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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
-
formate
-
mimics the phosphoryl group in the transition state
guanidinium hydrochloride
-
first dissociation of subunits, then unfolding into random coil
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
NaCl
enzyme activity slightly decreases with NaCl concentration up to 4 M, and a dramatic decline is observed above that value, with full inactivation at 4.5 M. In presence of guanidinium chloride, inactivation occurs much earlier. 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
NaCl
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
5-(4-benzoylbiphenyl-4-yl)-2-furoic acid
-
-
5-(4-benzoylbiphenyl-4-yl)-2-furoic acid
-
63% inhibition, docking energy -46.3 kcal/mol
Creatinine phosphate
-
competitive to MgATP2-
Creatinine phosphate
-
competitive to phosphocreatine
iodoacetamide
-
-
iodoacetamide
-
substrates can protect against alkylation
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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
deletion of N-terminal 15 amino acids causes dissociation of the functional homodimer into monomers with reduced catalytic activity
additional information
-
deletion of N-terminal 15 amino acids causes dissociation of the functional homodimer into monomers with reduced catalytic activity
additional information
-
fusion proteins of Stichopus japonicus arginine kinase and rabbit muscle creatine kinase in direction arginine kinase-creatine kinase, AK-CK and creatine kinase-arginine kinase, CK-AK. In both fusion proteins, both of the enzymes show about 50% decrease in activity and about 2fold Km values. Fused proteins have similar secondary structure, tertiary structure, molecular size, and thermodynamic stability
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