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Information on EC 2.7.3.2 - creatine kinase and Organism(s) Gallus gallus and UniProt Accession P11009
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2.7.3.2 creatine kinaseIUBMB Comments
N-Ethylglycocyamine can also act as acceptor.
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Word Map
- 2.7.3.2
- myocardial
- cardiac
- infarct
- coronary
- artery
- ventricular
- troponin
- ischemia
- muscular
-
reperfusion
- pain
- myopathy
- aminotransferase
- necrosis
- myoglobin
- rhabdomyolysis
-
admission
-
admitted
- dystrophy
- chest
-
cytokeratins
-
postoperative
-
cardioprotective
-
alt
-
hemodynamic
-
ejection
-
fatigue
-
percutaneous
-
c-reactive
- angina
- soreness
-
thrombolysis
-
angioplasty
-
electrocardiograph
- myalgia
-
st-segment
- arrhythmia
-
exercise-induced
-
echocardiography
-
cardiopulmonary
-
eccentric
-
langendorff
-
athlete
-
duchenne
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electromyography
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angiographic
-
perioperative
-
in-hospital
-
revascularization
- diagnostics
- biotechnology
-
reperfused
- medicine
The taxonomic range for the selected organisms is: Gallus gallus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine triphosphate-creatine transphosphorylase
-
-
-
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ATP:creatine phosphotransferase
-
-
-
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BB-CK
-
-
-
-
CK
-
-
-
-
CK-BB
-
-
-
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CK-MB
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-
-
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CK-MM
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-
-
-
CKMiMi
-
-
-
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creatine phosphokinase
-
-
-
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creatine phosphotransferase
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-
-
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kinase, creatine (phosphorylating)
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-
-
-
MB-CK
-
-
-
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Mi-CK
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-
-
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MiMi-CK
-
-
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MM-CK
-
-
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phosphocreatine kinase
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-
-
-
additional information
the enzyme is a member of the phosphagen (guanidino) kinase family
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + creatine = ADP + phosphocreatine
catalytic cysteine, active site residues are Glu226, Glu227, and Asp228, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview
ATP + creatine = ADP + phosphocreatine
mitochondrial enzymes, mechanism, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:creatine N-phosphotransferase
N-Ethylglycocyamine can also act as acceptor.
CAS REGISTRY NUMBER
COMMENTARY
9001-15-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + creatine
ADP + phosphocreatine
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + creatine phosphate
-
-
-
-
?
ATP + creatine
ADP + phosphocreatine
-
mitochondrial model of CK in energy transport
-
-
r
ATP + creatine
ADP + phosphocreatine
-
physiological roles: 1. buffering of ADP/ATP ratio, 2. transport of high-energy phosphates from sites of ATP production to sites of ATP consumption
-
-
r
additional information
?
-
substrate binding structure, reaction equilibrium is highly influenced by pH and Mg2+ concentration, substrate specificity of isozymes
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + creatine
ADP + phosphocreatine
key enzyme in energy homeostasis
-
-
r
ATP + creatine
ADP + phosphocreatine
-
mitochondrial model of CK in energy transport
-
-
r
ATP + creatine
ADP + phosphocreatine
-
physiological roles: 1. buffering of ADP/ATP ratio, 2. transport of high-energy phosphates from sites of ATP production to sites of ATP consumption
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics, the enzyme shows negative cooperativity and nonidentical active sites
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK differ in their pI and ar therefore also termed the acidic and basic isozymes
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
4 isozymes encoded by 4 different genes: 2 cytosolic isozymes, a muscle-type MM-CK and a brain-type BB-CK or a heterodimer MB-CK, and 2 mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK
Uniprot
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
creatine kinase activity is much greater females than in males. Plasma creatine kinase activity may reflect the protein turnover, which is closely related to muscle growth rate
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after beta-actin, cytosolic brain isoform of creatin kinase is the most abundant protein in hair bundle and capable of maintaining high aTP levels despite 1 mM/s ATP consumption by the plasma-membrane Ca2+-ATPase
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
accumulated in contact sites between inner and outer mitochondrial membrane
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KCRS_CHICK
419
0
47084
Swiss-Prot
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
306000 - 352000
-
isozyme Mia-CK, octameric form, gel permeation chromatography, scanning transmission electron microscopy
328000 - 340000
-
isoenzyme Mi-CK, octameric form, sedimentation velocity analysis, sedimentation equilibrium centrifugation, scanning transmission electron microscopy
42000
85000
-
isozyme Mia-CK, dimeric form, gel permeation chromatography, analytical ultracentrifugation
89000
-
isozyme Mia-CK, dimeric form, scanning transmission electron microscopy
42000
-
8 * 42000, SDS-PAGE, octameric structure dissociates during storage at -20°C, pH above 8.5, protein concentration below 0.3 mg/ml to dimeric form
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
dimer
octamer
additional information
octamer
-
8 * 42000, SDS-PAGE, octameric structure dissociates during storage at -20°C, pH above 8.5, protein concentration below 0.3 mg/ml to dimeric form
additional information
analysis of the structure of cardiac sarcomeric mitochondrial isozyme, free or bound to MgATP or transition state analogue complex
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of the cytosolic brain isozyme, and of the cardiac sarcomeric mitochondrial crystallized free or bound to MgATP or transition state analogue complex
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W264C
-
absoluteley conserved residue involved in octamer stability in most organisms, mutant forms dimers instead of octamers
W264Y
-
absoluteley conserved residue involved in octamer stability in most organisms, mutant forms dimers instead of octamers
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM MOPS buffer, pH 7.2, 2% v/v glycerol, 25 mM 2-mercaptoethanol, 0.1 mM EDTA, stable for more than 4 months
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4°C, octameric enzyme, protein concentration above 1 mg/ml, 1 mM 2-mercaptoethanol, 0.2 mM EDTA, 0.26 M NaCl, 25 mM sodium phosphate buffer, pH 7.0
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liquid N2 preserves octameric stucture, dissociation to dimer at higher temperatures
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Schnyder, T.; Winkler, H.; Gross, H.; Eppenberger, H.M.; Wallimann, T.
Crystallization of mitochondrial creatine kinase. Growing of large protein crystals and electron microscopic investigation of microcrystals consisting of octamers
J. Biol. Chem.
266
5318-5322
1991
Gallus gallus
Schnyder, T.; Sargent, D.F.; Richmond, T.J.; Eppenberger, H.M.; Wallimann, T.
Crystallization and preliminary X-ray analysis of two different forms of mitochondrial creatine kinase from chicken cardiac muscle
J. Mol. Biol.
216
809-812
1990
Gallus gallus
Wyss, M.; Schlegel, J.; James, P.; Eppenberger, H.M.; Wallimann, T.
Mitochondrial creatine kinase from chicken brain. Purification, biophysical characterization, and generation of heterodimeric and heterooctameric molecules with subunits of other creatine kinase isoenzymes
J. Biol. Chem.
265
15900-15908
1990
Gallus gallus
Schlegel, J.; Zurbriggen, B.; Wegmann, G.; Wyss, M.; Eppenberger, H.M.; Wallimann, T.
Native mitochondrial creatine kinase forms octameric structures. I. Isolation of two interconvertible mitochondrial creatine kinase forms, dimeric and octameric mitochondrial creatine kinase: characterization, localization, and structure-function relationships
J. Biol. Chem.
263
16942-16953
1988
Gallus gallus
Schnyder, T.; Engel, A.; Lustig, A.; Wallimann, T.
Native mitochondrial creatine kinase forms octameric structures. II. Characterization of dimers and octamers by ultracentrifugation, direct mass measurements by scanning transmission electron microscopy, and image analysis of single mitochondrial creatine kinase octamers
J. Biol. Chem.
263
16954-16962
1988
Gallus gallus
Brooks, S.P.; Bennett, V.D.; Suelter, C.H.
Homogeneous chicken heart mitochondrial creatine kinase purified by dye-ligand and transition-state analog-affinity chromatography
Anal. Biochem.
164
190-198
1987
Gallus gallus
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
Hossle, J.P.; Schlegel, J.; Wegmann, G.; Wyss, M.; Bohlen, P.; Eppenberger, H.M.; Wallimann, T.;Perriard, J.C.
Distinct tissue specific mitochondrial creatine kinases from chicken brain and striated muscle with a conserved CK framework
Biochem. Biophys. Res. Commun.
151
408-416
1988
Gallus gallus
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
Eder, M.; Schlattner, U.; Becker, A.; Wallimann, T.; Kabsch, W.; Fritz-Wolf, K.
Crystal structure of brain-type creatine kinase at 1.41 A resolution
Protein Sci.
8
2258-2269
1999
Gallus gallus
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)
Hoffman, G.G.; Sona, S.; Bertin, M.; Ellington, W.R.
The role of an absolutely conserved tryptophan residue in octamer formation and stability in mitochondrial creatine kinases
Biochim. Biophys. Acta
1764
1512-1517
2006
Chaetopterus variopedatus, Gallus gallus, Tethya aurantium
Shin, J.B.; Streijger, F.; Beynon, A.; Peters, T.; Gadzala, L.; McMillen, D.; Bystrom, C.; Van der Zee, C.E.; Wallimann, T.; Gillespie, P.G.
Hair bundles are specialized for ATP delivery via creatine kinase
Neuron
53
371-386
2007
Gallus gallus, Mus musculus
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