Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.35
ATP
allosteric enzyme, pH 7.0
0.0003 - 4.58
phosphoenolpyruvate
additional information
additional information
-
0.00017
ADP
pH and temperature not specified in the publication
0.00039
ADP
in presence of inhibitor suramin, pH and temperature not specified in the publication
0.03
ADP
cPK2, pH 7.5, 25°C
0.03 - 0.05
ADP
-
PKc-isozyme
0.03 - 0.05
ADP
-
25°C, pH 7.9
0.037
ADP
-
ADP in form of MgADP-
0.055
ADP
-
at pH 7.4, in the presence of 10 mM glutamate
0.069
ADP
70°C, pH not specified in the publication
0.07
ADP
cPK4, pH 7.5, 25°C
0.082 - 0.4
ADP
-
pH 7.1, 37°C
0.082 - 0.4
ADP
-
pH 7.4, 25°C
0.082 - 0.4
ADP
-
L-type isozyme, pH 7.4, 37°C
0.087
ADP
-
ADP in form of MgADP-
0.092
ADP
pH 6.0, 45°C, recombinant enzyme with His6 tag
0.0965
ADP
-
pH 7.0, 25°C
0.101
ADP
-
at pH 6.4, in the presence of 10 mM glutamate
0.113
ADP
80°C, pH not specified in the publication
0.12
ADP
Musa cavendishii
-
hyperbolic saturation kinetics, pH 6.9, 25°C
0.12
ADP
-
cosubstrate UDP, isozyme PKc, 25°C, pH 7.9
0.12
ADP
liver enzyme, pH 7.2, 22°C
0.13
ADP
anoxic liver enzyme, pH 7.2, 22°C
0.137
ADP
65°C, pH not specified in the publication
0.14
ADP
pH 6.0, 45°C, recombinant enzyme without His6 tag
0.14
ADP
cPK3, pH 7.5, 25°C
0.15
ADP
cPK1, pH 7.5, 25°C
0.16 - 0.17
ADP
-
pH 6.5, 25°C
0.16 - 0.17
ADP
-
isozyme II, 30°C, pH 6.8
0.164
ADP
50°C, pH not specified in the publication
0.2
ADP
muscle enzyme, pH 7.2, 22°C
0.2 - 0.35
ADP
-
enzyme form I
0.2 - 0.35
ADP
-
enzyme form I
0.2 - 0.35
ADP
-
30°C, pH 6.8
0.2 - 0.35
ADP
-
25°C, pH 7.9
0.2 - 0.35
ADP
Busycotypus canaliculatum
-
pH 7.0, 20°C
0.2 - 0.35
ADP
-
PKp-isozyme
0.2 - 0.35
ADP
-
PKp-isozyme
0.2 - 0.35
ADP
-
M-type isozyme, 25°C, pH 7.0
0.214
ADP
wild-type, pH 7.5
0.214
ADP
mutant E451W, pH 7.5
0.24
ADP
allosteric enzyme, pH 7.0
0.24
ADP
pH 8.0, 32°C, activation by 2 mM D-fructose-1,6-bisphosphate
0.25
ADP
mutant PKM2G415R, pH 7.6, 37°C
0.26
ADP
pH 7.0, 25°C, recombinant His-tagged enzyme
0.27
ADP
pH 7.0, 25°C, recombinant non-His-tagged enzyme
0.28
ADP
anoxic muscle enzyme, pH 7.2, 22°C
0.32
ADP
-
purified enzyme, pH 7.0, 5°C
0.34
ADP
cPK5, pH 7.5, 25°C
0.357
ADP
-
native enzyme, at pH 7.4 and 37°C
0.365
ADP
-
recombinant enzyme, at pH 7.4 and 37°C
0.39
ADP
-
in the presence of glucose 6-phosphate, pH 7.5
0.4 - 0.6
ADP
-
pH 7.4, 37°C
0.4 - 0.6
ADP
-
R-type isozyme, pH 7.4, 37°C
0.44
ADP
-
purified enzyme, pH 7.0, 35°C
0.46
ADP
-
solubilized enzyme
0.52 - 0.56
ADP
-
bound enzyme
0.57
ADP
-
purified enzyme, pH 7.0, 25°C/room temperature
0.6
ADP
-
50°C, pH not specified in the publication
0.7
ADP
-
in the presence of Mg2+, pH 7.1, 30°C
0.83
ADP
-
in the presence of ATP, pH 7.4, 37°C
0.98 - 1
ADP
-
M1-type isozyme, pH 7.4, 37°C
1.05
ADP
-
apparent value
1.4 - 1.5
ADP
-
M2-type isozyme, pH 7.4, 37°C
2
ADP
-
mutant enzyme E117K, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C
2.3
ADP
-
wild type enzyme, in the presence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C
7.99
ADP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C
14.1
ADP
-
wild type enzyme, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°Cin 50 mM Mes-Tris, pH 6.0, at 25°C
2.53
CDP
-
pH 7.4, 25°C
6.8
CDP
-
isozyme PKII, pH 7.1, 25°C
9
CDP
-
isozyme PKI, pH 7.1, 25°C
0.026
GDP
-
pH 7.5
0.0544
GDP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C
0.098 - 0.1
GDP
-
pH 7.5, 25°C
0.098 - 0.1
GDP
-
pH 7.4, 25°C
0.25 - 0.26
GDP
-
IDP, isozyme PKc, 25°C, pH 7.9
0.25 - 0.26
GDP
-
UDP, at pH 7.5
2.2
GDP
-
isozyme PKp, 25°C, pH 7.9
0.049 - 0.1
IDP
-
-
0.049 - 0.1
IDP
-
25°C, pH 7.9
0.049 - 0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049 - 0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049 - 0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049 - 0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049 - 0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049 - 0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049 - 0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049 - 0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049 - 0.1
IDP
-
isozyme PKc
0.193
IDP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C
4
IDP
-
isozyme PKp, 25°C, pH 7.9
0.0003
phosphoenolpyruvate
Y235F mutant, Vmax = 0.6 micromol/min/mg
0.0018
phosphoenolpyruvate
Y235A mutant, Vmax = 1.1 micromol/min/mg
0.0018
phosphoenolpyruvate
Y235S mutant, Vmax = 1.2 micromol/min/mg
0.0019
phosphoenolpyruvate
wild-type, Vmax = 3.8 micromol/min/mg
0.011
phosphoenolpyruvate
muscle enzyme, pH 7.2, 22°C
0.02 - 0.05
phosphoenolpyruvate
-
bound enzyme
0.02 - 0.03
phosphoenolpyruvate
-
solubilized enzyme
0.021
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mn2+- and fructose 1,6-bisphosphate activated
0.024
phosphoenolpyruvate
-
15°, pH 7.0, isoform PK I, in winter
0.025
phosphoenolpyruvate
-
purified enzyme, pH 7.0, 5°C
0.029
phosphoenolpyruvate
muscle enzyme, pH 6.6, 22°C
0.033
phosphoenolpyruvate
-
pH 7.5, 30°C
0.033
phosphoenolpyruvate
-
15°, pH 7.0, isoform PK I, in summer
0.033
phosphoenolpyruvate
-
purified enzyme, pH 7.0, 35°C
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
pH 7.5
0.04 - 0.063
phosphoenolpyruvate
-
25°C, pH 7.9
0.04 - 0.063
phosphoenolpyruvate
Busycotypus canaliculatum
-
in the absence of fructose 1,6-diphosphate
0.04 - 0.063
phosphoenolpyruvate
-
in the presence of fructose 1,6-diphosphate
0.04 - 0.063
phosphoenolpyruvate
Busycotypus canaliculatum
-
in the presence of fructose 1,6-diphosphate
0.04 - 0.063
phosphoenolpyruvate
-
in the presence of fructose 1,6-diphosphate
0.04 - 0.063
phosphoenolpyruvate
Busycotypus canaliculatum
-
pH 7.0, 20°C
0.04 - 0.063
phosphoenolpyruvate
-
2 isozymes with different kinetic mechanisms
0.045
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mn2+-activated
0.046
phosphoenolpyruvate
-
at pH 7.4
0.048
phosphoenolpyruvate
-
purified enzyme, pH 7.0, 25°C/room temperature
0.05
phosphoenolpyruvate
-
-
0.05
phosphoenolpyruvate
-
30°C, pH 8.5
0.05
phosphoenolpyruvate
cPK5, pH 7.5, 25°C
0.051
phosphoenolpyruvate
liver enzyme, pH 6.6, 22°C
0.052
phosphoenolpyruvate
-
24°C, pH 8.0
0.057
phosphoenolpyruvate
anoxic muscle enzyme, pH 6.6, 22°C
0.059
phosphoenolpyruvate
-
activated by fructose D-1,6-bisphosphate
0.06
phosphoenolpyruvate
cPK1, pH 7.5, 25°C
0.06
phosphoenolpyruvate
pH 7.0, 25°C, recombinant non-His-tagged enzyme, in presence of fructose 1,6-bisphosphate
0.061
phosphoenolpyruvate
anoxic muscle enzyme, pH 7.2, 22°C
0.064
phosphoenolpyruvate
-
-
0.066
phosphoenolpyruvate
-
pH 6.2, mutant enzyme T298C, Mn2+- and fructose 1,6-bisphosphate activated
0.069
phosphoenolpyruvate
pH 7.0, 25°C, recombinant His-tagged enzyme, in presence of fructose 1,6-bisphosphate
0.07
phosphoenolpyruvate
-
apparent value
0.073
phosphoenolpyruvate
-
recombinant enzyme, at pH 7.4 and 37°C
0.076
phosphoenolpyruvate
-
native enzyme, at pH 7.4 and 37°C
0.082
phosphoenolpyruvate
-
at pH 6.4
0.089
phosphoenolpyruvate
-
pH 6.5, 30°C
0.09
phosphoenolpyruvate
-
30°C, pH 7.5
0.092
phosphoenolpyruvate
anoxic liver enzyme, pH 6.6, 22°C
0.093
phosphoenolpyruvate
-
at pH 7.4, in the presence of 10 mM glutamate
0.093
phosphoenolpyruvate
70°C, pH not specified in the publication
0.098
phosphoenolpyruvate
Musa cavendishii
-
hyperbolic saturation kinetics, pH 6.9, 25°C
0.099
phosphoenolpyruvate
-
pH 6.2, 30°C
0.1
phosphoenolpyruvate
-
pH 6.8, 30°C
0.1
phosphoenolpyruvate
-
in the presence of D-fructose 1,6-bisphosphate
0.11
phosphoenolpyruvate
allosteric enzyme, pH 7.0
0.112
phosphoenolpyruvate
mutant C436M, pH not specified in the publication, 30°C
0.113
phosphoenolpyruvate
-
mutant enzyme C9S/C268S, in the presence of 0.1 mM ribose 5'-phosphate, in 50 mM imidazole-HCl buffer, pH 7.2, 50 mM KCl, 7 mM MgCl2, 0.12 mM NADH, 0.02 mg/ml lactate dehydrogenase, 2 mM PEP, and 4 mM ADP, at 30°C
0.115
phosphoenolpyruvate
65°C, pH not specified in the publication
0.116
phosphoenolpyruvate
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C
0.12
phosphoenolpyruvate
-
pH 6.8, 24°C
0.12
phosphoenolpyruvate
-
30°C, pH 6.5
0.13
phosphoenolpyruvate
-
wild type enzyme, in the presence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C
0.15
phosphoenolpyruvate
-
at pH 6.4, in the presence of 10 mM glutamate
0.15 - 0.16
phosphoenolpyruvate
-
-
0.15 - 0.16
phosphoenolpyruvate
-
enzyme form I
0.17
phosphoenolpyruvate
pH 8.0, 32°C, activation by 2 mM D-fructose-1,6-bisphosphate
0.17
phosphoenolpyruvate
cPK3, pH 7.5, 25°C
0.17
phosphoenolpyruvate
cPK4, pH 7.5, 25°C
0.1785
phosphoenolpyruvate
-
pH 7.0, 25°C
0.18
phosphoenolpyruvate
-
cosubstrate ADP
0.18
phosphoenolpyruvate
-
cosubstrate ADP
0.18
phosphoenolpyruvate
-
pH 7.4, 37°C
0.18
phosphoenolpyruvate
-
L-type isozyme, 25°C, pH 7.0
0.18
phosphoenolpyruvate
-
isozyme PKp
0.181
phosphoenolpyruvate
-
15°, pH 7.0, isoform PK II, in summer
0.186
phosphoenolpyruvate
-
wild type enzyme, in the presence of 0.1 mM ribose 5'-phosphate, in 50 mM imidazole-HCl buffer, pH 7.2, 50 mM KCl, 7 mM MgCl2, 0.12 mM NADH, 0.02 mg/ml lactate dehydrogenase, 2 mM PEP, and 4 mM ADP, at 30°C
0.19
phosphoenolpyruvate
-
-
0.193
phosphoenolpyruvate
-
15°, pH 7.0, isoform PK II, in winter
0.2
phosphoenolpyruvate
-
pH 7.1, 30°C, in the presence of Mg2+, 7fold lower in the presence of Mn2+
0.21
phosphoenolpyruvate
-
26°C
0.22
phosphoenolpyruvate
-
in the presence of glucose 6-phosphate, at pH 7.5
0.22
phosphoenolpyruvate
-
enzyme from larva
0.225
phosphoenolpyruvate
50°C, pH not specified in the publication
0.23
phosphoenolpyruvate
pH 7.5, 37°C
0.24
phosphoenolpyruvate
-
mutant enzyme E117K, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C
0.24
phosphoenolpyruvate
wild-type enzyme, pH not specified in the publication, 30°C
0.242
phosphoenolpyruvate
-
pH 6.2, mutant enzyme T298C, Mn2+-activated
0.26
phosphoenolpyruvate
-
enzyme from adult
0.26
phosphoenolpyruvate
80°C, pH not specified in the publication
0.27
phosphoenolpyruvate
-
in the absence of the high-affinity IgE receptor FcepsilonRI
0.3 - 0.96
phosphoenolpyruvate
-
L-type, pH 7.4, 37°C
0.31
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mg2+ and fructose 1,6-bisphosphate activated
0.31
phosphoenolpyruvate
liver enzyme, pH 7.2, 22°C
0.33
phosphoenolpyruvate
recombinant enzyme, pH 7.2, 25°C, in presence of fructose 1,6-bisphosphate
0.345
phosphoenolpyruvate
mutant C436H, pH not specified in the publication, 30°C
0.35
phosphoenolpyruvate
-
-
0.372
phosphoenolpyruvate
mutant C436A, pH not specified in the publication, 30°C
0.38
phosphoenolpyruvate
recombinant enzyme, pH 7.2, 25°C, in presence of fructose 2,6-bisphosphate
0.39
phosphoenolpyruvate
recombinant enzyme, pH 7.2, 25°C, in presence of fructose 1,6-bisphosphate
0.4 - 0.57
phosphoenolpyruvate
Pigeon
-
-
0.4 - 0.57
phosphoenolpyruvate
-
-
0.4 - 0.57
phosphoenolpyruvate
-
pH 7.4, 37°C
0.4 - 0.57
phosphoenolpyruvate
-
M2-type isozyme, pH 7.4, 37°C
0.41
phosphoenolpyruvate
-
pH 7.4, 30°C
0.45
phosphoenolpyruvate
-
allosteric enzyme, pH 7.5, 24°C
0.49
phosphoenolpyruvate
recombinant enzyme, pH 7.2, 25°C, in presence of fructose 2,6-bisphosphate
0.54
phosphoenolpyruvate
-
allosteric enzyme, pH 7.0, 24°C
0.55
phosphoenolpyruvate
pH 7.0, 25°C, recombinant His-tagged enzyme
0.55
phosphoenolpyruvate
anoxic liver enzyme, pH 7.2, 22°C
0.552
phosphoenolpyruvate
mutant S12D, pH not specified in the publication, 30°C
0.59
phosphoenolpyruvate
-
in the presence of the high-affinity IgE receptor FcepsilonRI
0.6
phosphoenolpyruvate
-
enzyme from pupae
0.61
phosphoenolpyruvate
-
wild type enzyme, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C
0.65
phosphoenolpyruvate
recombinant enzyme, pH 7.2, 25°C
0.68
phosphoenolpyruvate
pH 7.0, 25°C, recombinant non-His-tagged enzyme
0.703
phosphoenolpyruvate
mutant C436N, pH not specified in the publication, 30°C
0.76
phosphoenolpyruvate
cPK2, pH 7.5, 25°C
0.768
phosphoenolpyruvate
mutant C436T, pH not specified in the publication, 30°C
0.802
phosphoenolpyruvate
mutant C436S, pH not specified in the publication, 30°C
0.804
phosphoenolpyruvate
mutant C436D, pH not specified in the publication, 30°C
0.88
phosphoenolpyruvate
-
in the presence of alanine
0.9
phosphoenolpyruvate
-
-
1
phosphoenolpyruvate
pH 7.0, 25°C, recombinant His-tagged enzyme, in presence of glucose 6-phosphate
1.05
phosphoenolpyruvate
-
26°C
1.1
phosphoenolpyruvate
-
at 25°C
1.18
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mg2+-activated
1.2
phosphoenolpyruvate
mutant PKM2G415R, pH 7.6, 37°C
1.3
phosphoenolpyruvate
-
pH 7.4
1.4
phosphoenolpyruvate
-
R-type isozyme, pH 7.4, 37°C
1.5
phosphoenolpyruvate
-
in the absence of activator
1.88
phosphoenolpyruvate
recombinant enzyme, pH 7.2, 25°C
2.1
phosphoenolpyruvate
pH 8.0, 32°C
3.3
phosphoenolpyruvate
-
50°C, pH not specified in the publication
4.43
phosphoenolpyruvate
-
pH 6.2, mutant enzyme T298C, Mg2+- and fructose 1,6-bisphosphate activated
4.58
phosphoenolpyruvate
pH 7.0, 35°C
0.025
pyruvate
-
25°C, sample taken in June
0.055
pyruvate
-
25°C, sample taken in January
0.48
pyruvate
allosteric enzyme, pH 7.0
0.41
UDP
-
pH 7.4, 25°C
0.72 - 0.73
UDP
-
pH 7.1, 25°C
2.4
UDP
-
isozyme PKp, 25°C, pH 7.9
additional information
additional information
-
-
-
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
Busycotypus canaliculatum
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
Busycotypus canaliculatum
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
pH-dependence
-
additional information
additional information
-
allosteric enzyme
-
additional information
additional information
-
kinetic properties of phosphorylated and dephosphorylated kinases
-
additional information
additional information
-
kinetic properties compared to pyruvate kinase from other insects
-
additional information
additional information
-
alteration of kinetic properties by purification
-
additional information
additional information
-
kinetic properties of different MW-forms of Chlorella kinase
-
additional information
additional information
-
hyperbolic saturation kinetics for phosphoenolpyruvate, ADP, Mg2+, K+
-
additional information
additional information
-
assay and kinetics overview
-
additional information
additional information
-
assay and kinetics overview
-
additional information
additional information
-
assay and kinetics overview
-
additional information
additional information
-
assay and kinetics overview
-
additional information
additional information
-
assay and kinetics overview
-
additional information
additional information
-
assay and kinetics overview
-
additional information
additional information
Amaranthus sp.
-
coupled assay for leaf crude extracts
-
additional information
additional information
-
coupled assay for leaf crude extracts
-
additional information
additional information
-
coupled assay for leaf crude extracts
-
additional information
additional information
-
coupled assay for leaf crude extracts
-
additional information
additional information
-
coupled assay for leaf crude extracts
-
additional information
additional information
-
allosteric pattern dissappears at pH 5.9
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
Antarctic fish
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
influence of fructose 1,6-bisphosphate on kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Km value of the enzyme towards phosphoenolpyruvate is higher in the pupae stage than in the rest developmental stages although the same enzyme type appears to be present throughout the life span of the insect. Starvation results to activation of the enzyme by increasing the Km value in the two feeding stages, namely larvae and adult, while injury has the opposite effect
-
additional information
additional information
in the presence of the effector fructose 2,6-bisphosphate the enzyme displays a hyperbolic saturation curve, whereas in the absence of fructose 2,6-bisphosphate the curve is sigmoid. The phosphoenolpyruvate concentration for S0.5 in presence of fructose 2,6-bisphosphate is 0.08 mM, and 1.16 mM in absence, with a concomitant increase in Vmax from 492.1 U/mg in absence to 506.99 U/mg in presence of fructose 2,6-bisphosphate. For ADP, a Km of 0.32 mM has been calculated
-
additional information
additional information
-
in the presence of the effector fructose 2,6-bisphosphate the enzyme displays a hyperbolic saturation curve, whereas in the absence of fructose 2,6-bisphosphate the curve is sigmoid. The phosphoenolpyruvate concentration for S0.5 in presence of fructose 2,6-bisphosphate is 0.08 mM, and 1.16 mM in absence, with a concomitant increase in Vmax from 492.1 U/mg in absence to 506.99 U/mg in presence of fructose 2,6-bisphosphate. For ADP, a Km of 0.32 mM has been calculated
-
additional information
additional information
S0.5 value of phosphoenolpyruvate is 1.06 mM for wild-type, 1.3 mM for mutant E451W
-
additional information
additional information
-
S0.5 value of phosphoenolpyruvate is 1.06 mM for wild-type, 1.3 mM for mutant E451W
-
additional information
additional information
-
kinetics, in presence of saturated substrate concentration, the enzyme exhibits hyperbolic kinetics for both ADP and PEP
-
additional information
additional information
phosphoenolpyruvate affinity is sensitive to the nature of the side chain at position 436
-
additional information
additional information
-
phosphoenolpyruvate affinity is sensitive to the nature of the side chain at position 436
-
additional information
additional information
steady-state kinetics of recombinant wild-type and truncated PKin the absence or presence of 1 mM AMP as a function of phosphoenolpyruvate
-
additional information
additional information
-
steady-state kinetics of recombinant wild-type and truncated PKin the absence or presence of 1 mM AMP as a function of phosphoenolpyruvate
-
additional information
additional information
the kinetic mechanism is random order with a rapid equilibrium
-
additional information
additional information
-
the kinetic mechanism is random order with a rapid equilibrium
-
additional information
additional information
allosteric mechanism and structural changes, overview
-
additional information
additional information
-
allosteric mechanism and structural changes, overview
-
additional information
additional information
despite their different allosteric behavior, both isozymes display a rapid equilibrium random order kinetic mechanism. Kinetic analysis, detailed overview
-
additional information
additional information
despite their different allosteric behavior, both isozymes display a rapid equilibrium random order kinetic mechanism. Kinetic analysis, detailed overview
-
additional information
additional information
isozyme Pyk2 has a relatively lower affinity for ADP compared to isozyme Pyk1
-
additional information
additional information
isozyme Pyk2 has a relatively lower affinity for ADP compared to isozyme Pyk1
-
additional information
additional information
-
isozyme Pyk2 has a relatively lower affinity for ADP compared to isozyme Pyk1
-
additional information
additional information
Michaelis-Menten kinetics for phosphoenolpyruvate
-
additional information
additional information
-
Michaelis-Menten kinetics for phosphoenolpyruvate
-
additional information
additional information
-
torpid pyruvate kinase (PK) displays a nearly threefold increase in Km PEP as compared to control PK when assayed at 5°C
-