sulfonate
unfolding agent
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
inactivation mechanism of wild-type and mutant enzymes, overview
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
5-(4-[(benzylamino)carbonyl]phenyl)-2-furoic acid
-
20% inhibition, docking energy -47.4 kcal/mol
5-(4-[[(benzoylphenyl)amino]carbonyl]phenyl)-2-furoic acid
-
-
5-(4-[[(biphenyl-4-ylmethyl)amino]carbony]phenyl)-2-furoic acid
-
-
5-[4-[(benzylamino)carbonyl]phenyl]-2-furoic acid
-
-
Acrylamide
-
CK-BB is kinetically reversibly inactivated by acrylamide accompanied by the disruption of the hydrophobic surface, complete inhibition at 800 mM
alpha-P-borano substituted ADP Sp isomer
-
strong competitive inhibitor
bovine serum albumin
-
no influence on enzyme activity
-
Chromium ADP
-
competitive to MgADP-
Chromium ATP
-
competitive to MgATP2-
Cl-
-
inactivation at -17°C
copper metabolism gene MURR1 domain 6
-
0.006 mg is capable of inhibiting the activities of both the MM- and BB-type creatine kinases
-
Creatinine phosphate
formate
-
mimics the phosphoryl group in the transition state
guanidinium hydrochloride
-
first dissociation of subunits, then unfolding into random coil
iodoacetamide
iodoacetic acid
-
-
Iodoethane
-
-
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
LiCl
-
inactivation due to subunit dissociation, mechanism
NaCl
-
inactivation due to subunit dissociation, mechanism
nitrate
-
mimics the phosphoryl group in the transition state
nitrite
-
mimics the phosphoryl group in the transition state
NO3-
-
inactivation at -17°C
Phenylglyoxal
-
complete inactivation, reacts on arginine residues
SDS
-
dissociation of subunits, no unfolding
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
Zn2+
-
Zn2+ may induce CK-BB inactivation and misfolding, when the Zn2+ concentration is 0.4 mM, CK-BB activity is completely abolished
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20(R)-protopanaxadiol
significantly increases the enzyme activity
20(S)-protopanaxadiol
best activator
20(S)-protopanaxatriol
significantly increases the enzyme activity
24-COOH-protopanaxadiol
significantly increases the enzyme activity
-
25-OH-protopanaxadiol
significantly increases the enzyme activity
-
ginsenoside Rh2
significantly increases the enzyme activity
panaxadiol
significantly increases the enzyme activity
-
additional information
panaxatriol, ocotillol, ginsenoside Rg1, and ginsenoside Rd have no significant influence on the enzyme activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27 - 0.7
ATP
2.8 - 25
Creatine
0.065 - 0.067
ADP
1
alpha-(RP)-borano substituted ADP
-
-
0.008
alpha-(SP)-borano substituted ADP
-
-
0.37 - 10.3
ATP
6.4 - 167
Creatine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
alpha-(RP)-borano substituted ADP
-
-
0.03
alpha-(SP)-borano substituted ADP
-
-
0.08 - 148
ATP
0.08 - 148
Creatine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
5-(4-([(benzoylphenyl)amino]carbonyl)phenyl)-2-furoic acid
-
-
0.025
5-(4-[[(benzoylphenyl)amino]carbonyl]phenyl)-2-furoic acid
-
-
0.049
alpha-P-borano substituted ADP Sp isomer
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
Zn2+
Oryctolagus cuniculus
-
at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
148
mutant V72A, 25°C
256
mutant C74M, 25°C
258
mutant C74L, 25°C
261
wild-type, 25°C
263
mutant V75A, 25°C
266
mutant C74S, 25°C
272
mutant A76G, 25°C
278
mutant C74A, 25°C
46.5
mutant L115D
8208
mutant G73A, 25°C
94.4
mutant L121D
2.99
-
crude homogenate
205.1
-
after 68.6fold purification
210
-
oxidized form of creatine kinase
261
-
wild-type containing both oxidized and reduced form
274.9
-
reduced form of creatine kinase
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
native enzyme in solution
6 - 7
-
synthesis of ATP
7 - 9
-
assay at
7.5 - 9
-
synthesis of phosphocreatine
8.7
-
synthesis of phosphocreatine
additional information
in comparison to free enzyme in solution, enzyme adsorbed onto silicon wafers presents a shift of the optimal pH value toward alkaline pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
psoas myofibril, study of creatine kinase exchange rates between the myofibrillar M-band and its surroundings. In presence of substrates, the exchange rate of the enzyme slows down indicating an increase in the strength of the bond between creatine kinase and the M-band
Manually annotated by BRENDA team
additional information
-
overview tissue distribution of mitochondrial enzyme
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
overview
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KCRM_RABIT
381
0
43112
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
recombinant mutant R147A, analytical ultracentrifugation
45000
recombinant mutant R147A/R151A, gel filtration and analytical ultracentrifugation
46000
recombinant mutant R147A, gel filtration
47000
67000
recombinant mutant R151A, analytical ultracentrifugation
71000
recombinant mutant D209A, analytical ultracentrifugation
74000
recombinant mutant D209A, gel filtration
81000
recombinant mutant R151A, gel filtration
85000
recombinant wild-type enzyme, gel filtration
86000
recombinant wild-type enzyme, analytical ultracentrifugation
43000
-
monomer
82600
-
cytosolic muscle isozyme, gel filtration
86000
-
homodimer
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
1 * 47000, about, recombinant mutant enzymes D209A, R147A, and R147A/R151A, SDS-PAGE
dimer
homodimer
-
2 * 43000, using NMR chemical-shift perturbation and relaxation experiments designed to study the active site 320s flexible loop of muscle creatine kinase it is shown that each subunit can bind substrates independently
octamer
-
8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
intrachain disulfide bond in oxidized form of enzyme is formed between C74 and C146
additional information
-
enzyme activity depends on free sulfhydryl groups
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of mutant R134K in a transition-state analogue complex. The functional enzyme dimer shows significant structural asymmetry with one monomer in a closed conformation with the active site occupied by the transition-state analogue components craetine, MgADP and nitrate. The other monomer has the two loops that control access to the active site in an open conformation and only MgADP is bound
crystal structure analysis of muscle cytosolic isozyme
-
crystals of the mutant G268N are successfully raised to study the fine structural change around the active site. Results show that one residue mutation in can cause the mutant G268N to exhibit cold-adapted enzyme properties comparable to those of Cyprinus carpio M1-creatine kinase
-
muscle isoform
-
NMR screening of inhibitors docked to the crystal structure of enzyme. A phenylfuroic acid may enter into a pocket adjacent to the nucleotide binding site
-
overview: electron microscopy, X-ray crystallography
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A76G
mutation in the intra-subunit domain-domain interface, similar to wild-type in kinetics and thermal inactivation
C74A
mutation in the intra-subunit domain-domain interface, no significant effect on activity and structure, decrease in stability and reactivation
C74L
mutation in the intra-subunit domain-domain interface, no significant effect on activity and structure, decrease in stability and reactivation
C74M
mutation in the intra-subunit domain-domain interface, no significant effect on activity and structure, decrease in stability and reactivation
C74S
mutation in the intra-subunit domain-domain interface, no significant effect on activity and structure, decrease in stability and reactivation
D209A
site-directed mutagenesis, mutant enzyme appears as a mixture of monomeric and dimeric forms, the monomer shows higher thermolability and sensitivity aginst unfolding by 1-anilinonaphthalene-8-sulfonate due to a higher surface area
G268D
site-directed mutagenesis, the mutant shows increased activity at 10°C and pH 8.0 compared to the wild-type
G268K
site-directed mutagenesis, the mutant shows increased activity at 10°C and pH 8.0 compared to the wild-type
G268L
site-directed mutagenesis, the mutant does not show altered activity at 10°C and pH 8.0 compared to the wild-type
G268N
site-directed mutagenesis, the mutant shows increased activity at 10°C compared to the wild-type
G73A
mutation in the intra-subunit domain-domain interface, decrease in activity and stability
L115D
gradual decrease in enzyme activity and secondary structures, mutation does not affect enzyme inactivation by heat or guanidine hydrochloride. Inactivated mutant cannot recover activity by dilution-initiated refolding
L121D
gradual decrease in enzyme activity and secondary structures, mutation does not affect enzyme inactivation by heat or guanidine hydrochloride. Inactivated mutant cannot recover activity by dilution-initiated refolding
P20G
disruption of subunit cohesion, causing dissociation of the functional homodimer into monomers with reduced catalytic activity
R134K
highly soluble mutant, crystallization data
R147A
site-directed mutagenesis, mutant enzyme is a monomer showing higher thermolability and sensitivity aginst unfolding by 1-anilinonaphthalene-8-sulfonate due to a higher surface area, reduced activity and 89% reduced kcat compared to the wild-type enzyme, the mutant enzyme does not follow a random-order rapid-equilibrium mechanism like the wild-type enzyme, but to an ordered mechanism with creatine binding first
R147A/R151A
site-directed mutagenesis, double mutant enzyme is a monomer showing higher thermolability and sensitivity aginst unfolding by 1-anilinonaphthalene-8-sulfonate due to a higher surface area, 10fold reduced substrate binding and 40% reduced kcat compared to the wild-type enzyme, the mutant enzyme follows a random-order rapid-equilibrium mechanism like the wild-type enzyme
R147A/R151A/D209A
site-directed mutagenesis, the triple mutant enzyme is expressed as insoluble, aggregated protein
R151A
site-directed mutagenesis, mutant enzyme is a dimer, reduced activity compared to the wild-type enzyme
V72A
mutation in the intra-subunit domain-domain interface, decrease in activity and stability
V75A
mutation in the intra-subunit domain-domain interface, no significant effect on activity and structure, decrease in stability and reactivation
W210Y
mutation in the interface of enzyme dimer, dissociates more readily than wild-type to monomer. Dissociation equilibrium constant is 9.7 nM compared to 0.017 nM for wild-type
A267H
-
at pH 7.1 mutant shows 30% higher specific activity than the wild-type at 35°C, in contrast to mutant G268N this mutant shows no cold-adapted characteristics
C146S
-
enzyme preparation contains only reduced form
C254S
-
enzyme preparation contains both oxidized and reduced forms
C283S
-
enzyme preparation contains both oxidized and reduced forms
C74S
-
enzyme preparation contains only reduced form
G286N
-
Km values of the rabbit creatine kinase G268N mutant are similar to those of the wild-type rabbit enzyme, circular dichroism spectra show that the overall secondary structures of the mutant enzyme, at pH 8.0 and 5 °C, are almost identical to the carp M1-creatine kinase enzyme. At pH 7.4-8.0 and 35-10 °C, with a smaller substrate, dADP, specific activities of the mutant enzyme are consistently higher than the wild-type rabbit enzyme. At pH 7.1 mutant shows 23% higher specific activity than the wild-type at 35°C. At pH 7.7 and pH 8.0 at 10°C mutant G268N exhibits 2 to 2.5fold higher specific activity than the wild-type, comparable to Cyprinus carpio M1-creatine kinase. Km and kcat values similar to wild-type
N285A
-
severe loss of activity
N285D
-
severe loss of activity, ordered binding mechanism
N285Q
-
severe loss of activity, random order mechanism, reduced affinity for second substrate
P270G
-
at pH 7.1 mutant shows 30% higher specific activity than the wild-type at 35°C, in contrast to mutant G268N this mutant shows no cold-adapted characteristics
R129A
-
site-directed mutagenesis, inactive mutant
R129K
-
site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme
R131A
-
site-directed mutagenesis, inactive mutant
R131K
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
R235A
-
site-directed mutagenesis, inactive mutant
R235K
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
R291K
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
R319K
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
R340A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
R340K
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
R340Q
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
comparison of various enzymes of various sources
642407
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
inactivation of recombinant mutant R147A/R151A
40 - 43
inactivation of recombinant mutant R151A
41
inactivation of recombinant mutant R147A
45
mutant G73A, inactivation
48
wild-type, stable up to 48°C, mutant V75A, inactivation
51.9
melting temperature of mutant L110D
52.3
melting temperature of wild-type
52.9
melting temperature of mutant L121D
53 - 55
inactivation of recombinant wild-type enzyme
53.6
melting temperature of mutant L115D
58
wild-type, inactivation
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
in the presence of cryoprotectant (sucrose or trehalose), the activities of wild-type and mutant RM-CK enzymes with a hydrophobic residue at 268 are higher, and the effect is more profound at pH 8.0
when incubated with 0.8 M guanidine hydrochloride, MM-CK accumulates as a monomeric molten globule which totally lost its enzymatic activity
isozyme CK-MM is more stable against unfolding by urea up to 3 M, while isozymes CK-BB and CK-MB unfold at lower urea concentrations of 2 M, at 25°C and pH 8.0
-
the activity of the 3-(4-chloro-6-p-glyoxal-phenoxy-1,3,5-triazinylamino)-7-(dimethylamino)-2-methylphenazine-labeled creatine kinase is found to be about 40% of that of the native creatine kinase, which supports that the modified arginine residue by 3-(4-chloro-6-p-glyoxal-phenoxy-1,3,5-triazinylamino)-7-(dimethylamino)-2-methylphenazine is at the active site
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
freeze drying leads to oxidation of isozyme CK-BB
-
660931
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-17°C, inactivation in presence of chloride or nitrate
-
freeze drying leads to oxidation of isozyme CK-BB and rearrangement of isozyme CK-MB
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
DEAE Sepharose column chromatography and Sephadex G-200 gel filtration
-
recombinant soluble monomeric or dimeric mutant enzymes by affinity chromatography, native enzyme from skeletal muscle, at high ionic strength, low temperature, and by fractionation with ethanol, or by affinity and ion exchange chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of soluble wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), triple mutant enzyme R147A/R151A/D209A is expressed as insoluble, aggregated protein
expression of soluble monomeric or dimeric mutants
-
expression of soluble wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
enzyme, inactivated due to unfolding after treatment with lactic acid, refolds in presence of NaCl
-
freeze drying leads to rearrangement of isozyme CK-MB after dissociation of the subunits
-
inhibition of enzyme by sodium barbital may be reveresed by dilution
-
reactivation of 5,5'-dithiobis-(2-nitrobenzoic acid)-modified enzyme by excess of dithiothreitol, kinetics
-
study on enzyme aggregation and reassociation in presence of sodium dodecyl sulfate-cyclodextrin. Aggregation does not occur at concentrations below 0.002 mM or temperature below 17°C. Trapping of monomeric creatine kinase variants such as thiol residue modified enzyme, sodium dodecyl sulfate binding enzyme, cyclodextrin treated enzyme, or dithiothreitol treated enzyme. Reassociation in presence of sodium dodecly sulfate-cyclodextrin follows first-order kinetics
-
study on refolding of creatine kinase after denaturation with guanidine hydrochloride. Mixed macromolecular crowding agents, e.g. CT DNA and Ficoll 70, are more favorable and can reflect the physiological environment more accurately than single crowding agents
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
stability of immobilized enzyme
medicine
-
possible roles in pathology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wyss, M.; Smeitink, J.; Wevers, R.A.; Wallimann, T.
Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism
Biochim. Biophys. Acta
1102
119-166
1992
Bos taurus, Gallus gallus, Columba livia, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Strongylocentrotus purpuratus, Sus scrofa
Manually annotated by BRENDA team
Hershenson, S.; Helmers, N.; Desmueles, P.; Stroud, R.
Purification and crystallization of creatine kinase from rabbit skeletal muscle
J. Biol. Chem.
261
3732-3736
1986
Oryctolagus cuniculus
Manually annotated by BRENDA team
Rudge, J.; Bickerstaff, G.F.
Thermal stability of immobilized creatine kinase
Biochem. Soc. Trans.
12
311-313
1984
Oryctolagus cuniculus
-
Manually annotated by BRENDA team
Blum, H.E.; Deus, B.; Gerok, W.
Mitochondrial creatine kinase from human heart muscle: purification and characterization of the crystallized isoenzyme
J. Biochem.
94
1247-1257
1983
Bos taurus, Gallus gallus, Oryctolagus cuniculus, Homo sapiens, Papio anubis, Rattus norvegicus, Sus scrofa, trout
Manually annotated by BRENDA team
Reddy, S.R.R.; Watts, D.C.
Inhibition of creatine kinase by iodoalkanes. Further appraisal of the essential nature of the reactive thiol group
Biochim. Biophys. Acta
569
109-113
1979
Oryctolagus cuniculus
Manually annotated by BRENDA team
Herasymowych, O.S.; Mani, R.S.; Kay, C.M.
Isolation, purification and characterization of creatine kinase from bovine cardiac muscle
Biochim. Biophys. Acta
534
38-47
1978
Bos taurus, Oryctolagus cuniculus
Manually annotated by BRENDA team
Burgess, A.N.; Liddell, J.M.; Cook, W.; Tweedlie, R.M.; Swan, I.D.A.
Creatine kinase. A new crystal form providing evidence of subunit structural homogeneity
J. Mol. Biol.
123
691-695
1978
Oryctolagus cuniculus
Manually annotated by BRENDA team
Reddy, S.R.R.; Watts, D.C.
Inhibition of rabbit muscle creatine kinase by iodomethane [proceedings]
Biochem. Soc. Trans.
6
553-555
1978
Oryctolagus cuniculus
Manually annotated by BRENDA team
Madelian, V.; Warren, W.A.
Properties of a structurally and functionally altered form of creatine kinase produced in solutions containing chloride and nitrate
Arch. Biochem. Biophys.
184
103-110
1977
Oryctolagus cuniculus
Manually annotated by BRENDA team
Gercken, G.; D"ring, V.
Inhibition of creatine kinase by creatinine phosphate
FEBS Lett.
46
87-91
1974
Oryctolagus cuniculus
Manually annotated by BRENDA team
Schimerlik, M.I.; Clelend, W.W.
Inhibition of creatine kinase by chromium nucleotides
J. Biol. Chem.
248
8418-8423
1973
Oryctolagus cuniculus
Manually annotated by BRENDA team
Keutel, H.J.; Okabe, K.; Jacobs, H.K.; Ziter, F.; Maland, L.; Kuby, S.A.
Studies on adenosine triphosphate transphosphorylases. XI. Isolation of the crystalline adenosine triphosphate-creatine transphosphorylases from the muscle and brain of man, calf, and rabbit; and a preparation of their enzymatically active hybrids
Arch. Biochem. Biophys.
150
648-678
1972
Bos taurus, Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Borders, C.L., Jr.; MacGregor, K.M.; Edmiston, P.L.; Gbeddy, E.R.K.; Thomenius, M.J.; Mulligan, G.B.; Snider, M.J.
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase
Protein Sci.
12
532-537
2003
Oryctolagus cuniculus
Manually annotated by BRENDA team
Ventura-Clapier, R.; Kuznetsov, A.; Veksler, V.; Boehm, E.; Anflous, K.
Functional coupling of creatine kinases in muscles: species and tissue specificity
Mol. Cell. Biochem.
184
231-247
1998
Gallus gallus, Columba livia, Oryctolagus cuniculus, Frog, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Yang, Y.; Zhou, H.M.
Reactivation kinetics of 5,5'-dithiobis-(2-nitrobenzoic acid)-modified creatine kinase reactivated by dithiothreitol
Biochim. Biophys. Acta
1388
190-198
1998
Oryctolagus cuniculus
Manually annotated by BRENDA team
Couthon, F.; Clottes, E.; Vial, C.
High salt concentrations induce dissociation of dimeric rabbit muscle creatine kinase. Physico-chemical characterization of the monomeric species
Biochim. Biophys. Acta
1339
277-288
1997
Oryctolagus cuniculus
Manually annotated by BRENDA team
Rao, J.K.; Bujacz, G.; Wlodawer, A.
Crystal structure of rabbit muscle creatine kinase
FEBS Lett.
439
133-137
1998
Oryctolagus cuniculus
Manually annotated by BRENDA team
Zhu, L.; Fan, Y.X.; Perrett, S.; Zhou, J.M.
Relationship between Kinetic and Equilibrium Folding Intermediates of Creatine Kinase
Biochem. Biophys. Res. Commun.
285
857-862
2001
Oryctolagus cuniculus
Manually annotated by BRENDA team
Tang, H.M.; Ou, W.B.; Zhou, H.M.
Effects of lactic acid and NaCl on creatine kinase from rabbit muscle
Biochem. Cell Biol.
81
1-7
2003
Oryctolagus cuniculus
Manually annotated by BRENDA team
Guo, Z.; Wang, Z.; Wang, X.
Studies on the stability of creatine kinase isozymes
Biochem. Cell Biol.
81
9-16
2003
Oryctolagus cuniculus
Manually annotated by BRENDA team
Cox, J.M.; Davis, C.A.; Chan, C.; Jourden, M.J.; Jorjorian, A.D.; Brym, M.J.; Snider, M.J.; Borders, C.L., Jr.; Edmiston, P.L.
Generation of an active monomer of rabbit muscle creatine kinase by site-directed mutagenesis: the effect of quaternary structure on catalysis and stability
Biochemistry
42
1863-1871
2003
Oryctolagus cuniculus (P00563), Oryctolagus cuniculus
Manually annotated by BRENDA team
Jourden, M.J.; Geiss, P.R.; Thomenius, M.J.; Horst, L.A.; Barty, M.M.; Brym, M.J.; Mulligan, G.B.; Almeida, R.M.; Kersteen, B.A.; Myers, N.R.; Snider, M.J.; Borders, C.L., Jr.; Edmiston, P.L.
Transition state stabilization by six arginines clustered in the active site of creatine kinase
Biochim. Biophys. Acta
1751
178-183
2005
Oryctolagus cuniculus
Manually annotated by BRENDA team
McLeish, M.; Kenyon, G.
Relating structure to mechanism in creatine kinase
Crit. Rev. Biochem. Mol. Biol.
40
1-20
2005
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Tetronarce californica, Gallus gallus (P11009)
Manually annotated by BRENDA team
Ohren, J.F.; Kundracik, M.L.; Borders, C.L.; Edmiston, P.; Viola, R.E.
Structural asymmetry and intersubunit communication in muscle creatine kinase
Acta Crystallogr. Sect. D
63
381-389
2007
Oryctolagus cuniculus (P00563), Oryctolagus cuniculus
Manually annotated by BRENDA team
Awama, A.M.; Mazon, H.; Vial, C.; Marcillat, O.
Despite its high similarity with monomeric arginine kinase, muscle creatine kinase is only enzymatically active as a dimer
Arch. Biochem. Biophys.
458
158-166
2007
Oryctolagus cuniculus (P00563)
Manually annotated by BRENDA team
Shi, F.; Zhao, T.J.; He, H.W.; Li, J.; Zeng, X.G.; Zhou, H.M.; Wu, P.
Sodium barbital is a slow reversible inactivator of rabbit-muscle creatine kinase
Biochem. Cell Biol.
84
142-147
2006
Oryctolagus cuniculus
Manually annotated by BRENDA team
Zhang, J.W.; Guo, Q.; Zhao, T.J.; Liu, T.T.; Wang, X.C.
Two fused proteins combining Stichopus japonicus arginine kinase and rabbit muscle creatine kinase
Biochemistry (Moscow)
71
983-988
2006
Oryctolagus cuniculus
Manually annotated by BRENDA team
Zhao, T.J.; Feng, S.; Wang, Y.L.; Liu, Y.; Luo, X.C.; Zhou, H.M.; Yan, Y.B.
Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability
FEBS Lett.
580
3835-3840
2006
Oryctolagus cuniculus (P00563)
Manually annotated by BRENDA team
He, H.W.; Feng, S.; Pang, M.; Zhou, H.M.; Yan, Y.B.
Role of the linker between the N- and C-terminal domains in the stability and folding of rabbit muscle creatine kinase
Int. J. Biochem. Cell Biol.
39
1816-1827
2007
Oryctolagus cuniculus (P00563), Oryctolagus cuniculus
Manually annotated by BRENDA team
Zhao, T.J.; Yan, Y.B.; Liu, Y.; Zhou, H.M.
The generation of the oxidized form of creatine kinase is a negative regulation on muscle creatine kinase
J. Biol. Chem.
282
12022-12029
2007
Oryctolagus cuniculus
Manually annotated by BRENDA team
Zou, H.; Yu, Z.; Wang, Y.; Yang, J.; Zhou, H.; Meng, F.; Park, Y.
Monomeric creatine kinase aggregation and sodium dodecyl sulfate-cyclodextrin assisted refolding
J. Biomol. Struct. Dyn.
24
359-367
2007
Oryctolagus cuniculus
Manually annotated by BRENDA team
Bretonnet, A.S.; Jochum, A.; Walker, O.; Krimm, I.; Goekjian, P.; Marcillat, O.; Lancelin, J.M.
NMR screening applied to the fragment-based generation of inhibitors of creatine kinase exploiting a new interaction proximate to the ATP binding site
J. Med. Chem.
50
1865-1875
2007
Oryctolagus cuniculus
Manually annotated by BRENDA team
Du, F.; Zhou, Z.; Mo, Z.Y.; Shi, J.Z.; Chen, J.; Liang, Y.
Mixed macromolecular crowding accelerates the refolding of rabbit muscle creatine kinase: implications for protein folding in physiological environments
J. Mol. Biol.
364
469-482
2006
Oryctolagus cuniculus
Manually annotated by BRENDA team
Pancera, S.M.; Gliemann, H.; Schimmel, T.; Petri, D.F.
Effect of pH on the adsorption and activity of creatine phosphokinase
J. Phys. Chem. B
110
2674-2680
2006
Oryctolagus cuniculus (P00563)
Manually annotated by BRENDA team
Zurmanova, J.; Difato, F.; Malacova, D.; Mejsnar, J.; Stefl, B.; Zahradnik, I.
Creatine kinase binds more firmly to the M-band of rabbit skeletal muscle myofibrils in the presence of its substrates
Mol. Cell. Biochem.
305
55-61
2007
Oryctolagus cuniculus
Manually annotated by BRENDA team
Wennefors, C.K.; Dobrikov, M.I.; Xu, Z.; Li, P.; Shaw, B.R.
Stereospecificity, substrate, and inhibitory properties of nucleoside diphosphate analogs for creatine and pyruvate kinases
Bioorg. Chem.
36
169-177
2008
Oryctolagus cuniculus
Manually annotated by BRENDA team
Mu, H.; Lue, Z.R.; Park, D.; Kim, B.C.; Bhak, J.; Zou, F.; Yang, J.M.; Li, S.; Park, Y.D.; Zou, H.C.; Zhou, H.M.
Kinetics of Zn2+-induced brain type creatine kinase unfolding and aggregation
Appl. Biochem. Biotechnol.
160
1309-1320
2010
Oryctolagus cuniculus
Manually annotated by BRENDA team
Wang, S.; Wang, X.; Shi, W.; Wang, K.; Ma, H.
Detection of local polarity and conformational changes at the active site of rabbit muscle creatine kinase with a new arginine-specific fluorescent probe
Biochim. Biophys. Acta
1784
415-422
2008
Oryctolagus cuniculus
Manually annotated by BRENDA team
Li, P.; Zhang, S.; Fan, C.
COMMD6 from amphioxus Branchiostoma belcheri (BbCOMMD6) interacts with creatine kinase and inhibits its activity
Int. J. Biochem. Cell Biol.
41
2459-2465
2009
Oryctolagus cuniculus
Manually annotated by BRENDA team
Lue, Z.R.; Zou, H.C.; Park, S.J.; Park, D.; Shi, L.; Oh, S.H.; Park, Y.D.; Bhak, J.; Zou, F.
The effects of acrylamide on brain creatine kinase: inhibition kinetics and computational docking simulation
Int. J. Biol. Macromol.
44
128-132
2009
Oryctolagus cuniculus
Manually annotated by BRENDA team
Wu, C.L.; Li, Y.H.; Lin, H.C.; Yeh, Y.H.; Yan, H.Y.; Hsiao, C.D.; Hui, C.F.; Wu, J.L.
Activity and function of rabbit muscle-specific creatine kinase at low temperature by mutation at gly268 to asn268
Comp. Biochem. Physiol. B
158
189-198
2011
Oryctolagus cuniculus
Manually annotated by BRENDA team
Riviere, G.; Hologne, M.; Marcillat, O.; Lancelin, J.M.
Dynamical properties of the loop 320s of substrate-free and substrate-bound muscle creatine kinase by NMR: evidence for independent subunits
FEBS J.
279
2863-2875
2012
Oryctolagus cuniculus
Manually annotated by BRENDA team
Londergan, C.H.; Baskin, R.; Bischak, C.G.; Hoffman, K.W.; Snead, D.M.; Reynoso, C.
Dynamic asymmetry and the role of the conserved active-site thiol in rabbit muscle creatine kinase
Biochemistry
54
83-95
2015
Oryctolagus cuniculus (P00563), Oryctolagus cuniculus
Manually annotated by BRENDA team
Wu, C.L.; Li, B.Y.; Wu, J.L.; Hui, C.F.
The activity of carp muscle-specific creatine kinase at low temperature is enhanced by decreased hydrophobicity of residue 268
Physiol. Biochem. Zool.
87
507-516
2014
Oryctolagus cuniculus (P00563), Oryctolagus cuniculus, Cyprinus carpio (Q9YI16), Cyprinus carpio
Manually annotated by BRENDA team
Cheng, Y.; Li, R.; Lin, Z.; Chen, F.; Dai, J.; Zhu, Z.; Chen, L.; Zhao, Y.
Structure-activity relationship analysis of dammarane-type natural products as muscle-type creatine kinase activators
Bioorg. Med. Chem. Lett.
30
127364
2020
Oryctolagus cuniculus (P00563), Homo sapiens (P06732)
Manually annotated by BRENDA team