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Information on EC 2.7.3.2 - creatine kinase and Organism(s) Homo sapiens

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EC Tree
IUBMB Comments
N-Ethylglycocyamine can also act as acceptor.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
adenosine triphosphate-creatine transphosphorylase
-
-
-
-
ATP-creatine transphosphorylase
-
-
ATP: creatine N-phosphotransferase
-
-
ATP:creatine phosphotransferase
-
-
-
-
BB-CK
brain creatine kinase
-
-
brain-type creatine kinase
-
CK
-
-
-
-
CK-BB
CK-MB
CK-MM
CKMBI
isoform
CKMiMi
-
-
-
-
creatine kinase
-
-
creatine kinase M-type
-
creatine kinase MB
isoform
creatine kinase-MB
isozyme
creatine N-phosphotransferase
-
-
creatine phosphokinase
-
-
-
-
creatine phosphotransferase
-
-
-
-
creatinine kinase MB
isoform
hBBCK
-
-
kinase, creatine (phosphorylating)
-
-
-
-
MB-CK
-
-
-
-
Mi-CK
-
-
-
-
MiMi-CK
-
-
-
-
mitochondrial creatine kinase
-
-
MM-CK
-
-
-
-
muscle creatine kinase
muscle-type creatine kinase
phosphocreatine kinase
-
-
-
-
plasma creatine kinase
recombinant human brain-type creatine kinase
-
-
rHBCK
-
-
sMiCK
-
-
additional information
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
-
-
-
-
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
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
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
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
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
ATP + creatine
ADP + creatine phosphate
show the reaction diagram
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
required
NaCl
-
prevents aggregation of the enzyme during recombinant expression in Escherichia coli
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
Bis-Tris
-
-
Ca2+
-
-
Cu2+
-
-
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
Fe3+
-
-
formate
-
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
imidazole
-
-
iodoacetamide
jujubogenin
16.9% inhibition at 0.005 mM
-
MOPS buffer
-
i.e. 3-(N-morpholino)propane sulfonate
nitrate
-
mimics the phosphoryl group in the transition state
nitrite
-
mimics the phosphoryl group in the transition state
NO2-
-
-
phosphate
-
competitive against ATP and phosphocreatine, noncompetitive against ADP and creatine
Pipes buffer
-
i.e. 1,4-piperazine diethanesulfonic acid
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
SO32-
-
-
SO42-
-
-
sulfate
-
competitive against ATP and phosphocreatine, noncompetitive against ADP and creatine
transition state analogue complex
-
consists of creatine, MgADP, and planar ions such as nitrate, nitrite, and formate, binding structure
-
Tris
-
-
additional information
-
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)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20(R)-protopanaxadiol
23.5% increase of activity at 0.02 mM
20(S)-protopanaxadiol
best activator of isoform CK-MM, 54.3% increase of activity at 0.04 mM
20(S)-protopanaxatriol
32.2% increase of activity at 0.02 mM
24-carboxy-protopanaxadiol
17.3% increase of activity at 0.005 mM
-
25-hydroxy-protopanaxadiol
23.5% increase of activity at 0.02 mM
-
ginsenoside Rh2
3.5% increase of activity at 0.04 mM
panaxadiol
15.4% increase of activity at 0.08 mM
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.15
ADP
0.11 - 8.96
ATP
0.69 - 156.44
Creatine
1.07 - 3
creatine phosphate
0.51 - 1.33
phosphocreatine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
78.3 - 483.3
ADP
28.99 - 215
ATP
4.2 - 417
Creatine
1.5 - 35.2
cyclocreatine
0.55 - 14.5
N-ethylglycocyamine
78.3 - 483.3
phosphocreatine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.22
SDS
-
in 5 mM glycine-NaOH (pH 9.0), at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
-
synthesis of phosphocreatine
245.5
-
wild-type enzyme
246
-
wild-type
410
-
30°C
49.5
-
synthesis of ATP
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
-
synthesis of ATP
6.7
-
synthesis of MgATP2-
7 - 9
-
assay at
7.5 - 9
-
synthesis of phosphocreatine
8
-
assay at
8.7
-
synthesis of phosphocreatine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
-
isoelectric focusing, enzyme variant IV
6.4
-
isoelectric focusing, enzyme variant IV
6.55 - 6.95
-
isoelectric focusing, dimeric sarcomeric isoform
6.6
-
isoelectric focusing, dimeric ubiquitous isoform
6.7
-
isoelectric focusing, enzyme variant III
6.8
-
several bands in serum of a patient with ovarian hepatoid yolk sac tumor, atypical ubiquitous mitochondrial enzyme, isoelectric focusing
7
-
ubiquitous mitochondrial enzyme, 2 bands at pH 6.9 and pH 7.0 in isoelectric focusing
7 - 7.8
-
several bands in serum of a patient with ovarian hepatoid yolk sac tumor, atypical ubiquitous mitochondrial enzyme, isoelectric focusing
7.2
-
isoelectric focusing, enzyme variant I
7.44
-
isoelectric focusing, dimeric form
7.5
-
isoelectric focusing, dimeric form
7.7
-
isoelectric focusing, octameric form
8.3
-
isoelectric focusing, octameric form
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the inter-individual variation in creatine kinase activity in the general population is wide, ranging from below 25 to up to 5000 IU/L5, with particularly high levels in men and in persons of African ancestry
Manually annotated by BRENDA team
-
CKB mRNA and protein levels are significantly higher in probands affected with autosomal dominant inherited anomaly CKBE
Manually annotated by BRENDA team
-
CKB mRNA and protein levels are significantly higher in probands affected with autosomal dominant inherited anomaly CKBE
Manually annotated by BRENDA team
-
patient with ovarian hepatoid yolk sac tumor, an atypical ubiquitous mitochondrial enzyme form
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
downregulation of brain-type creatine kinase in brains of Huntington's disease patients. Huntington's disease is a hereditary neurodegenerative disorder caused by a CAG repeat expansion in the huntingtin (HTT) gene
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KCRB_HUMAN
381
0
42644
Swiss-Prot
other Location (Reliability: 2)
KCRM_HUMAN
381
0
43101
Swiss-Prot
other Location (Reliability: 2)
KCRS_HUMAN
419
0
47504
Swiss-Prot
Mitochondrion (Reliability: 3)
KCRU_HUMAN
417
0
47037
Swiss-Prot
Mitochondrion (Reliability: 2)
B4DH34_HUMAN
264
0
30031
TrEMBL
other Location (Reliability: 2)
C9J6W7_HUMAN
203
0
22477
TrEMBL
Mitochondrion (Reliability: 2)
B4DP56_HUMAN
346
0
38694
TrEMBL
other Location (Reliability: 2)
B4DFE8_HUMAN
254
0
28335
TrEMBL
Mitochondrion (Reliability: 2)
B3KVA7_HUMAN
356
0
40479
TrEMBL
other Location (Reliability: 1)
H0YJG0_HUMAN
179
0
20147
TrEMBL
other Location (Reliability: 3)
B7Z9T7_HUMAN
146
0
16687
TrEMBL
Mitochondrion (Reliability: 2)
B4DUP1_HUMAN
267
0
29941
TrEMBL
Mitochondrion (Reliability: 2)
C9JSQ1_HUMAN
241
0
26721
TrEMBL
Mitochondrion (Reliability: 2)
A0A024RAK5_HUMAN
419
0
47504
TrEMBL
Mitochondrion (Reliability: 3)
B2R892_HUMAN
381
0
43029
TrEMBL
other Location (Reliability: 2)
F8WCN3_HUMAN
298
0
33518
TrEMBL
Mitochondrion (Reliability: 2)
V9HW77_HUMAN
381
0
42675
TrEMBL
other Location (Reliability: 2)
H0YJK0_HUMAN
90
0
9818
TrEMBL
other Location (Reliability: 2)
B4DF55_HUMAN
338
0
37856
TrEMBL
Mitochondrion (Reliability: 3)
E9PCP8_HUMAN
257
0
29194
TrEMBL
other Location (Reliability: 2)
B2R8A3_HUMAN
419
0
47533
TrEMBL
Mitochondrion (Reliability: 3)
V9HWH2_HUMAN
381
0
42644
TrEMBL
other Location (Reliability: 2)
B4DNF8_HUMAN
126
0
14124
TrEMBL
other Location (Reliability: 1)
C9JT96_HUMAN
221
0
24541
TrEMBL
Mitochondrion (Reliability: 2)
G3V4N7_HUMAN
217
0
24116
TrEMBL
other Location (Reliability: 2)
A0A0S2Z471_HUMAN
405
0
44922
TrEMBL
other Location (Reliability: 2)
B4DF72_HUMAN
168
0
19288
TrEMBL
other Location (Reliability: 2)
G3V461_HUMAN
128
0
14221
TrEMBL
other Location (Reliability: 1)
B4DJW9_HUMAN
146
0
16719
TrEMBL
Mitochondrion (Reliability: 2)
B4DGR9_HUMAN
243
0
27643
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
346000
-
gel filtration, also 86000
371000
-
and also 79700, gel filtration
41000
-
2 * 41000, SDS-PAGE
42000
-
2 * 42000, SDS-PAGE
43000
43600
78500 - 85100
-
cytosolic muscle isozyme
79700
-
and also 371000, gel filtration
80000
gel filtration
84000 - 85000
-
isozyme MiMi-CK, sedimentation equilibrium centrifugation, gel filtration
85300
-
wild-type hMMCK
86000
86200
-
wild-type hMMCK
additional information
-
overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
heterodimer
homodimer
-
-
octamer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of muscle-type cytosolic isozyme, and of ubiquitous mitochondrial isozyme, and of cytosolic brain type isozyme
-
crystallized at 22°C using PEG 4000 as a precipitant. X-ray diffraction data are collected to 2.2 A resolution using synchrotron radiation. The crystals belong to the tetragonal space group P4(3)2(1)2, with cell parameters of a = b = 97.963, c = 164.312 A, and alpha = beta = gamma = 90°. The symmetric unit contains two molecules of creatine kinase
-
isozyme MiMi-CK
-
muscle isoform
-
overview: electron microscopy, X-ray crystallography
-
ubiquituos mitochondrial isoform
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A267H
-
Km and kcat values similar to wild-type, T0.5 (°C): 56.9 (wild-type: 56.9°C)
A329S
-
Km and kcat values similar to wild-type, T0.5 (°C): 56.6 (wild-type: 56.9°C)
C146N
-
Km and kcat values similar to wild-type, T0.5 (°C): 52.4 (wild-type: 56.9°C)
C283S/S285C
pKa value of active site cysteine increase by 1 pH unit
D189A
-
Km values 2-3fold decreased compared to wild-type, kcat 30% decreased compared to wild-type, T0.5 (°C): 57 (wild-type: 56.9°C)
D326A
D326E
DeltaH65
-
affinity to substrates almost like wild type enzyme, very little stability
DeltaH65P66
-
8-fold decreased affinity for creatine phosphate
E226Q
-
catalytic site mutants which show no detectable creatine kinase activity demonstrate that enzymatic activity is not required for the regulation of NCX1 activity
E227L
-
catalytic site mutants which show no detectable creatine kinase activity demonstrate that enzymatic activity is not required for the regulation of NCX1 activity
E231Q
-
catalytic site mutants which show no detectable creatine kinase activity demonstrate that enzymatic activity is not required for the regulation of NCX1 activity
E232L
-
catalytic site mutants which show no detectable creatine kinase activity demonstrate that enzymatic activity is not required for the regulation of NCX1 activity
E46Q
-
Km values 2-3fold decreased compared to wild-type, kcat 30% decreased compared to wild-type, T0.5 (°C): 50.1 (wild-type: 56.9°C)
H66P/D326A
I69A
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
I69L
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
I69V
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K304T
-
Km and kcat values similar to wild-type, T0.5 (°C): 57.1 (wild-type: 56.9°C)
L36K
-
Km and kcat values similar to wild-type, T0.5 (°C): 47.3 (wild-type: 56.9°C)
P284A
pKa value of active site cysteine increase by 1.2 pH units
Q185E
-
Km values 2-3fold decreased compared to wild-type, kcat 30% decreased compared to wild-type, T0.5 (°C): 56.4 (wild-type: 56.9°C)
S123A
-
mutation analysis show that a putative PKC phosphorylation site on sMiCK and CKM is required for the regulation of NCX1 activity: S123A mutant fails to produce a recovery in the decreased NCX1 activity under energy-compromised conditions
S128A
-
mutation analysis show that a putative PKC phosphorylation site on sMiCK and CKM is required for the regulation of NCX1 activity: S123A mutant fails to produce a recovery in the decreased NCX1 activity under energy-compromised conditions
S205A
-
Km and kcat values similar to wild-type, T0.5 (°C): 58.1 (wild-type: 56.9°C)
S285A
pKa value of active site cysteine increase by 1 pH unit
T277V
-
autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity
T282V
-
autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity
T284V
-
autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity
T289V
-
autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity
T322V
-
autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity
T327V
-
autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity
V325A
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme, mutant shows a slight preference for cyclocreatine, i.e. 1-carboxymethy-2-iminoimidazolidine, as substrate
V325E
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme, mutant shows a more than 100fold higher preference for N-ethylglycocyamine as substrate compared to creatine, highly reduced activity with other substrates compared to the wild-type enzyme
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 10.5
-
rapid inactivation above and below
642385
additional information
-
comparison of various enzymes of various sources
642407
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 60
the wild type enzyme remains stable after 10 min at 25-45°C. The activity drops to about 70% and after 10 min at 50°C. The enzyme is almost completely inactive after 10 min at 60°C
25 - 65
the activity of the wild type enzyme has few changes after heat treatment for 10 min at temperatures below 48°C. A steep decrease of activity is observed between 48°C and 60°C
36
-
mutant D54G, melting temperature
37
-
midpoint temperature of thermal inactivation of mutant enzyme D54G is 36.5°C
42.2
-
T0.5: 42.2°C wild-type hBBCK
53
-
midpoint temperature of thermal inactivation of wild-type enzyme is 52.5°C
56.9
-
muscle-type creatine kinase of Danio rerio is less stable compared to human muscle-type creatine kinase, T0.5: 56.9°C
57.2
-
T0.5: 57.2°C wild-type hMMCK
62
-
wild-type hMMCK gets completely inactivated above 62°C
additional information
-
comparison of various enzymes of various sources
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
a His6-tag portion has no effect on the enzyme activity
polyethylene glycol 2000 (PEG 2000) and dextran 70 are used as model crowding agents to examine the effects of macromolecular crowding on the inactivation of recombinant HBCK (rHBCK) during denaturation by GdnHCl. Both PEG 2000 and dextran 70 have a protective effect on the inactivation of rHBCK induced by GdnHCl at 25°C. The presence of PEG 2000 results in the retention of 35.33% of rHBCK activity after 4 h of inactivation, while no rHBCK activity is observed after denaturation in the absence of macromolecular crowding agents. The presence of PEG 2000 and dextran 70 at a concentration of 100 g/l can decelerate the k2 value of the slow track to 21 and 33%, respectively, in comparison to values obtained in the absence of crowding agents
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, TAP-purified recombinant isoform CK-MB in 50% (v/v) glycerol, 64 weeks, no loss of activity
-80°C, all the samples with 500, 250, and 20 U/l enzyme activity or with 300, 100, and 20 ng/ml mass concentration in 50% (v/v) glycerol, 64 weeks, no loss of activity
4°C, pH 7.0, 1 mM dithiothreitol or 14 mM 2-mercaptoethanol, at least 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
5 varieties of isozyme MM-CK
-
affinity chromatography
Ni-NTA column chromatography
Ni-NTA column chromatography and His GraviTrap column chromatography
Ni-NTA column chromatography, and Superdex 200 gel filtration
Ni-NTA resin affinity column chromatography, His GraviTrap column chromatography, and streptavidin magnetic resin chromatography
overview
-
preparation of catalytically active hybrids of brain and muscle enzymes
-
recombinant Fc-III-tagged enzyme from Escherichia coli strain BL21 (DE3)-plysS by IgG-Fc immunoaffinity chromatography, recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3)-plysS by nickel affinity chromatography
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
typical ubiquitous mitochondrial enzyme from heart muscle tissue, atypical ubiquitous mitochondrial from serum
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
both subunits are co-expressed in Escherichia coli BL21(DE3) cells
brain isoform
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli, mostly in insoluble form, after optimization of the conditions the enzyme does not aggregate and shows multi-kinetic phases
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
overexpressed as a soluble form in Escherichia coli
-
recombinant expression of Fc-III-tagged enzyme and of His-tagged enzyme in Escherichia coli strain BL21 (DE3)-plysS, respectively, the Fc-III-tagged GFP-fusion muscle creatine kinase is used as a model system to investigate effects of the Fc-III tag on activities and stabilities of recombinantly expressed multicysteine-containing proteins
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CKB mRNA and protein levels are significantly higher in probands affected with autosomal dominant inherited anomaly CKBE
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
insoluble recombinant enzyme from Escherichia coli by 6 M urea, unfolding shows biphasic kinetic courses, aggregation during refolding follows first-order kinetics, refolding intermediates are stabilized by NaCl, refolded enzyme shows high specific activity
-
reactivators are thiols, like N-acetylcysteine, beta-mercaptoethanol, dithiothreitol, monothioglycerol, glutathione
-
refolded in 50 mM Tris-HCl at pH 8.3 containing 500 mM NaCl and 5 mM dithiothreitol
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
enzyme is clinically important as an indicator of myocardial and skeletal muscle disorders and for the diagnosis of acute myocardial infarction
medicine
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
Vaidya, H.; Dietzler, D.N.; Leykam, J.F.; Ladenson, J.H.
Purification of five creatine kinase-MM variants from human heart and skeletal muscle
Biochim. Biophys. Acta
790
230-237
1984
Homo sapiens
Manually annotated by BRENDA team
Grace, A.M.; Perryman, M.B.; Roberts, R.
Purification and characterization of human mitochondrial creatine kinase. A single enzyme form
J. Biol. Chem.
258
15346-15354
1983
Homo sapiens
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
Gerhardt, W.
Creatine kinase
Methods Enzym. Anal. ,3rd Ed. (Bergmeyer,H. U. ,ed. )
3
508-510
1983
Homo sapiens
-
Manually annotated by BRENDA team
Roberts, R.
Purification of human and canine creatine kinase isozymes
Methods Enzymol.
90
185-195
1982
Canis lupus familiaris, Homo sapiens
-
Manually annotated by BRENDA team
Witteveen, S.A.G.J.; Sobel, B.E.; DeLuca, M.
Kinetic properties of the isoenzymes of human creatine phosphokinase
Proc. Natl. Acad. Sci. USA
71
1384-1387
1974
Homo sapiens
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
Schneider, C.; Stull, G.A.; Apple, F.S.
Kinetic characterization of human heart and skeletal muscle CK isoenzymes
Enzyme
39
220-226
1988
Homo sapiens
Manually annotated by BRENDA team
Walterscheid-Muller, U.; Braun, S.; Salvenmoser, W.; Meffert, G.; Dapunt, O.; Gnaiger, E.; Zierz, S.; Margreiter, R.; Wyss, M.
Purification and characterization of human sarcomeric mitochondrial creatine kinase
J. Mol. Cell. Cardiol.
29
921-927
1997
Homo sapiens
Manually annotated by BRENDA team
Schlattner, U.; Eder, M.; Dolder, M.; Khuchua, Z.A.; Strauss, A.W.; Wallimann, T.
Divergent enzyme kinetics and structural properties of the two human mitochondrial creatine kinase isoenzymes
Biol. Chem.
381
1063-1070
2000
Homo sapiens
Manually annotated by BRENDA team
Kanemitsu, F.; Mizushima, J.; Kageoka, T.; Okigaki, T.; Taketa, K.; Kira, S.
Characterization of two types of mitochondrial creatine kinase isolated from normal human cardiac muscle and brain tissue
Electrophoresis
21
266-270
2000
Homo sapiens
Manually annotated by BRENDA team
Mourad-Terzian, T.; Steghens, J.P.; Min, K.L.; Collombel, C.; Bozon, D.
Creatine kinase isoenzymes specificities: histidine 65 in human CK-BB, a role in protein stability, not in catalysis
FEBS Lett.
475
22-26
2000
Homo sapiens
Manually annotated by BRENDA team
Eder, M.; Fritz-Wolf, K.; Kabsch, W.; Wallimann, T.; Schlattner, U.
Crystal structure of human ubiquitous mitochondrial creatine kinase
Proteins
39
216-225
2000
Homo sapiens
Manually annotated by BRENDA team
Tang, L.; Zhou, H.M.; Lin, Z.J.
Crystallization and preliminary X-ray analysis of human muscle creatine kinase
Acta Crystallogr. Sect. D
55
669-670
1999
Homo sapiens
Manually annotated by BRENDA team
Novak, W.R.P.; Wang, P.F.; McLeish, M.J.; Kenyon, G.L.; Babbitt, P.C.
Isoleucine 69 and valine 325 form a specificity pocket in human muscle creatine kinase
Biochemistry
43
13766-13774
2004
Homo sapiens (P12277), Homo sapiens
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
Kanemitsu, F.; Kageoka, T.; Kira, S.
Mitochondrial creatine kinase with atypical pI values detected in serum of a patient with ovarian hepatoid yolk sac tumor
J. Chromatogr. B
783
191-197
2003
Homo sapiens
Manually annotated by BRENDA team
Hahn, H.S.; Park, Y.D.; Lee, J.R.; Park, K.H.; Kim, T.J.; Yang, J.M.; Hahn, M.J.
Aggregation and folding of recombinant human creatine kinase
J. Protein Chem.
22
563-570
2003
Homo sapiens
Manually annotated by BRENDA team
Wang, P.F.; Flynn, A.J.; Naor, M.M.; Jensen, J.H.; Cui, G.; Merz, K.M.; Kenyon, G.L.; McLeish, M.J.
Exploring the role of the active site cysteine in human muscle creatine kinase
Biochemistry
45
11464-11472
2006
Homo sapiens (P12532), Homo sapiens
Manually annotated by BRENDA team
Eliuk, S.M.; Renfrow, M.B.; Shonsey, E.M.; Barnes, S.; Kim, H.
Active site modifications of the brain isoform of creatine kinase by 4-hydroxy-2-nonenal correlate with reduced enzyme activity: mapping of modified sites by Fourier transform-ion cyclotron resonance mass spectrometry
Chem. Res. Toxicol.
20
1260-1268
2007
Homo sapiens
Manually annotated by BRENDA team
Feng, S.; Zhao, T.J.; Zhou, H.M.; Yan, Y.B.
Effects of the single point genetic mutation D54G on muscle creatine kinase activity, structure and stability
Int. J. Biochem. Cell Biol.
39
392-401
2007
Homo sapiens
Manually annotated by BRENDA team
Wang, P.F.; Kenyon, G.L.; McLeish, M.J.
Heterogeneity of Escherichia coli-expressed human muscle creatine kinase
IUBMB Life
58
421-428
2006
Homo sapiens
Manually annotated by BRENDA team
Barschak, A.G.; Ferreira, G.D.; Andre, K.R.; Schuck, P.F.; Viegas, C.M.; Tonin, A.; Filho, C.S.; Wyse, A.T.; Wannmacher, C.M.; Vargas, C.R.; Wajner, M.
Inhibition of the electron transport chain and creatine kinase activity by ethylmalonic acid in human skeletal muscle
Metab. Brain Dis.
21
11-19
2006
Homo sapiens
Manually annotated by BRENDA team
Buerklen, T.S.; Hirschy, A.; Wallimann, T.
Brain-type creatine kinase BB-CK interacts with the Golgi matrix protein GM130 in early prophase
Mol. Cell. Biochem.
297
53-64
2007
Homo sapiens
Manually annotated by BRENDA team
Lenz, H.; Schmidt, M.; Welge, V.; Kueper, T.; Schlattner, U.; Wallimann, T.; Elsaesser, H.P.; Wittern, K.P.; Wenck, H.; Staeb, F.; Blatt, T.
Inhibition of cytosolic and mitochondrial creatine kinase by siRNA in HaCaT- and HeLaS3-cells affects cell viability and mitochondrial morphology
Mol. Cell. Biochem.
306
153-162
2007
Homo sapiens, Homo sapiens (P06732), Homo sapiens (P12277)
Manually annotated by BRENDA team
Gruberg, L.; Sudarsky, D.; Kerner, A.; Hammerman, H.; Kapeliovich, M.; Beyar, R.
Troponin-positive, CK-MB-negative acute myocardial infarction: clinical, electrocardiographic and angiographic characteristics
J. Invasive Cardiol.
20
125-128
2008
Homo sapiens
Manually annotated by BRENDA team
Bong, S.M.; Moon, J.H.; Jang, E.H.; Lee, K.S.; Chi, Y.M.
Overexpression, purification, and preliminary X-ray crystallographic analysis of human brain-type creatine kinase
J. Microbiol. Biotechnol.
18
295-298
2008
Homo sapiens
Manually annotated by BRENDA team
Illa, I.; De Luna, N.; Dominguez-Perles, R.; Rojas-Garcia, R.; Paradas, C.; Palmer, J.; Marquez, C.; Gallano, P.; Gallardo, E.
Symptomatic dysferlin gene mutation carriers: characterization of two cases
Neurology
68
1284-1289
2007
Homo sapiens
Manually annotated by BRENDA team
Vissing, K.; Overgaard, K.; Nedergaard, A.; Fredsted, A.; Schjerling, P.
Effects of concentric and repeated eccentric exercise on muscle damage and calpain-calpastatin gene expression in human skeletal muscle
Eur. J. Appl. Physiol.
103
323-332
2008
Homo sapiens
Manually annotated by BRENDA team
Lue, Z.R.; Oh, S.H.; Zhou, S.S.; Zou, H.C.; Park, D.; Park, S.J.; Zhou, H.W.; Bhak, J.; Park, Y.D.; Zou, F.
Structural analysis and inhibitory Kinetics of brain type creatine kinase by sodium dodecyl sulfate
Appl. Biochem. Biotechnol.
160
831-842
2010
Homo sapiens
Manually annotated by BRENDA team
Fan, Y.Q.; Liu, H.J.; Li, C.; Luan, Y.S.; Yang, J.M.; Wang, Y.L.
Inactivation of recombinant human brain-type creatine kinase during denaturation by guanidine hydrochloride in a macromolecular crowding system
Appl. Biochem. Biotechnol.
169
268-280
2013
Homo sapiens
Manually annotated by BRENDA team
Arnold, H.; Wienker, T.; Hoffmann, M.; Scheuerbrandt, G.; Kemp, K.; Bugert, P.
High levels of brain-type creatine kinase activity in human platelets and leukocytes: A genetic anomaly with autosomal dominant inheritance
Blood Cells Mol. Dis.
48
62-67
2012
Homo sapiens
Manually annotated by BRENDA team
Gao, Y.S.; Zhao, T.J.; Chen, Z.; Li, C.; Wang, Y.; Yan, Y.B.; Zhou, H.M.
Isoenzyme-specific thermostability of human cytosolic creatine kinase
Int. J. Biol. Macromol.
47
27-32
2010
Homo sapiens
Manually annotated by BRENDA team
Gao, Y.S.; Wang, Y.; Li, C.; Chen, Z.; Yan, Y.B.; Zhou, H.M.
Dissecting the key residues crucial for the species-specific thermostability of muscle-type creatine kinase
Int. J. Biol. Macromol.
47
366-370
2010
Homo sapiens, Danio rerio (Q90X19), Danio rerio
Manually annotated by BRENDA team
Yang, Y.C.; Fann, M.J.; Chang, W.H.; Tai, L.H.; Jiang, J.H.; Kao, L.S.
Regulation of sodium-calcium exchanger activity by creatine kinase under energy-compromised conditions
J. Biol. Chem.
285
28275-28285
2010
Homo sapiens
Manually annotated by BRENDA team
Lin, Y.S.; Cheng, T.H.; Chang, C.P.; Chen, H.M.; Chern, Y.
Enhancement of brain-type creatine kinase activity ameliorates neuronal deficits in Huntingtons disease
Biochim. Biophys. Acta
1832
742-753
2013
Homo sapiens (P12277), Homo sapiens, Mus musculus (Q04447), Mus musculus, Mus musculus R6/2 (Q04447)
Manually annotated by BRENDA team
Feng, S.; Gong, Y.; Adilijiang, G.; Deng, H.
Effects of the Fc-III tag on activity and stability of green fluorescent protein and human muscle creatine kinase
Protein Sci.
22
1008-1015
2013
Homo sapiens (P06732), Homo sapiens
Manually annotated by BRENDA team
Horjus, D.L.; Nieuwland, R.; Boateng, K.B.; Schaap, M.C.; van Montfrans, G.A.; Clark, J.F.; Sturk, A.; Brewster, L.M.
Creatine kinase inhibits ADP-induced platelet aggregation
Sci. Rep.
4
6551
2014
Homo sapiens (P06732), Homo sapiens
Manually annotated by BRENDA team
Banihani, S.A.; Khasawneh, F.H.
Effect of lansoprazole on DNA integrity of human spermatozoa and activity of seminal creatine kinase
Andrologia
52
e13564
2020
Homo sapiens
Manually annotated by BRENDA team
Zou, L.; Su, W.; Wang, M.; Huang, W.; Zhao, H.; Zhang, E.; Jin, J.; Xu, H.; Xiao, F.
Characterization of a functional recombinant human creatine kinase-MB isoenzyme prepared by tandem affinity purification from Escherichia coli
Appl. Microbiol. Biotechnol.
101
5639-5644
2017
Homo sapiens (B2R892), Homo sapiens (P06732 and P12277), Homo sapiens
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
Wu, Q.Y.; Wei, F.; Zhu, Y.Y.; Tong, Y.X.; Cao, J.; Zhou, P.; Li, Z.Y.; Zeng, L.Y.; Li, F.; Wang, X.Y.; Xu, K.L.
Roles of amino acid residues H66 and D326 in the creatine kinase activity and structural stability
Int. J. Biol. Macromol.
107
512-520
2018
Homo sapiens (P06732)
Manually annotated by BRENDA team
Selimoglu, S.M.; Kasap, M.; Akpinar, G.; Karadenizli, A.; Wis, A.M.; Gormus, U.
Improved production of highly active and pure human creatine kinase MB
J. Mol. Microbiol. Biotechnol.
28
28-36
2018
Homo sapiens (P06732 and P12277), Homo sapiens
Manually annotated by BRENDA team
Clarke, W.T.; Peterzan, M.A.; Rayner, J.J.; Sayeed, R.A.; Petrou, M.; Krasopoulos, G.; Lake, H.A.; Raman, B.; Watson, W.D.; Cox, P.; Hundertmark, M.J.; Apps, A.P.; Lygate, C.A.; Neubauer, S.; Rider, O.J.; Rodgers, C.T.
Localized rest and stress human cardiac creatine kinase reaction kinetics at 3T
NMR Biomed.
32
e4085
2019
Homo sapiens
Manually annotated by BRENDA team