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(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
acetate + pyruvate
citramalate
acetyl-CoA + 2-oxobutyrate + H2O
?
-
-
-
-
?
acetyl-CoA + 2-oxoisovalerate + H2O
?
-
-
-
-
?
acetyl-CoA + glyoxylate + H2O
?
-
-
-
-
?
acetyl-CoA + pyruvate
(3S)-citramalyl-CoA
-
the enzyme is strictly specific for pyruvate as keto acid substrate
-
-
?
acetyl-CoA + pyruvate + H2O
(2S)-2-hydroxy-2-methylbutanedioate + CoA
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methyl-butanedioate
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
acetyl-CoA + pyruvate + H2O
CoA + (2S)-2-hydroxy-2-methylbutanedioate
-
-
-
r
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
acetyl-CoA + pyruvate + H2O
CoA + citramalate
pyruvate + acetyl-CoA + H2O
(2R)-2-hydroxy-2-methylbutanedioate + CoA
-
-
-
?
additional information
?
-
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
-
-
-
?
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
-
-
-
r
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
-
-
-
?
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
-
-
-
r
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
-
-
-
-
r
acetate + pyruvate
citramalate
-
-
-
?
acetate + pyruvate
citramalate
-
-
-
?
acetyl-CoA + pyruvate + H2O
(2S)-2-hydroxy-2-methylbutanedioate + CoA
-
-
-
-
r
acetyl-CoA + pyruvate + H2O
(2S)-2-hydroxy-2-methylbutanedioate + CoA
-
-
-
-
r
acetyl-CoA + pyruvate + H2O
(2S)-2-hydroxy-2-methylbutanedioate + CoA
-
-
-
-
r
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methyl-butanedioate
-
-
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methyl-butanedioate
-
-
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
-
i.e. (-)-citramalate
-
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
13C-labeled sodium acetate in culture medium to trace carbon pathways
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
-
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
-
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
-
(R)-citramalate is 2-methylmalate
-
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
the enzyme is involved in the biosynthesis of isoleucine
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
-
14C-labeled acetyl-CoA
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
-
-
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
-
the enzyme is involved in the threonine-independent biosynthesis of isoleucine via an alternative beta-methyl-D-malate pathway, the expression of cimA is transcriptionally regulated by isoleucine
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
-
the enzyme is strictly specific for pyruvate as the keto acid substrate
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
-
-
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
-
-
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
the organism exhibits an inactive pentose phosphate pathway and an alternate isoleucine biosynthesis pathway via the citramalate pathway that uses pyruvate and acetyl-CoA as precursors
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
-
-
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
-
-
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
-
-
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
-
-
-
?
acetyl-CoA + pyruvate + H2O
CoA + citramalate
-
-
-
-
?
additional information
?
-
-
LA2350 is a citramalate synthase without detectable alpha-isopropylmalate synthase activity
-
-
?
additional information
?
-
-
LiCMS shows high substrate specificity for pyruvate, but has very weak or no detectable activities for other alpha-oxo acids, such as glyoxylate, 2-oxobutyrate, and 2-oxoisovalerate
-
-
?
additional information
?
-
-
no activity with alpha-ketoglutarate, alpha-ketoadipate, alpha-ketopimelate, alpha-ketoisovalerate, and acetyl-CoA
-
-
?
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0.465 - 12.61
2-oxobutyrate
0.098 - 52.85
2-oxoisovalerate
0.465
2-oxobutyrate
-
L81A mutant
0.47 - 1
2-oxobutyrate
-
L104V mutant
0.695
2-oxobutyrate
-
wild-type
0.695
2-oxobutyrate
-
wild type LiCMS
2.924
2-oxobutyrate
-
L81V mutant
6.519
2-oxobutyrate
-
Y144V mutant
12.61
2-oxobutyrate
-
Y144L mutant
0.098
2-oxoisovalerate
-
L81A mutant
0.151
2-oxoisovalerate
-
Y144L mutant
0.253
2-oxoisovalerate
-
L104V mutant
52.85
2-oxoisovalerate
-
Y144V mutant
0.105
acetyl-CoA
-
I47V/E114V/H126Q/T204A/L238S mutant
0.105
acetyl-CoA
-
mutant CimA3.7
0.303
acetyl-CoA
-
wild-type
0.303
acetyl-CoA
-
wild type enzyme
0.626
acetyl-CoA
-
mutant T464A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.626
acetyl-CoA
-
T464A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.629
acetyl-CoA
-
D431A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.629
acetyl-CoA
-
mutant D431A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.712
acetyl-CoA
-
mutant Q495A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.712
acetyl-CoA
-
Q495A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.743
acetyl-CoA
-
mutant P493A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.743
acetyl-CoA
-
P493A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.803
acetyl-CoA
-
mutant Y454A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.803
acetyl-CoA
-
Y454A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.838
acetyl-CoA
-
I458A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.838
acetyl-CoA
-
mutant I458A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.097
acetyl-CoA
-
mutant Y430L, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.097
acetyl-CoA
-
Y430L 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
1.116
acetyl-CoA
-
mutant V468A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.116
acetyl-CoA
-
V468A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
1.118
acetyl-CoA
-
wild-type
1.118
acetyl-CoA
-
wild type LiCMS
1.118
acetyl-CoA
-
wild type, kinetic data for the C-terminal region of LiCMS
1.118
acetyl-CoA
-
wild type, kinetic data for the catalytic reaction of the active site of LiCMS
1.118
acetyl-CoA
-
wild type, kinetic data for the substrate-binding site of LiCMS
1.118
acetyl-CoA
-
wild-type, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
1.118
acetyl-CoA
-
wild-type, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.137
acetyl-CoA
-
L81A mutant
1.137
acetyl-CoA
-
mutant L81A, kinetic data for the substrate-binding site of LiCMS
1.214
acetyl-CoA
-
L81V mutant
1.214
acetyl-CoA
-
mutant L81V, kinetic data for the substrate-binding site of LiCMS
1.511
acetyl-CoA
-
E146D mutant
1.511
acetyl-CoA
-
mutant E146D, kinetic data for the catalytic reaction of the active site of LiCMS
1.554
acetyl-CoA
-
H400A/H408A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
1.554
acetyl-CoA
-
mutant H400A/H408A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.691
acetyl-CoA
-
Y144V mutant
1.691
acetyl-CoA
-
mutant Y144V, kinetic data for the substrate-binding site of LiCMS
1.711
acetyl-CoA
-
L451V 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
1.711
acetyl-CoA
-
mutant L451V, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.904
acetyl-CoA
-
Y144L mutant
1.904
acetyl-CoA
-
mutant Y144L, kinetic data for the substrate-binding site of LiCMS
2.272
acetyl-CoA
-
wild-type, 20 microM isoleucine, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
2.272
acetyl-CoA
-
wild-type, in the presence of 0.02 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
2.391
acetyl-CoA
-
E146Q mutant
2.391
acetyl-CoA
-
mutant E146Q, kinetic data for the catalytic reaction of the active site of LiCMS
2.409
acetyl-CoA
-
N310A mutant
2.409
acetyl-CoA
-
mutant N310A, kinetic data for the C-terminal region of LiCMS
3.028
acetyl-CoA
-
L104V mutant
3.028
acetyl-CoA
-
mutant L104V, kinetic data for the substrate-binding site of LiCMS
3.2
acetyl-CoA
-
measured by CoA formation
4.246
acetyl-CoA
-
wild-type, 60 microM isoleucine, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
4.246
acetyl-CoA
-
wild-type, in the presence of 0.06 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
5.186
acetyl-CoA
-
R16K/R16Q mutant
5.186
acetyl-CoA
-
F83A mutant
5.186
acetyl-CoA
-
mutant F83A, kinetic data for the catalytic reaction of the active site of LiCMS
5.273
acetyl-CoA
-
LiCMSN, N-terminal domain of LiCMS
5.273
acetyl-CoA
-
LiCMSN mutant
5.273
acetyl-CoA
-
LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS
5.851
acetyl-CoA
-
D304A mutant
5.851
acetyl-CoA
-
mutant D304A, kinetic data for the C-terminal region of LiCMS
8.921
acetyl-CoA
-
L311A mutant
8.921
acetyl-CoA
-
mutant L311A, kinetic data for the C-terminal region of LiCMS
1.023
glyoxylate
-
Y144V mutant
1.47
glyoxylate
-
wild-type
1.47
glyoxylate
-
wild type LiCMS
2.898
glyoxylate
-
L104V mutant
3.498
glyoxylate
-
Y144L mutant
7.225
glyoxylate
-
L81V mutant
10.6
glyoxylate
-
L81A mutant
0.04
pyruvate
-
recombinant enzyme, pH 8.0, 37°C
0.06
pyruvate
-
wild-type
0.06
pyruvate
-
wild type LiCMS
0.06
pyruvate
-
wild type, kinetic data for the C-terminal region of LiCMS
0.06
pyruvate
-
wild type, kinetic data for the catalytic reaction of the active site of LiCMS
0.06
pyruvate
-
wild type, kinetic data for the substrate-binding site of LiCMS
0.06
pyruvate
-
wild-type, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.06
pyruvate
-
wild-type, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.094
pyruvate
-
wild-type, 1 microM isoleucine, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.094
pyruvate
-
wild-type, in the presence of 0.001 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.105
pyruvate
-
L104V mutant
0.105
pyruvate
-
L104 mutant
0.105
pyruvate
-
mutant L104V, kinetic data for the substrate-binding site of LiCMS
0.15
pyruvate
-
LiCMSN, N-terminal domain of LiCMS
0.15
pyruvate
-
LiCMSN mutant
0.15
pyruvate
-
LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS
0.153
pyruvate
-
D304A mutant
0.153
pyruvate
-
mutant D304A, kinetic data for the C-terminal region of LiCMS
0.17
pyruvate
-
N310A mutant
0.17
pyruvate
-
mutant N310A, kinetic data for the C-terminal region of LiCMS
0.178
pyruvate
-
wild-type, 4 microM isoleucine, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.178
pyruvate
-
wild-type, in the presence of 0.004 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.184
pyruvate
-
wild-type
0.184
pyruvate
-
wild type enzyme
0.198
pyruvate
-
L81V mutant
0.198
pyruvate
-
mutant L81V, kinetic data for the substrate-binding site of LiCMS
0.263
pyruvate
-
D17N mutant
0.263
pyruvate
-
mutant D17N, kinetic data for the catalytic reaction of the active site of LiCMS
0.282
pyruvate
-
L81A mutant
0.282
pyruvate
-
mutant L81A, kinetic data for the substrate-binding site of LiCMS
0.342
pyruvate
-
I47V/E114V/H126Q/T204A/L238S mutant
0.342
pyruvate
-
mutant CimA3.7
0.979
pyruvate
-
T179A mutant
0.979
pyruvate
-
mutant T179A, kinetic data for the catalytic reaction of the active site of LiCMS
1.272
pyruvate
-
L311A mutant
1.272
pyruvate
-
mutant L311A, kinetic data for the C-terminal region of LiCMS
2.036
pyruvate
-
D17A mutant
2.036
pyruvate
-
mutant D17A, kinetic data for the catalytic reaction of the active site of LiCMS
6.859
pyruvate
-
Y144V mutant
6.859
pyruvate
-
mutant Y144V, kinetic data for the substrate-binding site of LiCMS
15.53
pyruvate
-
Y144L mutant
15.53
pyruvate
-
mutant Y144L, kinetic data for the substrate-binding site of LiCMS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.005 - 0.62
2-oxobutyrate
0.018 - 0.062
2-oxoisovalerate
0.005
2-oxobutyrate
-
Y144L mutant
0.014
2-oxobutyrate
-
L81V mutant
0.03
2-oxobutyrate
-
L104V mutant
0.05
2-oxobutyrate
-
L81A mutant
0.09
2-oxobutyrate
-
wild-type
0.09
2-oxobutyrate
-
wild type LiCMS
0.62
2-oxobutyrate
-
Y144V mutant
0.018
2-oxoisovalerate
-
L81A mutant
0.023
2-oxoisovalerate
-
Y144L mutant
0.03
2-oxoisovalerate
-
L104V mutant
0.062
2-oxoisovalerate
-
Y144V mutant
0.017
acetyl-CoA
-
Y144L mutant
0.017
acetyl-CoA
-
mutant Y144L, kinetic data for the substrate-binding site of LiCMS
0.36
acetyl-CoA
-
wild-type
0.6
acetyl-CoA
-
Y144V mutant
0.6
acetyl-CoA
-
mutant Y144V, kinetic data for the substrate-binding site of LiCMS
0.6
acetyl-CoA
-
mutant Y454A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.6
acetyl-CoA
-
Y454A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.62
acetyl-CoA
-
D304A mutant
0.62
acetyl-CoA
-
mutant D304A, kinetic data for the C-terminal region of LiCMS
0.7
acetyl-CoA
-
L81A mutant
0.7
acetyl-CoA
-
mutant L81A, kinetic data for the substrate-binding site of LiCMS
0.7
acetyl-CoA
-
I458A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
0.7
acetyl-CoA
-
mutant I458A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.84
acetyl-CoA
-
I47V/E114V/H126Q/T204A/L238S mutant
1.1
acetyl-CoA
-
L81V mutant
1.1
acetyl-CoA
-
LiCMSN, N-terminal domain of LiCMS
1.1
acetyl-CoA
-
LiCMSN mutant
1.1
acetyl-CoA
-
LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS
1.1
acetyl-CoA
-
mutant L81V, kinetic data for the substrate-binding site of LiCMS
1.7
acetyl-CoA
-
L311A mutant
1.7
acetyl-CoA
-
mutant L311A, kinetic data for the C-terminal region of LiCMS
2
acetyl-CoA
-
D431A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
2
acetyl-CoA
-
mutant D431A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
2.1
acetyl-CoA
-
E146D mutant
2.1
acetyl-CoA
-
mutant E146D, kinetic data for the catalytic reaction of the active site of LiCMS
2.4
acetyl-CoA
-
E146Q mutant
2.4
acetyl-CoA
-
mutant E146Q, kinetic data for the catalytic reaction of the active site of LiCMS
2.4
acetyl-CoA
-
L451V 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
2.4
acetyl-CoA
-
mutant L451V, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
2.4
acetyl-CoA
-
mutant T464A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
2.4
acetyl-CoA
-
T464A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
3.7
acetyl-CoA
-
mutant Q495A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
3.7
acetyl-CoA
-
Q495A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
3.9
acetyl-CoA
-
L104V mutant
3.9
acetyl-CoA
-
mutant L104V, kinetic data for the substrate-binding site of LiCMS
4
acetyl-CoA
-
mutant P493A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
4
acetyl-CoA
-
P493A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
4.5
acetyl-CoA
-
mutant Y430L, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
4.5
acetyl-CoA
-
Y430L 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
5
acetyl-CoA
-
mutant V468A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
5
acetyl-CoA
-
V468A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
5.9
acetyl-CoA
-
N310A mutant
5.9
acetyl-CoA
-
mutant N310A, kinetic data for the C-terminal region of LiCMS
8.5
acetyl-CoA
-
R16K/R16Q mutant
8.5
acetyl-CoA
-
F83A mutant
8.5
acetyl-CoA
-
mutant F83A, kinetic data for the catalytic reaction of the active site of LiCMS
9.1
acetyl-CoA
-
H400A/H408A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
9.1
acetyl-CoA
-
mutant H400A/H408A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
10.3
acetyl-CoA
-
wild-type
10.3
acetyl-CoA
-
wild type LiCMS
10.3
acetyl-CoA
-
wild type, kinetic data for the C-terminal region of LiCMS
10.3
acetyl-CoA
-
wild type, kinetic data for the catalytic reaction of the active site of LiCMS
10.3
acetyl-CoA
-
wild type, kinetic data for the substrate-binding site of LiCMS
10.3
acetyl-CoA
-
wild-type, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
10.3
acetyl-CoA
-
wild-type, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
10.6
acetyl-CoA
-
wild-type, 20 microM isoleucine, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
10.6
acetyl-CoA
-
wild-type, in the presence of 0.02 mM isoleucine 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
11.1
acetyl-CoA
-
wild-type, 60 microM isoleucine, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
11.1
acetyl-CoA
-
wild-type, in the presence of 0.06 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.005
glyoxylate
-
Y144L mutant
0.03
glyoxylate
-
Y144V mutant
0.19
glyoxylate
-
L81A mutant
0.21
glyoxylate
-
L81V mutant
0.51
glyoxylate
-
wild-type
0.51
glyoxylate
-
wild type LiCMS
0.6
glyoxylate
-
L104V mutant
0.12
pyruvate
-
Y144L mutant
0.12
pyruvate
-
mutant Y144L, kinetic data for the substrate-binding site of LiCMS
0.32
pyruvate
-
D304A mutant
0.32
pyruvate
-
mutant D304A, kinetic data for the C-terminal region of LiCMS
0.36
pyruvate
-
wild-type
0.36
pyruvate
-
wild type enzyme
0.4
pyruvate
-
LiCMSN, N-terminal domain of LiCMS
0.4
pyruvate
-
LiCMSN mutant
0.4
pyruvate
-
LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS
0.58
pyruvate
-
L81A mutant
0.58
pyruvate
-
mutant L81A, kinetic data for the substrate-binding site of LiCMS
0.84
pyruvate
-
I47V/E114V/H126Q/T204A/L238S mutant
0.84
pyruvate
-
mutant CimA3.7
0.9
pyruvate
-
L81V mutant
0.9
pyruvate
-
mutant L81V, kinetic data for the substrate-binding site of LiCMS
1.7
pyruvate
-
L311A mutant
1.7
pyruvate
-
Y144V mutant
1.7
pyruvate
-
mutant L311A, kinetic data for the C-terminal region of LiCMS
1.7
pyruvate
-
mutant Y144V, kinetic data for the substrate-binding site of LiCMS
1.9
pyruvate
-
D17N mutant
1.9
pyruvate
-
mutant D17N, kinetic data for the catalytic reaction of the active site of LiCMS
2.41
pyruvate
-
recombinant enzyme, pH 8.0, 37°C
2.7
pyruvate
-
L104V mutant
2.7
pyruvate
-
mutant L104V, kinetic data for the substrate-binding site of LiCMS
2.9
pyruvate
-
D17A mutant
2.9
pyruvate
-
mutant D17A, kinetic data for the catalytic reaction of the active site of LiCMS
3.8
pyruvate
-
N310A mutant
3.8
pyruvate
-
mutant N310A, kinetic data for the C-terminal region of LiCMS
4.9
pyruvate
-
T179A mutant
4.9
pyruvate
-
mutant T179A, kinetic data for the catalytic reaction of the active site of LiCMS
9.1
pyruvate
-
wild type LiCMS
9.1
pyruvate
-
wild type, kinetic data for the C-terminal region of LiCMS
9.1
pyruvate
-
wild type, kinetic data for the substrate-binding site of LiCMS
9.1
pyruvate
-
wild-type, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
9.1
pyruvate
-
wild-type, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
9.13
pyruvate
-
wild-type
9.13
pyruvate
-
wild type LiCMS
9.13
pyruvate
-
wild type, kinetic data for the catalytic reaction of the active site of LiCMS
9.2
pyruvate
-
wild-type, 1 microM isoleucine, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
9.2
pyruvate
-
wild-type, in the presence of 0.001 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
9.3
pyruvate
-
wild-type, 4 microM isoleucine, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
9.3
pyruvate
-
wild-type, in the presence of 0.004 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.74
acetyl-CoA
-
mutant Y454A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.8
acetyl-CoA
-
mutant I458A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.4
acetyl-CoA
-
L451V 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
1.4
acetyl-CoA
-
mutant L451V, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
2.6
acetyl-CoA
-
wild-type, 60 microM isoleucine, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
2.6
acetyl-CoA
-
wild-type, in the presence of 0.06 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
3.2
acetyl-CoA
-
D431A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
3.2
acetyl-CoA
-
mutant D431A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
3.8
acetyl-CoA
-
mutant T464A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
3.8
acetyl-CoA
-
T464A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
4.1
acetyl-CoA
-
mutant Y430L, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
4.1
acetyl-CoA
-
Y430L 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
4.5
acetyl-CoA
-
mutant V468A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
4.5
acetyl-CoA
-
V468A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
4.6
acetyl-CoA
-
wild-type, 20 microM isoleucine, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
4.6
acetyl-CoA
-
wild-type, in the presence of 0.02 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
5.2
acetyl-CoA
-
mutant Q495A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
5.2
acetyl-CoA
-
Q495A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
5.4
acetyl-CoA
-
mutant P493A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
5.4
acetyl-CoA
-
P493A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
5.9
acetyl-CoA
-
H400A/H408A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
5.9
acetyl-CoA
-
mutant H400A/H408A, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
7.4
acetyl-CoA
-
Y454A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
8
acetyl-CoA
-
I458A 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
9.2
acetyl-CoA
-
wild-type, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
9.2
acetyl-CoA
-
wild-type, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
1.5
pyruvate
-
wild-type, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
5.2
pyruvate
-
wild-type, 4 microM isoleucine, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
9.8
pyruvate
-
wild-type, 1 microM isoleucine, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7
52
pyruvate
-
wild-type, in the presence of 0.004 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
98
pyruvate
-
wild-type, in the presence of 0.001 mM isoleucine, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
150
pyruvate
-
wild-type, in the presence of 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.009
isoleucine
-
mutant V468A, calculated from the Cheng-Prusoff equation
0.009
isoleucine
-
V468A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.019
isoleucine
-
wild-type, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.019
isoleucine
-
wild-type, calculated from the Cheng-Prusoff equation
0.024
isoleucine
-
mutant T464A, calculated from the Cheng-Prusoff equation
0.024
isoleucine
-
T464A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.043
isoleucine
-
H400A/H408A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.043
isoleucine
-
mutant H400A/H408A, calculated from the Cheng-Prusoff equation
0.252
isoleucine
-
L451V 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.252
isoleucine
-
mutant L451V, calculated from the Cheng-Prusoff equation
0.382
isoleucine
-
D431A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.382
isoleucine
-
mutant D431A, calculated from the Cheng-Prusoff equation
0.421
isoleucine
-
mutant Y454A, calculated from the Cheng-Prusoff equation
0.421
isoleucine
-
Y454A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.581
isoleucine
-
mutant P493A, calculated from the Cheng-Prusoff equation
0.581
isoleucine
-
P493A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.715
isoleucine
-
mutant Q495A, calculated from the Cheng-Prusoff equation
0.715
isoleucine
-
Q495A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
1.092
isoleucine
-
mutant Y430L, calculated from the Cheng-Prusoff equation
1.092
isoleucine
-
Y430L 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.075
leucine
-
mutant V468A, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.075
leucine
-
mutant V468A, calculated from the Cheng-Prusoff equation
1.302
leucine
-
mutant Y454A, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
1.302
leucine
-
mutant Y454A, calculated from the Cheng-Prusoff equation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.041
isoleucine
Leptospira interrogans
-
mutant V468A, in the presence of 0.6 mM pyruvate, 4 mM acetyl-CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS and a varied concentration of isoleucine (approx. 0-10 mM) in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.041
isoleucine
Leptospira interrogans
-
V468A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.086
isoleucine
Leptospira interrogans
-
wild-type, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.086
isoleucine
Leptospira interrogans
-
wild-type, in the presence of 0.6 mM pyruvate, 4 mM acetyl-CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS and a varied concentration of isoleucine (approx. 0-10 mM) in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.153
isoleucine
Leptospira interrogans
-
H400A/H408A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.153
isoleucine
Leptospira interrogans
-
mutant H400A/H408A, in the presence of 0.6 mM pyruvate, 4 mM acetyl-CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS and a varied concentration of isoleucine (approx. 0-10 mM) in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.177
isoleucine
Leptospira interrogans
-
mutant T464A, in the presence of 0.6 mM pyruvate, 4 mM acetyl-CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS and a varied concentration of isoleucine (approx. 0-10 mM) in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
0.177
isoleucine
Leptospira interrogans
-
T464A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.839
isoleucine
Leptospira interrogans
-
L451V 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.839
isoleucine
Leptospira interrogans
-
mutant L451V, in the presence of 0.6 mM pyruvate, 4 mM acetyl-CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS and a varied concentration of isoleucine (approx. 0-10 mM) in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
2.519
isoleucine
Leptospira interrogans
-
mutant Y454A, in the presence of 0.6 mM pyruvate, 4 mM acetyl-CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS and a varied concentration of isoleucine (approx. 0-10 mM) in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
2.519
isoleucine
Leptospira interrogans
-
Y454A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
2.815
isoleucine
Leptospira interrogans
-
D431A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
2.815
isoleucine
Leptospira interrogans
-
mutant D431A, in the presence of 0.6 mM pyruvate, 4 mM acetyl-CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS and a varied concentration of isoleucine (approx. 0-10 mM) in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
3.704
isoleucine
Leptospira interrogans
-
mutant P493A, in the presence of 0.6 mM pyruvate, 4 mM acetyl-CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS and a varied concentration of isoleucine (approx. 0-10 mM) in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
3.704
isoleucine
Leptospira interrogans
-
P493A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
4.733
isoleucine
Leptospira interrogans
-
mutant Q495A, in the presence of 0.6 mM pyruvate, 4 mM acetyl-CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS and a varied concentration of isoleucine (approx. 0-10 mM) in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
4.733
isoleucine
Leptospira interrogans
-
Q495A 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
5.073
isoleucine
Leptospira interrogans
-
mutant Y430L, in the presence of 0.6 mM pyruvate, 4 mM acetyl-CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS and a varied concentration of isoleucine (approx. 0-10 mM) in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
5.073
isoleucine
Leptospira interrogans
-
Y430L 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.343
leucine
Leptospira interrogans
-
mutant V468A, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
0.343
leucine
Leptospira interrogans
-
mutant V468A, in the presence of 0.6 mM pyruvate, 4 mM acetyl-CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS and a varied concentration of leucine (approx. 0-20 mM) in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
7.786
leucine
Leptospira interrogans
-
mutant Y454A, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7
7.786
leucine
Leptospira interrogans
-
mutant Y454A, in the presence of 0.6 mM pyruvate, 4 mM acetyl-CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS and a varied concentration of leucine (approx. 0-20 mM) in a total volume of 50 microL using 0.1 M Hepes, pH 7.7
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D404A
-
construct for kinetic and mutagenesis studies of LiCMS
H400A/H408A
-
prevents Zn2+-binding and enables dimer instead of tetramer formation, no change in enzymatic activity or the inhibition by isoleucine
H400A/H408A mutant
-
exists purely as a dimer in solution. Is inhibited by isoleucine with comparable IC50 and Ki values as the wild-type enzyme, the double mutations have very little effects on the binding (Km) of acetyl-CoA and the kcat. Binding of isoleucine with the mutant does not affect the dimeric state of the enzyme
LiCMSN
-
truncation mutant, N-terminal catalytic domain of LiCMS. Although LiCMSN can bind both pyruvate and acetyl-CoA, it is enzymatically inactive. Binding affinities of LiCMSN for acetyl-CoA and pyruvate are decreased by approx. 5fold and 2.5fold respectively compared with those of the full-length enzyme
LiCMSN1-330
-
N-terminal catalytic domain used for crystallization experiments
I47V/E111K/E121V/H126Q/T204A/M250V
I47V/E114V/H126Q/T204A/L238S
I47V/H126Q/D141E/T204A/I286V/L327H
I47V/H126Q/E183K/T204A/L253S
I47V/H126Q/T204A/K265R/F349C
I47V/H126Q/T204A/V373STOP
wild-typeDELTA
-
1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with wild-typeDELTA mutant 0.2fold for 1-propanol, production for 1-butanol is not detected
WTDELTA
-
wild-type delta, mutant generated by directed evolution
I47V/H126Q/T204A
-
CimA2delta, mutant generated by directed evolution
-
I47V/H126Q/T204A/V373STOP
D17A
-
mutation of the active site
D17A
-
construct for kinetic and mutagenesis studies of LiCMS
D17A
-
LiCMS mutant, caused a 34fold increase in the Km for pyruvate, and a 315fold decrease in the kcat
D17N
-
mutation of the active site
D17N
-
construct for kinetic and mutagenesis studies of LiCMS
D17N
-
LiCMS mutant, causes a 4.4fold increase in the Km for pyruvate, and a 480fold decrease in the kcat
D304A
-
mutation in the C-regional region of LiCMSN
D304A
-
LiCMS mutant, substantially weakens the binding of both acetyl-CoA and pyruvate and also decrease the kcat value
D431A
-
changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, severely decreased inhibition by isoleucine (increase of IC50 and Ki values)
D431A
-
has markedly increased IC50 and Ki values for isoleucine
E146D
-
mutation of the active site
E146D
-
construct for kinetic and mutagenesis studies of LiCMS
E146D
-
LiCMS mutant, minor effects on the binding of acetyl-CoA, but can cause a decrease in the kcat by more than 400fold
E146Q
-
mutation of the active site
E146Q
-
construct for kinetic and mutagenesis studies of LiCMS
E146Q
-
LiCMS mutant, minor effects on the binding of acetyl-CoA, but can cause a decrease in the kcat by more than 400fold
F83A
-
mutation of the active site
F83A
-
construct for kinetic and mutagenesis studies of LiCMS
F83A
-
LiCMS mutant, results in a 5fold increase in the Km for acetyl-CoA and a 120fold decrease in the kcat
H302A/H302N
-
mutation in the C-regional region of LiCMSN
H302A/H302N
-
construct for kinetic and mutagenesis studies of LiCMS
H302A/H302N
-
LiCMS mutant, disrupts the enzymatic activity of LiCMS
I458A
-
changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, no inhibition by isoleucine, no binding of isoleucine
I458A
-
inhibition by isoleucine is severely decreased. Lower Kcat/Km as the wild-type
L104V
-
mutation of the substrate binding site
L104V
-
construct for kinetic and mutagenesis studies of LiCMS
L311A
-
mutation in the C-regional region of LiCMSN
L311A
-
construct for kinetic and mutagenesis studies of LiCMS
L311A
-
LiCMS mutant, substantially weakens the binding of both acetyl-CoA and pyruvate and also decrease the kcat value
L451V
-
changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, severely decreased inhibition by isoleucine (increase of IC50 and Ki values)
L451V
-
inhibition by isoleucine is severely decreased
L81A
-
mutation of the substrate binding site
L81A
-
construct for kinetic and mutagenesis studies of LiCMS
L81V
-
mutation of the substrate binding site
L81V
-
construct for kinetic and mutagenesis studies of LiCMS
N310A
-
mutation in the C-regional region of LiCMSN
N310A
-
construct for kinetic and mutagenesis studies of LiCMS
N310A
-
LiCMS mutant, has a much smaller effect on the binding of pyruvate and acetyl-CoA and on the enzymatic activity
P493A
-
changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, severely decreased inhibition by isoleucine (increase of IC50 and Ki values)
P493A
-
inhibition by isoleucine is greatly decreased
Q495A
-
changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, severely decreased inhibition by isoleucine (increase of IC50 and Ki values)
Q495A
-
exhibits significantly increased IC50 and Ki values for isoleucine
R16K/R16Q
-
mutation of the active site
R16K/R16Q
-
construct for kinetic and mutagenesis studies of LiCMS
R16K/R16Q
-
LiCMS mutant, abolishes the enzymatic activity of LiCMS
T179A
-
mutation of the active site
T179A
-
construct for kinetic and mutagenesis studies of LiCMS
T179A
-
LiCMS mutant, resultes in a 16.4fold increase in the Km for pyruvate and a 186fold decrease in the kcat, confirming its functional role in the binding of pyruvate and the catalytic reaction
T464A
-
changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, minor effect on IC50 and Ki values for isoleucine
T464A
-
minor effect on the IC50 and Ki values for isoleucine
V468A
-
changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, slightly increased inhibition by isoleucine, and inhibition by leucine
V468A
-
inhibition by isoleucine is slightly decreased
Y144L
-
mutation of the substrate binding site
Y144L
-
construct for kinetic and mutagenesis studies of LiCMS
Y144V
-
mutation of the substrate binding site
Y144V
-
construct for kinetic and mutagenesis studies of LiCMS
Y312A
-
mutation in the C-regional region of LiCMSN
Y312A
-
construct for kinetic and mutagenesis studies of LiCMS
Y312A
-
LiCMS mutant, abolishes the enzymatic activity of LiCMS
Y430L
-
changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, severely decreased inhibition by isoleucine (increase of IC50 and Ki values)
Y430L
-
inhibition by isoleucine is severely decreased
Y454A
-
changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, severely decreased inhibition by isoleucine (increase of IC50 and Ki values), slight inhibition by leucine
Y454A
-
inhibition by isoleucine is severely decreased. Lower Kcat/Km as the wild-type
I47V/D86G/H126Q/T204A
-
CimA3.5, mutant generated by directed evolution
I47V/D86G/H126Q/T204A
-
CimA3.5. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.5 mutant 7.7fold for 1-propanol and 7.8fold for 1-butanol
I47V/E111K/E121V/H126Q/T204A/M250V
-
CimA3.8, mutant generated by directed evolution
I47V/E111K/E121V/H126Q/T204A/M250V
-
CimA3.8. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.8 mutant 8.2fold for 1-propanol and 21.7fold for 1-butanol
I47V/E114V/H126Q/T204A/L238S
-
CimA3.7, mutant generated by directed evolution
I47V/E114V/H126Q/T204A/L238S
-
CimA3.7, shows higher activity at all temperatures tested relative to wild-type CimA, although the difference of the specific activity is larger at lower temperature, possibly because the mutant is screened at 30°C. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.7 mutant 9.2fold for 1-propanol and 21.9fold for 1-butanol
I47V/H126Q/D141E/T204A/I286V/L327H
-
CimA3.4, mutant generated by directed evolution
I47V/H126Q/D141E/T204A/I286V/L327H
-
CimA3.4. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.4 mutant 8.1fold for 1-propanol and 6.2fold for 1-butanol
I47V/H126Q/E183K/T204A/L253S
-
CimA3.2, mutant generated by directed evolution
I47V/H126Q/E183K/T204A/L253S
-
CimA3.2. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.2 mutant 8.5fold for 1-propanol and 14.1fold for 1-butanol
I47V/H126Q/T204A
-
CimA2delta, mutant generated by directed evolution
I47V/H126Q/T204A
-
CimA2DELTA. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA2DELTA mutant 8.0fold for 1-propanol and 5.9fold for 1-butanol
I47V/H126Q/T204A/D328V
-
CimA3.6, mutant generated by directed evolution
I47V/H126Q/T204A/D328V
-
CimA3.6. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.6 mutant 7.8fold for 1-propanol and 8.0fold for 1-butanol
I47V/H126Q/T204A/K265R/F349C
-
CimA3.3, mutant generated by directed evolution
I47V/H126Q/T204A/K265R/F349C
-
CimA3.3. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.3 mutant 7.9fold for 1-propanol and 6.9fold for 1-butanol
I47V/H126Q/T204A/V373STOP
-
CimA2, contains a frameshift mutation at bp 1117, creating a CimA variant missing the C-terminal domain from the 373rd residue. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA2 mutant 3.9fold for 1-propanol and 4.3fold for 1-butanol
I47V/H126Q/T204A/V373STOP
-
CimA2, mutant generated by directed evolution
I47V/K435N/V441A
-
CimA1, leads to the highest 1-propanol production, and thus the largest 2-ketobutyrate pool and highest cimA activity. CimA1 mutant contains 3 amino acid substitutions (I47V, K435N, and V441A). 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA1 mutant 2.3fold for 1-propanol and 1.2fold for 1-butanol
I47V/K435N/V441A
-
CimA1, mutant generated by directed evolution
I47V/R53S/H126Q/T204A
-
CimA3.1, mutant generated by directed evolution
I47V/R53S/H126Q/T204A
-
CimA3.1. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.1 mutant 8.2fold for 1-propanol and 20.7fold for 1-butanol
K32N/I47V/H126Q/T204A
-
CimA3.9, mutant generated by directed evolution
K32N/I47V/H126Q/T204A
-
CimA3.9. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.9 mutant 8.1fold for 1-propanol and 11.0fold for 1-butanol
I47V/H126Q/T204A/V373STOP
-
CimA2, contains a frameshift mutation at bp 1117, creating a CimA variant missing the C-terminal domain from the 373rd residue. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA2 mutant 3.9fold for 1-propanol and 4.3fold for 1-butanol
-
I47V/H126Q/T204A/V373STOP
-
CimA2, mutant generated by directed evolution
-
I47V/K435N/V441A
-
CimA1, leads to the highest 1-propanol production, and thus the largest 2-ketobutyrate pool and highest cimA activity. CimA1 mutant contains 3 amino acid substitutions (I47V, K435N, and V441A). 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA1 mutant 2.3fold for 1-propanol and 1.2fold for 1-butanol
-
I47V/K435N/V441A
-
CimA1, mutant generated by directed evolution
-
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Xu, H.; Zhang, Y.; Guo, X.; Ren, S.; Staempfli, A.A.; Chiao, J.; Jiang, W.; Zhao, G.
Isoleucine biosynthesis in Leptospira interrogans serotype lai strain 56601 proceeds via a threonine-independent pathway
J. Bacteriol.
186
5400-5409
2004
Leptospira interrogans
brenda
Howell, D.M.; Xu, H.; White, R.H.
(R)-citramalate synthase in methanogenic archaea
J. Bacteriol.
181
331-333
1999
Methanocaldococcus jannaschii
brenda
Ma, J.; Zhang, P.; Zhang, Z.; Zha, M.; Xu, H.; Zhao, G.; Ding, J.
Molecular basis of the substrate specificity and the catalytic mechanism of citramalate synthase from Leptospira interrogans
Biochem. J.
415
45-56
2008
Leptospira interrogans
brenda
Atsumi, S.; Liao, J.C.
Directed evolution of Methanococcus jannaschii citramalate synthase for biosynthesis of 1-propanol and 1-butanol by Escherichia coli
Appl. Environ. Microbiol.
74
7802-7808
2008
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii BW25113
brenda
Risso, C.; Van Dien, S.J.; Orloff, A.; Lovley, D.R.; Coppi, M.V.
Elucidation of an alternate isoleucine biosynthesis pathway in Geobacter sulfurreducens
J. Bacteriol.
190
2266-2274
2008
Geobacter sulfurreducens (Q74C76)
brenda
Feng, X.; Mouttaki, H.; Lin, L.; Huang, R.; Wu, B.; Hemme, C.L.; He, Z.; Zhang, B.; Hicks, L.M.; Xu, J.; Zhou, J.; Tang, Y.J.
Characterization of the central metabolic pathways in Thermoanaerobacter sp. strain X514 via isotopomer-assisted metabolite analysis
Appl. Environ. Microbiol.
75
5001-5008
2009
Thermoanaerobacter sp. (B0K6M2), Thermoanaerobacter sp. X514 (B0K6M2)
brenda
Zhang, P.; Ma, J.; Zhang, Z.; Zha, M.; Xu, H.; Zhao, G.; Ding, J.
Molecular basis of the inhibitor selectivity and insights into the feedback inhibition mechanism of citramalate synthase from Leptospira interrogans
Biochem. J.
421
133-143
2009
Leptospira interrogans
brenda
Tang, Y.J.; Yi, S.; Zhuang, W.Q.; Zinder, S.H.; Keasling, J.D.; Alvarez-Cohen, L.
Investigation of carbon metabolism in "Dehalococcoides ethenogenes" strain 195 by use of isotopomer and transcriptomic analyses
J. Bacteriol.
191
5224-5231
2009
Dehalococcoides mccartyi 195
brenda
Berg, I.; Ivanovsky, R.
Enzymes of the citramalate cycle in Rhodospirillum rubrum
Microbiology
78
16-24
2009
Rhodospirillum rubrum
-
brenda
Wu, B.; Zhang, B.; Feng, X.; Rubens, J.; Huang, R.; Hicks, L.; Pakrasi, H.; Tang, Y.
Alternative isoleucine synthesis pathway in cyanobacterial species
Microbiology
156
596-602
2010
Crocosphaera subtropica ATCC 51142
brenda
Wang, Q.; Liu, X.; Qi, Q.
Biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) from glucose with elevated 3-hydroxyvalerate fraction via combined citramalate and threonine pathway in Escherichia coli
Appl. Microbiol. Biotechnol.
98
3923-3931
2014
Leptospira interrogans
brenda
Yang, J.; Choi, Y.; Lee, S.; Kang, K.; Lee, H.; Oh, Y.; Lee, S.; Park, S.; Lee, S.
Metabolic engineering of Escherichia coli for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) from glucose
Appl. Microbiol. Biotechnol.
98
95-104
2014
Methanocaldococcus jannaschii
brenda
Wu, X.; Eiteman, M.A.
Production of citramalate by metabolically engineered Escherichia coli
Biotechnol. Bioeng.
113
2670-2675
2016
Methanocaldococcus jannaschii
brenda
Wu, X.; Eiteman, M.A.
Synthesis of citramalic acid from glycerol by metabolically engineered Escherichia coli
J. Ind. Microbiol. Biotechnol.
44
1483-1490
2017
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii (Q58787), Methanocaldococcus jannaschii DSM 2661 (Q58787)
brenda
Parimi, N.S.; Durie, I.A.; Wu, X.; Niyas, A.M.M.; Eiteman, M.A.
Eliminating acetate formation improves citramalate production by metabolically engineered Escherichia coli
Microb. Cell Fact.
16
114
2017
Escherichia coli, Methanocaldococcus jannaschii (Q58787), Methanocaldococcus jannaschii DSM 2661 (Q58787)
brenda
Webb, J.P.; Arnold, S.A.; Baxter, S.; Hall, S.J.; Eastham, G.; Stephens, G.
Efficient bio-production of citramalate using an engineered Escherichia coli strain
Microbiology
164
133-141
2018
Methanocaldococcus jannaschii
brenda
Shi, S.; Si, T.; Liu, Z.; Zhang, H.; Ang, E.L.; Zhao, H.
Metabolic engineering of a synergistic pathway for n-butanol production in Saccharomyces cerevisiae
Sci. Rep.
6
25675
2016
Leptospira interrogans, Methanocaldococcus jannaschii, Geobacter sulfurreducens
brenda
Wu, X.; Tovilla-Coutino, D.B.; Eiteman, M.A.
Engineered citrate synthase improves citramalic acid generation in Escherichia coli
Biotechnol. Bioeng.
117
2781-2790
2020
Escherichia coli
brenda