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0.0001 - 262.8
acetyl-CoA
0.0001 - 230.7
oxaloacetate
additional information
additional information
-
0.0001
acetyl-CoA
D317N mutant protein, value is very uncertain
0.0015
acetyl-CoA
D317G mutant protein
0.0133
acetyl-CoA
-
recombinant mutant G196V
0.03 - 0.55
acetyl-CoA
-
mutant W348Y, pH 8.0, 20°C
0.15
acetyl-CoA
-
recombinant wild-type
1.42
acetyl-CoA
presence of 5 mM phosphoenolpyruvate, pH 7.5, 37°C
2.51
acetyl-CoA
pH 7.5, 37°C
2.99
acetyl-CoA
presence of 5 mM ADP, pH 7.5, 37°C
3 - 6
acetyl-CoA
-
mutant enzyme Y145A, in presence of 0.1 M KCl
6.73
acetyl-CoA
-
mutant W348Y, pH 8.0, 20°C
7
acetyl-CoA
-
mutant A10E
8.3
acetyl-CoA
30°C, pH 8, native enzyme
8.51
acetyl-CoA
pH not specified in the publication, temperature not specified in the publication
8.56
acetyl-CoA
pH 8.0, 25°C
8.8
acetyl-CoA
30°C, pH 8, recombinant enzyme
9.17
acetyl-CoA
-
recombinant wild-type, pH 8.0
9.2
acetyl-CoA
wild-type protein
9.8
acetyl-CoA
-
wild-type, pH 8.0, 20°C
11
acetyl-CoA
-
mutant H187Q, pH 8.0, 20°C
11.2
acetyl-CoA
pH 7.5, 37°C
13
acetyl-CoA
-
mutant A361R/A10E
14.5
acetyl-CoA
-
mutant R344K, pH 8.0, 20°C
15
acetyl-CoA
-
mutant A361R
15.4
acetyl-CoA
-
mutant W245F/W115F/W17F, pH 8.0, 20°C
17
acetyl-CoA
mutant enzyme T204R, pH and temperature not specified in the publication
17.1
acetyl-CoA
pH 8.0, 25°C
18
acetyl-CoA
-
wild-type
18
acetyl-CoA
mutant enzyme G181E, pH and temperature not specified in the publication
21
acetyl-CoA
-
hexameric enzyme form
22
acetyl-CoA
-
dimeric enzyme form
23
acetyl-CoA
pH 8.0, 25°C
44
acetyl-CoA
wild type enzyme, pH and temperature not specified in the publication
54
acetyl-CoA
-
mutant enzyme T111A, in presence of 0.1 M KCl
67
acetyl-CoA
-
mutant enzyme H110A, in presence of 0.1 M KCl
78
acetyl-CoA
-
wild-type, + 0.1 M KCl
81
acetyl-CoA
-
wild-type, + 0.1 M KCl
81
acetyl-CoA
-
wild-type enzyme, in presence of 0.1 M KCl
84
acetyl-CoA
-
mutant enzyme K167A, in presence of 0.1 M KCl
95
acetyl-CoA
-
mutant enzyme Q182A, in presence of 0.1 M KCl
108
acetyl-CoA
-
mutant enzyme R163L, in presence of 0.1 M KCl
118
acetyl-CoA
-
mutant enzyme T204A, in presence of 0.1 M KCl
121
acetyl-CoA
-
mutant enzyme R109L, in presence of 0.1 M KCl
124
acetyl-CoA
-
mutant enzyme N189A, in presence of 0.1 M KCl
174
acetyl-CoA
-
with 0.1 M KCl
262.8
acetyl-CoA
at pH 8.0 and 35°C
0.5
citrate
-
mutant H187Q, pH 8.0, 20°C
7.75
citrate
-
mutant W348Y, pH 8.0, 20°C
9.17
citrate
-
recombinant enzyme, pH 8.0
11.4
citrate
-
wild-type, pH 8.0, 20°C
12.66
citrate
-
mutant H187Q, pH 8.0, 20°C
17.3
citrate
-
mutant W245F/W115F/W17F, pH 8.0, 20°C
0.0001
oxaloacetate
D317N mutant protein, value is very uncertain
0.0015
oxaloacetate
D317G mutant protein
1.53
oxaloacetate
presence of 5 mM phosphoenolpyruvate, pH 7.5, 37°C
2.76
oxaloacetate
pH 7.5, 37°C
3 - 6
oxaloacetate
-
mutant enzyme Y145A, in presence of 0.1 M KCl
3.35
oxaloacetate
presence of 5 mM ADP, pH 7.5, 37°C
6.92
oxaloacetate
pH not specified in the publication, temperature not specified in the publication
7.62
oxaloacetate
pH 8.0, 25°C
8.3
oxaloacetate
30°C, pH 8, native enzyme
8.8
oxaloacetate
30°C, pH 8, recombinant enzyme
9.2
oxaloacetate
wild-type protein
24.5
oxaloacetate
pH 8.0, 25°C
31.9
oxaloacetate
pH 8.0, 25°C
54
oxaloacetate
-
mutant enzyme T111A, in presence of 0.1 M KCl
56
oxaloacetate
-
K295 acetylated variant, pH 7.8, 25°C
67
oxaloacetate
-
mutant enzyme H110A, in presence of 0.1 M KCl
81
oxaloacetate
-
wild-type enzyme, in presence of 0.1 M KCl
84
oxaloacetate
-
mutant enzyme K167A, in presence of 0.1 M KCl
89
oxaloacetate
-
K168 acetylated variant, pH 7.8, 25°C
92
oxaloacetate
-
wild-type, pH 7.8, 25°C
95
oxaloacetate
-
mutant enzyme Q182A, in presence of 0.1 M KCl
108
oxaloacetate
-
mutant enzyme R163L, in presence of 0.1 M KCl
114
oxaloacetate
-
K283 acetylated variant, pH 7.8, 25°C
118
oxaloacetate
-
mutant enzyme T204A, in presence of 0.1 M KCl
121
oxaloacetate
-
mutant enzyme R109L, in presence of 0.1 M KCl
124
oxaloacetate
-
mutant enzyme N189A, in presence of 0.1 M KCl
170
oxaloacetate
-
with 0.1 mM KCl
230.7
oxaloacetate
at pH 8.0 and 35°C
4
propionyl-CoA
-
mutant loop/K313L/A361R
6
propionyl-CoA
-
mutant A361R
8
propionyl-CoA
-
wild-type
12
propionyl-CoA
-
dimeric enzyme form
additional information
additional information
-
values for acetyl-CoA and oxaloacetate of mutants with a loop introduced into the active site
-
additional information
additional information
-
kcat is stable over pH-range 6.0-8.0
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
chimeric mutants, overview
-
additional information
additional information
-
chimeric mutants, overview
-
additional information
additional information
-
kcat with citrate and CoA
-
additional information
additional information
-
kcat with citrate and CoA
-