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2.7.3.2: creatine kinase

This is an abbreviated version!
For detailed information about creatine kinase, go to the full flat file.

Word Map on EC 2.7.3.2

Reaction

ATP
+
Creatine
=
ADP
 +
phosphocreatine

Synonyms

adenosine triphosphate-creatine transphosphorylase, adenosine-5'-triphosphate: creatine phosphotransferase, ATP-creatine transphosphorylase, ATP: creatine N-phosphotransferase, ATP:creatine phosphotransferase, B-type creatine kinase, BB-CK, BB-type creatine kinase, BCK, brain creatine kinase, brain type creatine kinase, brain-type CK, brain-type creatine kinase, CK, CK MM, CK-B, CK-BB, CK-MB, CK-MM, ckb, CKM, CKMB, CKMBI, CKMiMi, creatine kinase, creatine kinase B, creatine kinase M-type, creatine kinase MB, creatine kinase muscle type, creatine kinase-MB, creatine N-phosphotransferase, creatine phosphokinase, creatine phosphotransferase, creatinine kinase, creatinine kinase MB, hBBCK, hMMCK, kinase, creatine (phosphorylating), M-CK, M1-CK, MB-CK, MCK, Mi-CK, MiMi-CK, mit-CK, mitochondrial creatine kinase, MM-CK, MM-type creatine kinase, More, MtCK, muscle creatine kinase, muscle type creatine kinase, muscle-type creatine kinase, phosphocreatine kinase, plasma creatine kinase, PSCKM, recombinant human brain-type creatine kinase, rHBCK, RM-CK, s-type CK, sarcomeric CK, sMiCK, sMtCK, u-type CK, ubiquitous CK, ubiquitous MtCK, uMiCK, uMtCK, zMMCK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.3 Phosphotransferases with a nitrogenous group as acceptor
                2.7.3.2 creatine kinase

Engineering

Engineering on EC 2.7.3.2 - creatine kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
A189D
Km and kcat values similar to wild-type, T0.5 (°C): 46.2 (wild-type: 48.0°C)
A205S
Km and kcat values similar to wild-type, T0.5 (°C): 46.6 (wild-type: 48.0°C)
E185Q
Km (ATP) and (creatine) significantly higher compared to wild-type, kcat value 74% of wild-type, T0.5 (°C): 47.4 (wild-type: 48.0°C)
H267A
Km and kcat values similar to wild-type, T0.5 (°C): 47.6 (wild-type: 48.0°C)
K36L
Km and kcat values similar to wild-type, T0.5 (°C): 46.7 (wild-type: 48.0°C)
N146C
Km and kcat values similar to wild-type, T0.5 (°C): 51 (wild-type: 48.0°C)
Q46E
Km and kcat values similar to wild-type, T0.5 (°C): 50.9 (wild-type: 48.0°C)
S329A
Km and kcat values similar to wild-type, T0.5 (°C): 48.3 (wild-type: 48.0°C)
T304K
Km and kcat values similar to wild-type, T0.5 (°C): 47.6 (wild-type: 48.0°C)
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
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
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
A76G
mutation in the intra-subunit domain-domain interface, similar to wild-type in kinetics and thermal inactivation
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
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
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
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
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
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
P20G
disruption of subunit cohesion, causing dissociation of the functional homodimer into monomers with reduced catalytic activity
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
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
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
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
additional information