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additional information
Chorismic acid
0.03
chorismate
-
mutant enzyme V35A, in PBS buffer (pH 7.5) at 20°C
0.04
chorismate
-
in presence of NAD+
0.041
chorismate
-
30°C, pH 7.2, mutant H347N
0.045
chorismate
-
in presence of Trp
0.045
chorismate
-
30°C, pH 7.2, wild-type
0.051
chorismate
-
30°C, pH 7.2, mutant H153N
0.053
chorismate
-
30°C, pH 7.2, mutant H131A
0.054
chorismate
-
wild type enzyme, in PBS buffer (pH 7.5) at 20°C
0.059
chorismate
-
mutant enzyme D48G, in PBS buffer (pH 7.5) at 20°C
0.067
chorismate
30°C, pH 7, wild-type
0.067
chorismate
pH 7.5, 37°C, recombinant AroH
0.068
chorismate
-
30°C, pH 7.2, mutant H197N
0.073
chorismate
-
mutant enzyme F77W, in PBS buffer (pH 7.5) at 20°C
0.074
chorismate
-
wild-type
0.081
chorismate
-
30°C, pH 7.5, wild-type, with 4 mM substrate
0.092
chorismate
-
pH 7.5, in absence of NAD+
0.098
chorismate
-
30°C, pH 7.2, mutant H257A
0.099
chorismate
-
30°C, pH 7.2, mutant H265A
0.126
chorismate
-
30°C, pH 7.2, mutant H239N
0.15
chorismate
30°C, pH 7, mutant R90G
0.15
chorismate
-
leaderless MtCM with C-terminal His tag, at 30°C and pH 7.5
0.15
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
0.18
chorismate
-
untagged enzyme, at 30°C and pH 7.5
0.185
chorismate
-
in absence of Trp
0.22
chorismate
mutant A32S
0.225
chorismate
-
30°C, pH 7.2, mutant H245N
0.226
chorismate
-
37°C, pH 7.8, in presence of P-protein
0.24
chorismate
-
enzyme form CM2
0.249
chorismate
mutant L7I
0.29
chorismate
-
genetically engineered monofunctional chorismate mutase that contains only 109 amino acids
0.29
chorismate
70°C, pH 7.6
0.296
chorismate
-
37°C, pH 7.8
0.3
chorismate
-
wild-type enzyme
0.304
chorismate
wild type
0.365
chorismate
mutant V35I
0.39
chorismate
-
chorismate mutase domain of P-protein
0.4
chorismate
-
chorismate, mutant enzyme Thr226Ile, activated by 0.01 mM Trp
0.4
chorismate
-
wild-type enzyme, activated by 0.01 mM Trp
0.45
chorismate
-
mutant enzyme Lys39Asn
0.5
chorismate
-
enzyme form CM2
0.5
chorismate
pH 7.0, 37°C
0.5
chorismate
+/-0.05, substrate chorismate
0.5
chorismate
at 37°C and pH 7.5
0.55
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
0.57
chorismate
mutant enzyme G86A
0.59
chorismate
-
mutant enzyme Lys39Arg
0.59 - 1
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 2 mM phenylalanine
0.628
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 0.5 mM phenylalanine
0.669
chorismate
mutant I81L/V85I
0.7
chorismate
-
mutant enzyme Tyr234Phe, activated by 0.01 mM Trp
0.8
chorismate
-
mutant enzyme Tyr234Ala, activated by 0.01 mM Trp
1
chorismate
-
strain WB672
1.036
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 0.05 mM phenylalanine
1.1
chorismate
-
enzyme CM1
1.1
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
1.14
chorismate
wild type enzyme
1.16
chorismate
-
mutant enzyme Lys39Gln
1.2
chorismate
-
mutant enzyme Q88N, in PBS buffer (pH 7.5) at 20°C
1.3
chorismate
-
mutant enzyme Tyr234Ser, activated by 0.01 mM Trp
1.3
chorismate
-
mutant enzyme R51Q, in PBS buffer (pH 7.5) at 20°C
1.5
chorismate
-
mutant enzyme Ile225Thr/Thr226Ile, activated by 0.01 mM Trp
1.5
chorismate
at 37°C and pH 7.5
1.514
chorismate
pH 7.5, 37°C, recombinant BsCM_2
1.6
chorismate
-
mutant enzyme Glu23Asp, activated by 0.01 mM Trp
1.6
chorismate
37°C, in presence of 0.01 mM tryptophan
1.7
chorismate
-
enzyme form CM1, weak positive cooperativity
1.9
chorismate
30°C, pH 7, mutant C88K/R90S
2.33
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
2.39
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
2.547
chorismate
-
37°C, pH 7.8, DELTA102-285
2.6
chorismate
-
strain 168
2.83
chorismate
-
at 37°C
3.19
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
3.9
chorismate
-
30°C, pH 7.5, mutant DELTA118-127, with 5.8 mM substrate
4
chorismate
-
30°C, pH 7.5, mutant DELTA119-127/D118N, with 5.8 mM substrate
4.1
chorismate
-
30°C, pH 7.5, mutant DELTA118-127, with 3.4 mM substrate
4.3
chorismate
30°C, pH 7, mutant C88S/R90K
5.19
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
5.2
chorismate
-
mutant enzyme Glu23Ala, activated by 0.01 mM Trp
6
chorismate
-
mutant enzyme Glu23Gln, activated by 0.01 mM Trp
6.3
chorismate
-
mutant enzyme Tyr234Glu, activated by 0.01 mM Trp
6.79
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
9.3
chorismate
-
30°C, pH 7.5, mutant DELTA117-127, with 3.8 mM substrate
9.6
chorismate
-
DELTA 117-127
15
chorismate
-
30°C, pH 7.5, mutant DELTA118-127/K111N/A112S/V113N, with 4 mM substrate
16
chorismate
-
30°C, pH 7.5, mutant DELTA118-127/R116L/P117T, with 3.9 mM substrate
0.47 - 1
prephenate
-
-
0.549
prephenate
-
37°C, pH 7.8, in presence of P-protein
additional information
Chorismic acid
Competetive inhibition by I IV Structur: increase the Km
additional information
Chorismic acid
-
Competetive inhibition by I IV Structur: increase the Km
additional information
additional information
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when the pH increases from pH 6.2 to pH 8.6 the Km-values for prephenate and chorismate increase substantially
-
additional information
additional information
sigmoid substrate saturation curve with S0.5: 16.7 mM for chorismate at 37°C and S0.5: 12 mM for chorismate at 37°C in presence of 0.1 mM tyrosine
-
additional information
additional information
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sigmoid substrate saturation curve with S0.5: 16.7 mM for chorismate at 37°C and S0.5: 12 mM for chorismate at 37°C in presence of 0.1 mM tyrosine
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
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Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
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Michaelis-Menten kinetics
-
additional information
additional information
A lower Km of 0.5 +/-0.05 mM is obtained with a 27.5 nM protein concentration (11 pmol) whereas a Km of 0.67 +/-0.05 nM is obtained with a 8 nM protein concentration (3.2 pmol)
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additional information
additional information
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A lower Km of 0.5 +/-0.05 mM is obtained with a 27.5 nM protein concentration (11 pmol) whereas a Km of 0.67 +/-0.05 nM is obtained with a 8 nM protein concentration (3.2 pmol)
-
additional information
additional information
The Km of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown
-
additional information
additional information
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The Km of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
due to instability of chorismate at higher temperature, a Km value is not determined
-
additional information
additional information
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due to instability of chorismate at higher temperature, a Km value is not determined
-
additional information
additional information
steady-state kinetics, isozyme AtCM1 shows Michaelis-Menten kinetics. Effect of aromatic amino acids on wild-type and mutant AtCM1, overview
-
additional information
additional information
steady-state kinetics, isozyme AtCM1 shows Michaelis-Menten kinetics. Effect of aromatic amino acids on wild-type and mutant AtCM1, overview
-
additional information
additional information
steady-state kinetics, isozyme AtCM1 shows Michaelis-Menten kinetics. Effect of aromatic amino acids on wild-type and mutant AtCM1, overview
-
additional information
additional information
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steady-state kinetics, isozyme AtCM1 shows Michaelis-Menten kinetics. Effect of aromatic amino acids on wild-type and mutant AtCM1, overview
-
additional information
additional information
steady-state kinetics, isozyme AtCM2, shows Michaelis-Menten kinetics
-
additional information
additional information
steady-state kinetics, isozyme AtCM2, shows Michaelis-Menten kinetics
-
additional information
additional information
steady-state kinetics, isozyme AtCM2, shows Michaelis-Menten kinetics
-
additional information
additional information
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steady-state kinetics, isozyme AtCM2, shows Michaelis-Menten kinetics
-
additional information
additional information
steady-state kinetics, isozyme AtCM3 displays positive cooperativity with a Hill coefficient of 2.1, indicating that substrate binding at one active site of the homodimer enhanced interaction at the second active site
-
additional information
additional information
steady-state kinetics, isozyme AtCM3 displays positive cooperativity with a Hill coefficient of 2.1, indicating that substrate binding at one active site of the homodimer enhanced interaction at the second active site
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additional information
additional information
steady-state kinetics, isozyme AtCM3 displays positive cooperativity with a Hill coefficient of 2.1, indicating that substrate binding at one active site of the homodimer enhanced interaction at the second active site
-
additional information
additional information
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steady-state kinetics, isozyme AtCM3 displays positive cooperativity with a Hill coefficient of 2.1, indicating that substrate binding at one active site of the homodimer enhanced interaction at the second active site
-