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0.0003 - 366000
chorismate
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
0.0003
chorismate
30°C, pH 7, mutant R90G
0.00983
chorismate
-
mutant enzyme Lys39Arg
0.042
chorismate
-
mutant enzyme Q88N, in PBS buffer (pH 7.5) at 20°C
0.0492
chorismate
-
mutant enzyme Lys39Asn
0.11
chorismate
mutant enzyme G86A
0.123
chorismate
-
mutant enzyme Lys39Arg
0.29
chorismate
30°C, pH 7, mutant C88S/R90K
0.32
chorismate
30°C, pH 7, mutant C88K/R90S
0.41
chorismate
-
mutant enzyme F77W, in PBS buffer (pH 7.5) at 20°C
0.5
chorismate
-
mutant enzyme V35A, in PBS buffer (pH 7.5) at 20°C
0.78
chorismate
pH 7.5, 37°C, recombinant BsCM_2
1.05
chorismate
-
at 37°C
1.3
chorismate
-
mutant enzyme D48G, in PBS buffer (pH 7.5) at 20°C
2 - 8
chorismate
-
mutant DELTA117-127
2
chorismate
wild type enzyme
2.3
chorismate
-
30°C, pH 7.2, mutant H239N
2.6
chorismate
-
mutant enzyme R51Q, in PBS buffer (pH 7.5) at 20°C
3
chorismate
-
wild type enzyme, in PBS buffer (pH 7.5) at 20°C
4.8
chorismate
-
30°C, pH 7.2, mutant H245N
5.5
chorismate
at 37°C and pH 7.5
6
chorismate
-
30°C, pH 7.2, mutant H347N
7.2
chorismate
-
30°C, pH 7.2, mutant H131A
8
chorismate
-
30°C, pH 7.2, mutant H257A
10
chorismate
-
30°C, pH 7.2, mutant H153N
13
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
13
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
14
chorismate
-
mutant enzyme Glu23Ala, activated by 0.01 mM Trp
15
chorismate
-
30°C, pH 7.2, mutant H265A
15
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
16
chorismate
-
30°C, pH 7.2, mutant H197N
16
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
16.1
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
18.8
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
19.5
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
20.7
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
22
chorismate
-
30°C, pH 7.5, mutant DELTA118-127, with 5.8 mM substrate
22.8
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
23
chorismate
-
30°C, pH 7.5, mutant DELTA119-127/D118N, with 5.8 mM substrate
23.8
chorismate
37°C, in presence of 0.1 mM tyrosine
24
chorismate
-
30°C, pH 7.5, mutant DELTA118-127, with 3.4 mM substrate
26
chorismate
-
30°C, pH 7.5, mutant DELTA117-127, with 3.8 mM substrate and DELTA 118-127/R116L/P117T, with 3.9 mM substrate
27
chorismate
-
30°C, pH 7.2, wild-type
30
chorismate
-
30°C, pH 7.5, mutant DELTA118-127/K111N/A112S/V113N, with 4 mM substrate
33.4
chorismate
mutant I81L/V85I
36.55
chorismate
mutant L7I
38.7
chorismate
recombinant enzyme, pH 8.0, temperature not specified in the publication
38.87
chorismate
wild type
39
chorismate
-
wild-type enzyme
39
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
40.7
chorismate
-
genetically engineered enzyme containg the amino acid residues 1-300
41
chorismate
-
wild-type
41.4
chorismate
-
wild-type enzyme
44
chorismate
-
mutant enzyme Tyr234Glu, activated by 0.01 mM Trp
44.3
chorismate
-
genetically engineered enzyme containg the amino acid residues 1-285
45.13
chorismate
mutant A32S
46
chorismate
30°C, pH 7, wild-type
46
chorismate
pH 7.5, 37°C, recombinant AroH
47
chorismate
-
30°C, pH 7.5, wild-type, with 4 mM substrate
50
chorismate
-
untagged enzyme, at 30°C and pH 7.5
50.77
chorismate
mutant V35I
52
chorismate
70°C, pH 7.6
56
chorismate
-
leaderless MtCM with C-terminal His tag, at 30°C and pH 7.5
60
chorismate
pH 7.0, 37°C
60
chorismate
+/-4, substrate chorismate
64
chorismate
-
chorismate mutase domain of P-protein
70
chorismate
at 37°C and pH 7.5
74
chorismate
-
mutant enzyme Tyr234Ser, activated by 0.01 mM Trp
82
chorismate
Q9Y7B2
30°C, pH 7.6
89.3
chorismate
37°C, in presence of 0.1 mM tyrosine
92
chorismate
Q9Y7B2
30°C, pH 7.6, in presence of 0.005 mM tryptophan
171
chorismate
-
mutant enzyme Glu23Gln, activated by 0.01 mM Trp
252
chorismate
-
mutant enzyme Tyr234Ala, activated by 0.01 mM Trp
351
chorismate
-
mutant enzyme Thr226Ile, activated by 0.01 mM Trp
361
chorismate
-
wild-type enzyme, activated by 0.01 mM Trp
535
chorismate
-
mutant enzyme Ile225Thr/Thr226Ile, activated by 0.01 mM Trp
565
chorismate
-
mutant enzyme Tyr234Phe, activated by 0.01 mM Trp
625
chorismate
-
mutant enzyme Glu23Asp, activated by 0.01 mM Trp
140500
chorismate
-
37°C, pH 7.8, in presence of P-protein
141000
chorismate
-
37°C, pH 7.8, in presence of P-protein
148900
chorismate
-
37°C, pH 7.8, chorismate mutase
149000
chorismate
-
37°C, pH 7.8, chorismate mutase
234000
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 0.05 mM phenylalanine
234100
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 0.05 mM phenylalanine
253000
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 0.5 mM phenylalanine
253400
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 0.5 mM phenylalanine
257900
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 2 mM phenylalanine
258000
chorismate
-
37°C, pH 7.8, DELTA102-285 in presence of 2 mM phenylalanine
365600
chorismate
-
37°C, pH 7.8, DELTA102-285
366000
chorismate
-
37°C, pH 7.8, DELTA102-285
94100
prephenate
-
37°C, pH 7.8, in presence of P-protein
94140
prephenate
-
37°C, pH 7.8, in presence of P-protein
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
turnover of mutant H189N enzyme is lower than 0.0025 per second
additional information
additional information
-
turnover of mutant H189N enzyme is lower than 0.0025 per second
-
additional information
additional information
-
CM spezific activity in Escherichia coli extracts: Control (M. Tuberculosis) Sp act (U/mg) 0.889 Cloned extract/control 1 AroQMt (Rv0948c) Sp act (U/mg) 127.38 Cloned extract/control 143.28 *AroQMt (Rv1885c) Sp act (U/mg) 94.23 Cloned extract/control 105.9. CM specific activity in Escherichia coli cells expressing either the AroQMt or the *AroQMt protein is determined to be, repectively, 143- and 106-fold higher than the enzyme activity obtained for Escherichia coli cells carrying the pET-23a(+) expression vector
-
additional information
additional information
R90Cit 10E4-fold decrease in the catalytic activity of kcat. R90K 10E4-fold decrease in the catalytic activity of kcat/Km is obtained
-
additional information
additional information
-
R90Cit 10E4-fold decrease in the catalytic activity of kcat. R90K 10E4-fold decrease in the catalytic activity of kcat/Km is obtained
-
additional information
additional information
The kcat of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown
-
additional information
additional information
-
The kcat of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown
-