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Literature summary extracted from

  • McLeish, M.; Kenyon, G.
    Relating structure to mechanism in creatine kinase (2005), Crit. Rev. Biochem. Mol. Biol., 40, 1-20.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.7.3.2 diagnostics enzyme is clinically important as an indicator of myocardial and skeletal muscle disorders and for the diagnosis of acute myocardial infarction Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.3.2 expression of soluble monomeric or dimeric mutants Oryctolagus cuniculus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.3.2 crystal structure analysis of muscle cytosolic isozyme Bos taurus
2.7.3.2 crystal structure analysis of muscle cytosolic isozyme Oryctolagus cuniculus
2.7.3.2 crystal structure analysis of muscle-type cytosolic isozyme crystallized with transition state analogue complex Tetronarce californica
2.7.3.2 crystal structure analysis of muscle-type cytosolic isozyme, and of ubiquitous mitochondrial isozyme, and of cytosolic brain type isozyme Homo sapiens
2.7.3.2 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 Gallus gallus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.3.2 formate mimics the phosphoryl group in the transition state Bos taurus
2.7.3.2 formate mimics the phosphoryl group in the transition state Gallus gallus
2.7.3.2 formate mimics the phosphoryl group in the transition state Homo sapiens
2.7.3.2 formate mimics the phosphoryl group in the transition state Oryctolagus cuniculus
2.7.3.2 formate mimics the phosphoryl group in the transition state Tetronarce californica
2.7.3.2 guanidinium hydrochloride first dissociation of subunits, then unfolding into random coil Oryctolagus cuniculus
2.7.3.2 iodoacetamide substrates can protect against alkylation Bos taurus
2.7.3.2 iodoacetamide substrates can protect against alkylation Gallus gallus
2.7.3.2 iodoacetamide substrates can protect against alkylation Homo sapiens
2.7.3.2 iodoacetamide substrates can protect against alkylation Oryctolagus cuniculus
2.7.3.2 iodoacetamide substrates can protect against alkylation Tetronarce californica
2.7.3.2 nitrate mimics the phosphoryl group in the transition state Bos taurus
2.7.3.2 nitrate mimics the phosphoryl group in the transition state Gallus gallus
2.7.3.2 nitrate mimics the phosphoryl group in the transition state Homo sapiens
2.7.3.2 nitrate mimics the phosphoryl group in the transition state Oryctolagus cuniculus
2.7.3.2 nitrate mimics the phosphoryl group in the transition state Tetronarce californica
2.7.3.2 nitrite mimics the phosphoryl group in the transition state Bos taurus
2.7.3.2 nitrite mimics the phosphoryl group in the transition state Gallus gallus
2.7.3.2 nitrite mimics the phosphoryl group in the transition state Homo sapiens
2.7.3.2 nitrite mimics the phosphoryl group in the transition state Oryctolagus cuniculus
2.7.3.2 nitrite mimics the phosphoryl group in the transition state Tetronarce californica
2.7.3.2 Phenylglyoxal complete inactivation, reacts on arginine residues Oryctolagus cuniculus
2.7.3.2 phosphate competitive against ATP and phosphocreatine, noncompetitive against ADP and creatine Homo sapiens
2.7.3.2 SDS dissociation of subunits, no unfolding Oryctolagus cuniculus
2.7.3.2 sulfate competitive against ATP and phosphocreatine, noncompetitive against ADP and creatine Homo sapiens
2.7.3.2 transition state analogue complex consists of creatine, MgADP, and planar ions such as nitrate, nitrite, and formate, binding structure Homo sapiens
2.7.3.2 transition state analogue complex creatine, MgADP-, and planar ions such as nitrate, nitrite, and formate Tetronarce californica

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.3.2 additional information
-
 additional information kinetic mechanism, the enzyme shows negative cooperativity and nonidentical active sites Homo sapiens
2.7.3.2 additional information
-
 additional information kinetic mechanism, the enzyme shows negative cooperativity and nonidentical active sites Oryctolagus cuniculus
2.7.3.2 additional information
-
 additional information kinetics, the enzyme shows negative cooperativity and nonidentical active sites Bos taurus
2.7.3.2 additional information
-
 additional information kinetics, the enzyme shows negative cooperativity and nonidentical active sites Tetronarce californica
2.7.3.2 additional information
-
 additional information kinetics, the enzyme shows negative cooperativity and nonidentical active sites Gallus gallus
2.7.3.2 0.03
-
 ADP pH 7.0, muscle-type cytosolic isozyme Homo sapiens
2.7.3.2 0.04
-
 ADP pH 7.0, brain-type cytosolic isozyme Homo sapiens
2.7.3.2 0.11
-
 ATP pH 8.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 0.13
-
 ADP pH 7.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 0.15
-
 ADP pH 7.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 0.51
-
 phosphocreatine pH 7.0, brain-type cytosolic isozyme Homo sapiens
2.7.3.2 0.55
-
 phosphocreatine pH 7.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 0.68
-
 ATP pH 8.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 0.81
-
 ATP pH 9.0, brain-type cytosolic isozyme Homo sapiens
2.7.3.2 0.89
-
 ATP pH 9.0, muscle-type cytosolic isozyme Homo sapiens
2.7.3.2 1.01
-
 Creatine pH 8.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 1.16
-
 phosphocreatine pH 7.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 1.33
-
 phosphocreatine pH 7.0, muscle-type cytosolic isozyme Homo sapiens
2.7.3.2 4.9
-
 Creatine pH 9.0, brain-type cytosolic isozyme Homo sapiens
2.7.3.2 7.31
-
 Creatine pH 8.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 9.5
-
 Creatine pH 9.0, muscle-type cytosolic isozyme Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.3.2 cytosol
-
 Homo sapiens 5829
-
2.7.3.2 cytosol
-
 Bos taurus 5829
-
2.7.3.2 cytosol
-
 Oryctolagus cuniculus 5829
-
2.7.3.2 cytosol
-
 Tetronarce californica 5829
-
2.7.3.2 cytosol
-
 Gallus gallus 5829
-
2.7.3.2 mitochondrion
-
 Homo sapiens 5739
-
2.7.3.2 mitochondrion
-
 Bos taurus 5739
-
2.7.3.2 mitochondrion
-
 Oryctolagus cuniculus 5739
-
2.7.3.2 mitochondrion
-
 Tetronarce californica 5739
-
2.7.3.2 mitochondrion
-
 Gallus gallus 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.3.2 Mg2+
-
 Bos taurus
2.7.3.2 Mg2+
-
 Gallus gallus
2.7.3.2 Mg2+ binding structure Homo sapiens
2.7.3.2 Mg2+ binding structure Oryctolagus cuniculus
2.7.3.2 Mg2+ binding structure Tetronarce californica

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.3.2 78500 85100 cytosolic muscle isozyme Homo sapiens
2.7.3.2 78500 85100 cytosolic muscle isozyme Bos taurus
2.7.3.2 78500 85100 cytosolic muscle isozyme Gallus gallus
2.7.3.2 82600
-
 cytosolic muscle isozyme, gel filtration Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.3.2 ATP + creatine Homo sapiens key enzyme in energy homeostasis ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine Bos taurus key enzyme in energy homeostasis ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine Oryctolagus cuniculus key enzyme in energy homeostasis ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine Tetronarce californica key enzyme in energy homeostasis ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine Gallus gallus key enzyme in energy homeostasis ADP + phosphocreatine
-
 r
2.7.3.2 additional information Homo sapiens probable enzyme evolution, overview ?
-
 ?
2.7.3.2 additional information Bos taurus probable enzyme evolution, overview ?
-
 ?
2.7.3.2 additional information Oryctolagus cuniculus probable enzyme evolution, overview ?
-
 ?
2.7.3.2 additional information Tetronarce californica probable enzyme evolution, overview ?
-
 ?
2.7.3.2 additional information Gallus gallus probable enzyme evolution, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.3.2 Bos taurus
-
 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
-
2.7.3.2 Gallus gallus P11009 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
-
2.7.3.2 Homo sapiens
-
 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
-
2.7.3.2 Oryctolagus cuniculus
-
 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
-
2.7.3.2 Tetronarce californica
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.3.2 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 Oryctolagus cuniculus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.3.2 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 Gallus gallus
a
2.7.3.2 ATP + creatine = ADP + phosphocreatine catalytic cysteine, active site structure involving His66 and Asp326, overview, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview Tetronarce californica
a
2.7.3.2 ATP + creatine = ADP + phosphocreatine catalytic cysteine, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview Homo sapiens
a
2.7.3.2 ATP + creatine = ADP + phosphocreatine catalytic cysteine, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview Bos taurus
a
2.7.3.2 ATP + creatine = ADP + phosphocreatine catalytic cysteine, the enzyme follows a random or an ordered bimolecular mechanism dependent on pH, direct phosphoryl transfer, no phosphorylated intermediate, overview Oryctolagus cuniculus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.3.2 brain
-
 Gallus gallus
-
2.7.3.2 heart
-
 Gallus gallus
-
2.7.3.2 skeletal muscle
-
 Homo sapiens
-
2.7.3.2 skeletal muscle
-
 Bos taurus
-
2.7.3.2 skeletal muscle
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.3.2 additional information
-
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.3.2 ATP + creatine
-
 Bos taurus ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine
-
 Oryctolagus cuniculus ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine
-
 Tetronarce californica ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine
-
 Gallus gallus ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine key enzyme in energy homeostasis Homo sapiens ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine key enzyme in energy homeostasis Bos taurus ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine key enzyme in energy homeostasis Oryctolagus cuniculus ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine key enzyme in energy homeostasis Tetronarce californica ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine key enzyme in energy homeostasis Gallus gallus ADP + phosphocreatine
-
 r
2.7.3.2 ATP + creatine the reaction equilibrium lies towards ATP production Homo sapiens ADP + phosphocreatine
-
 r
2.7.3.2 ATP + cyclocreatine i.e. 1-carboxymethy-2-iminoimidazolidine Oryctolagus cuniculus ADP + phospho-cyclocreatine
-
 ?
2.7.3.2 ATP + cyclocreatine i.e. 1-carboxymethyl-2-iminoimidazolidine Homo sapiens ADP + phospho-cyclocreatine
-
 ?
2.7.3.2 ATP + glycocyamine very low activity Homo sapiens ADP + glycocyamine phosphate
-
 ?
2.7.3.2 ATP + glycocyamine very low activity Oryctolagus cuniculus ADP + glycocyamine phosphate
-
 ?
2.7.3.2 ATP + N-ethylglycocyamine
-
 Homo sapiens ADP + N-ethylglycocyamine phosphate
-
 ?
2.7.3.2 ATP + N-ethylglycocyamine
-
 Oryctolagus cuniculus ADP + N-ethylglycocyamine phosphate
-
 ?
2.7.3.2 additional information probable enzyme evolution, overview Homo sapiens ?
-
 ?
2.7.3.2 additional information probable enzyme evolution, overview Bos taurus ?
-
 ?
2.7.3.2 additional information probable enzyme evolution, overview Oryctolagus cuniculus ?
-
 ?
2.7.3.2 additional information probable enzyme evolution, overview Tetronarce californica ?
-
 ?
2.7.3.2 additional information probable enzyme evolution, overview Gallus gallus ?
-
 ?
2.7.3.2 additional information substrate binding structure, arginine residues R130, R132, R236, R292, and R320 form a nucleotide phosphate bindig pocket, reaction equilibrium is highly influenced by pH and Mg2+ concentration, substrate specificity of isozymes Homo sapiens ?
-
 ?
2.7.3.2 additional information substrate binding structure, reaction equilibrium is highly influenced by pH and Mg2+ concentration, assay methods, overview, structure-function analysis, substrate specificity of isozymes, the cytosolic isozymes of skeletal muscle shows broad substrate specificity Oryctolagus cuniculus ?
-
 ?
2.7.3.2 additional information substrate binding structure, reaction equilibrium is highly influenced by pH and Mg2+ concentration, substrate specificity of isozymes Bos taurus ?
-
 ?
2.7.3.2 additional information substrate binding structure, reaction equilibrium is highly influenced by pH and Mg2+ concentration, substrate specificity of isozymes Gallus gallus ?
-
 ?
2.7.3.2 additional information substrate binding structure, substrate binding at both subunits Tetronarce californica ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.3.2 ? x * 40000-44000, mature enzyme Tetronarce californica
2.7.3.2 dimer 2 * 40000-44000, mature cytosolic isozymes Homo sapiens
2.7.3.2 dimer 2 * 40000-44000, mature cytosolic isozymes Bos taurus
2.7.3.2 dimer 2 * 40000-44000, mature cytosolic isozymes Oryctolagus cuniculus
2.7.3.2 dimer 2 * 40000-44000, mature cytosolic isozymes Gallus gallus
2.7.3.2 More analysis of the structure of cardiac sarcomeric mitochondrial isozyme, free or bound to MgATP or transition state analogue complex Gallus gallus
2.7.3.2 More structure-function analysis, the monomeric enzyme is active, the subunits act independently Oryctolagus cuniculus
2.7.3.2 octamer 8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions Homo sapiens
2.7.3.2 octamer 8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions Bos taurus
2.7.3.2 octamer 8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions Oryctolagus cuniculus
2.7.3.2 octamer 8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions Gallus gallus

Synonyms

EC Number Synonyms Comment Organism
2.7.3.2 ATP-creatine transphosphorylase
-
 Homo sapiens
2.7.3.2 ATP-creatine transphosphorylase
-
 Bos taurus
2.7.3.2 ATP-creatine transphosphorylase
-
 Oryctolagus cuniculus
2.7.3.2 ATP-creatine transphosphorylase
-
 Tetronarce californica
2.7.3.2 ATP-creatine transphosphorylase
-
 Gallus gallus
2.7.3.2 CK
-
 Oryctolagus cuniculus
2.7.3.2 More the enzyme is a member of the phosphagen (guanidino) kinase family Homo sapiens
2.7.3.2 More the enzyme is a member of the phosphagen (guanidino) kinase family Bos taurus
2.7.3.2 More the enzyme is a member of the phosphagen (guanidino) kinase family Oryctolagus cuniculus
2.7.3.2 More the enzyme is a member of the phosphagen (guanidino) kinase family Tetronarce californica
2.7.3.2 More the enzyme is a member of the phosphagen (guanidino) kinase family Gallus gallus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.3.2 51.7
-
 ATP pH 8.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 51.7
-
 Creatine pH 8.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 75
-
 ATP pH 8.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 75
-
 Creatine pH 8.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 78.3
-
 ADP pH 7.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 78.3
-
 phosphocreatine pH 7.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 90
-
 ADP pH 7.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 90
-
 phosphocreatine pH 7.0, ubiquitous mitochondrial isozyme Homo sapiens
2.7.3.2 153.5
-
 ATP pH 9.0, muscle-type cytosolic isozyme Homo sapiens
2.7.3.2 153.5
-
 Creatine pH 9.0, muscle-type cytosolic isozyme Homo sapiens
2.7.3.2 215
-
 ATP pH 9.0, brain-type cytosolic isozyme Homo sapiens
2.7.3.2 215
-
 Creatine pH 9.0, brain-type cytosolic isozyme Homo sapiens
2.7.3.2 350
-
 ADP pH 7.0, brain-type cytosolic isozyme Homo sapiens
2.7.3.2 350
-
 phosphocreatine pH 7.0, brain-type cytosolic isozyme Homo sapiens
2.7.3.2 483.3
-
 ADP pH 7.0, muscle-type cytosolic isozyme Homo sapiens
2.7.3.2 483.3
-
 phosphocreatine pH 7.0, muscle-type cytosolic isozyme Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.3.2 7 9 assay at Homo sapiens
2.7.3.2 7 9 assay at Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.3.2 ADP
-
 Homo sapiens
2.7.3.2 ADP
-
 Bos taurus
2.7.3.2 ADP
-
 Oryctolagus cuniculus
2.7.3.2 ADP
-
 Gallus gallus
2.7.3.2 ADP binding structure Tetronarce californica
2.7.3.2 ATP
-
 Homo sapiens
2.7.3.2 ATP
-
 Bos taurus
2.7.3.2 ATP
-
 Oryctolagus cuniculus
2.7.3.2 ATP
-
 Gallus gallus
2.7.3.2 ATP binding structure Tetronarce californica

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.3.2 Homo sapiens 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
-
 additional information
2.7.3.2 Bos taurus 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
-
 additional information
2.7.3.2 Gallus gallus 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
-
 additional information
2.7.3.2 Oryctolagus cuniculus the mitochondrial isozymes, a ubiquitous MiU-CK and a sarcomeric MiS-CK differ in their pI and are therefore also termed the acidic and basic isozymes
-
 additional information