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(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
(2R,3S)-3-isopropylmalate + NAD+
2-isopropyl-3-oxosuccinate + NADH + H+
(2R,3S)-3-isopropylmalate + NAD+
2-ketoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxopentanoate + CO2 + NADH + H+
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxovalerate + CO2 + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
?
(2R,3S)-3-isopropylmalate + NAD+
D-3-isopropyl-2-oxosuccinate + NADH + H+
(2R,3S)-3-isopropylmalate + thionicotinamide NAD+
2-oxoisohexanoate + thionicotinamideNADH + CO2
(S)-malate + NAD+
pyruvate + NADH + CO2
-
12% of the activity with 3-isopropylmalate
-
-
?
3-(2'-methylthio)ethylmalate + NAD+
? + NADH + H+
-
-
-
?
3-ethylmalate + NAD+
3-ethylpyruvate + NADH + CO2
3-isoamylmalate + NAD+
3-isoamylpyruvate + NADH + CO2
-
-
-
-
?
3-isopropylmalate + NAD+
2-ketoisocaproate + CO2 + NADH + H+
3-isopropylmalate + NAD+
2-ketoisocaproate + NADH + CO2
3-isopropylmalate + NAD+
?
-
-
-
-
?
3-methylmalate + NAD+
3-methylpyruvate + NADH + CO2
-
-
-
-
?
3-tert-butylmalate + NAD+
3-tert-butylpyruvate + NADH + CO2
-
-
-
-
?
beta-methylmalate + NAD+
2-oxobutyrate + NADH + CO2
-
enzyme catalyzes the final step in the pyruvate pathway to 2-oxobutyrate
-
-
?
D-3-ethylmalate + NAD+
D-3-ethyl-2-oxosuccinate + NADH + H+
D-3-isobutylmalate + NAD+
D-3-isobutyl-2-oxosuccinate + NADH + H+
D-3-isopentylmalate + NAD+
D-3-isopentyl-2-oxosuccinate + NADH + H+
D-3-methylmalate + NAD+
D-3-methyl-2-oxosuccinate + NADH + H+
-
-
-
?
D-3-t-butylmalate + NAD+
D-3-t-butyl-2-oxosuccinate + NADH + H+
-
-
-
?
D-malate + NAD+
pyruvate + NADH + CO2
DL-3-isopropylmalate + NAD+
DL-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
-
?
erythro-Lg-beta-isopropylmalate + NAD+
?
-
-
-
-
r
ethylmalate + NAD+
2-oxopentanoate + NADH + H+ + CO2
-
-
-
-
?
homoisocitrate + NAD+
? + NADH + H+
isopropylmalate + NAD+
?
-
-
-
-
?
malate + NAD+
3-oxosuccinate + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + NADH + H+ + CO2
malate + NADP+
pyruvate + NADPH + CO2
-
-
-
-
?
propylmalate + NAD+
?
-
-
-
-
r
tartrate + NAD+
?
-
-
-
-
?
tartrate + NADP+
?
-
-
-
-
?
tert-butylmalate + NAD+
2-hydroxy-4,4-dimethylpentanoate + NADH + H+ + CO2
-
-
-
-
?
threo-D-3-isopropylmalate + NAD+
?
threo-DL-isopropylmalate + NAD+
2-isopropyl-3-oxosuccinate + NADH
additional information
?
-
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
-
r
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
-
r
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
-
r
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
mutant enzymes with increased activity
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
r
(2R,3S)-3-isopropylmalate + NAD+
2-isopropyl-3-oxosuccinate + NADH + H+
-
-
-
r
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
a large movement of domain 1 is induced by substrate binding, which results in the formation of the hydrophobic pocket for the gamma-isopropyl moiety of isopropylmalate
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
key enzyme in leucine biosynthesis
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
Bacillus sp. (in: Bacteria) no 38-2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
erythro-Lg-beta-isopropylmalate
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
the enzyme catalyzes the third pathway-specific reaction in the biosynthesis of leucine
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
penultimate step in leucine biosynthesis
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
enzyme is involved in leucine biosynthesis
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
639130, 639131, 639136, 639138, 639139, 639140, 639146, 639152, 639153, 639155, 639156, 639157, 639158, 639159, 639160, 639164, 639165, 639167, 724976 -
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
decarboxylation appears to take place with retention of configuration
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
enzyme of leucine biosynthesis
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
key enzyme in leucine biosynthesis
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
-
-
-
ir
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
-
-
-
ir
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
-
-
ir
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxopentanoate + CO2 + NADH + H+
the enzyme belongs to the leucine biosynthetic pathway
-
-
ir
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
-
-
ir
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxopentanoate + CO2 + NADH + H+
the enzyme belongs to the leucine biosynthetic pathway
-
-
ir
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
-
-
ir
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
-
-
ir
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
-
-
ir
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
-
-
-
ir
(2R,3S)-3-isopropylmalate + NAD+
4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
?
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
?
the enzyme is enzyme involved in leucine biosynthesis
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
D-3-isopropyl-2-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + NAD+
D-3-isopropyl-2-oxosuccinate + NADH + H+
-
-
-
?
(2R,3S)-3-isopropylmalate + thionicotinamide NAD+
2-oxoisohexanoate + thionicotinamideNADH + CO2
-
-
-
-
?
(2R,3S)-3-isopropylmalate + thionicotinamide NAD+
2-oxoisohexanoate + thionicotinamideNADH + CO2
-
-
-
-
?
3-ethylmalate + NAD+
3-ethylpyruvate + NADH + CO2
-
-
-
-
?
3-ethylmalate + NAD+
3-ethylpyruvate + NADH + CO2
-
DL-erythro-beta-ethylmalate
-
-
?
3-isopropylmalate + NAD+
2-ketoisocaproate + CO2 + NADH + H+
-
-
-
-
?
3-isopropylmalate + NAD+
2-ketoisocaproate + CO2 + NADH + H+
-
the enzyme catalyzes a step in leucine biosynthesis
-
-
?
3-isopropylmalate + NAD+
2-ketoisocaproate + NADH + CO2
-
-
-
-
?
3-isopropylmalate + NAD+
2-ketoisocaproate + NADH + CO2
-
-
-
?
D-3-ethylmalate + NAD+
D-3-ethyl-2-oxosuccinate + NADH + H+
-
-
-
-
?
D-3-ethylmalate + NAD+
D-3-ethyl-2-oxosuccinate + NADH + H+
-
-
-
?
D-3-ethylmalate + NAD+
D-3-ethyl-2-oxosuccinate + NADH + H+
-
-
-
?
D-3-isobutylmalate + NAD+
D-3-isobutyl-2-oxosuccinate + NADH + H+
-
-
-
?
D-3-isobutylmalate + NAD+
D-3-isobutyl-2-oxosuccinate + NADH + H+
-
-
-
?
D-3-isopentylmalate + NAD+
D-3-isopentyl-2-oxosuccinate + NADH + H+
-
-
-
?
D-3-isopentylmalate + NAD+
D-3-isopentyl-2-oxosuccinate + NADH + H+
-
-
-
?
D-malate + NAD+
pyruvate + NADH + CO2
-
19% of the activity with 3-isopropylmalate
-
-
?
D-malate + NAD+
pyruvate + NADH + CO2
-
-
-
-
?
D-malate + NAD+
pyruvate + NADH + CO2
-
-
-
-
?
D-malate + NAD+
pyruvate + NADH + CO2
-
-
-
-
?
homoisocitrate + NAD+
? + NADH + H+
-
-
-
?
homoisocitrate + NAD+
? + NADH + H+
-
-
-
?
malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
-
?
malate + NAD+
pyruvate + NADH + H+ + CO2
-
-
-
-
?
threo-D-3-isopropylmalate + NAD+
?
domain 1 binds the coenzyme NAD+, while the substrate 3-isopropylmalate binds mainly to domain 2
-
-
?
threo-D-3-isopropylmalate + NAD+
?
domain 1 binds the coenzyme NAD+, while the substrate 3-isopropylmalate binds mainly to domain 2
-
-
?
threo-D-3-isopropylmalate + NAD+
?
-
domain 1 binds the coenzyme NAD+, while the substrate 3-isopropylmalate binds mainly to domain 2
-
-
?
threo-D-3-isopropylmalate + NAD+
?
-
domain 1 binds the coenzyme NAD+, while the substrate 3-isopropylmalate binds mainly to domain 2
-
-
?
threo-DL-isopropylmalate + NAD+
2-isopropyl-3-oxosuccinate + NADH
-
-
-
?
threo-DL-isopropylmalate + NAD+
2-isopropyl-3-oxosuccinate + NADH
-
-
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes a step in leucine biosynthesis
-
-
?
additional information
?
-
substrate specificity-determining residues, e.g. L103, T105, A337, and T341, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
-
enzyme does not catalyze the oxidation of L-malate, L-tartrate, D-tartrate, DL-isocitrate or DL-lactate
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
-
no activity with threo-Ds-isocitrate
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
-
no activity with threo-Ds-isocitrate
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
the enzyme does not show detectable activity for isocitrate using NAD+ as a coenzyme, and is inactive with NADP+
-
-
?
additional information
?
-
-
the enzyme does not show detectable activity for isocitrate using NAD+ as a coenzyme, and is inactive with NADP+
-
-
?
additional information
?
-
the enzyme does not show detectable activity for isocitrate using NAD+ as a coenzyme, and is inactive with NADP+
-
-
?
additional information
?
-
no substrate: isocitrate
-
-
?
additional information
?
-
no substrate: isocitrate
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
-
reaction scheme based on incorporation of the rate constant of a fast protein conformational change such as domain closure derived from the separately recorded time-dependent formation of the fluorescence resonance energy transfer signal. The rate-limiting step seems to be another slower conformational change that allows product release
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
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.
0.0035 - 3.73
(2R,3S)-3-isopropylmalate
0.045 - 0.502
3-(2'-methylthio)ethylmalate
0.0039 - 0.0254
3-isopropylmalate
0.074
3-tert-butylmalate
-
-
0.0011
D-3-ethylmalate
pH 8.0
0.0015
D-3-isobutylmalate
pH 8.0
0.0058
D-3-isopentylmalate
pH 8.0
0.0012
D-3-isopropylmalate
pH 8.0
0.0037
D-3-methylmalate
pH 8.0
0.0023
D-3-t-butylmalate
pH 8.0
0.002 - 0.0133
DL-3-isopropylmalate
0.019
dl-erythro-beta-ethylmalate
-
pH 9.0, 22°C
0.0092
erythro-Lg-beta-isopropylmalate
-
pH 9.0, 22°C
0.09
ethylmalate
-
pH 7.6
5.9
homoisocitrate
at pH 8.0 and 60°C
0.000017 - 0.316
isopropylmalate
0.105
propylmalate
-
pH 7.6
0.214
tert-butylmalate
-
pH 7.6
0.051
thionicotinamide-NAD+
-
pH 9.0, 22°C
0.0061 - 0.0161
threo-D,L-isopropylmalate
0.08
threo-Ds-3-Isopropylmalate
-
60°C
additional information
additional information
-
0.0035
(2R,3S)-3-isopropylmalate
wild type enzyme, at pH 7.5 and 25°C
0.0047
(2R,3S)-3-isopropylmalate
-
acIPMDH-ML, pH 8.0, 40°C
0.005
(2R,3S)-3-isopropylmalate
at pH 8.0 and 60°C
0.0053
(2R,3S)-3-isopropylmalate
-
ancIPMDH-IQ, pH 8.0, 40°C
0.0063
(2R,3S)-3-isopropylmalate
mutant enzyme Y181H, at pH 7.5 and 25°C
0.0074
(2R,3S)-3-isopropylmalate
mutant enzyme Y181F, at pH 7.5 and 25°C
0.0083
(2R,3S)-3-isopropylmalate
mutant enzyme Y181A, at pH 7.5 and 25°C
0.0087
(2R,3S)-3-isopropylmalate
-
pressure 100 MPa, 20°C, pH not specified in the publication
0.0092
(2R,3S)-3-isopropylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.01
(2R,3S)-3-isopropylmalate
-
acIPMDH-ML, pH 8.0, 70°C
0.01
(2R,3S)-3-isopropylmalate
-
ancIPMDH-IQ, pH 8.0, 70°C
0.0109
(2R,3S)-3-isopropylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.011
(2R,3S)-3-isopropylmalate
-
pH 7.5, 37°C
0.011
(2R,3S)-3-isopropylmalate
mutant F137L, pH not specified in the publication, temperature not specified in the publication
0.0114
(2R,3S)-3-isopropylmalate
mutant enzyme V235A, at pH 7.5 and 25°C
0.0122
(2R,3S)-3-isopropylmalate
mutant enzyme L106M, at pH 7.6 and 25°C
0.0122
(2R,3S)-3-isopropylmalate
-
wild type enzyme, at pH 7.6 and 25°C
0.013
(2R,3S)-3-isopropylmalate
-
pH 7.6, 20°C, stopped flow experiment
0.013
(2R,3S)-3-isopropylmalate
mutant enzyme D217A, at pH 7.6 and 20°C
0.014
(2R,3S)-3-isopropylmalate
mutant enzyme N102A, at pH 7.6 and 20°C
0.0141
(2R,3S)-3-isopropylmalate
wild type enzyme, at pH 7.6 and 25°C
0.015
(2R,3S)-3-isopropylmalate
-
-
0.015
(2R,3S)-3-isopropylmalate
-
pressure 0.1 MPa, 20°C, pH not specified in the publication
0.016
(2R,3S)-3-isopropylmalate
wild type enzyme, at pH 7.6 and 20°C
0.016
(2R,3S)-3-isopropylmalate
wild type enzyme, in the presence of 25 mM K+, at pH 7.6 and 20°C
0.0169
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172D
0.0169
(2R,3S)-3-isopropylmalate
-
mutant enzyme A172D, at 55°C, pH not specified in the publication
0.019
(2R,3S)-3-isopropylmalate
-
pH 9.0
0.02
(2R,3S)-3-isopropylmalate
pressure 100 MPa, 20°C, pH not specified in the publication
0.02
(2R,3S)-3-isopropylmalate
mutant enzyme D245A, at pH 7.6 and 20°C
0.022
(2R,3S)-3-isopropylmalate
60°C, pH 7.6, mutant enzyme A172V
0.0221
(2R,3S)-3-isopropylmalate
-
55°C, wild-type enzyme
0.0221
(2R,3S)-3-isopropylmalate
-
wild type enzyme, at 55°C, pH not specified in the publication
0.0226
(2R,3S)-3-isopropylmalate
mutant enzyme S266A, at pH 7.6 and 25°C
0.0234
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172N
0.0234
(2R,3S)-3-isopropylmalate
-
mutant enzyme A172N, at 55°C, pH not specified in the publication
0.0239
(2R,3S)-3-isopropylmalate
-
mutant enzyme M106L, at pH 7.6 and 25°C
0.024
(2R,3S)-3-isopropylmalate
-
kcat/Km: 88000/Msec
0.0242
(2R,3S)-3-isopropylmalate
mutant enzyme L132A, at pH 7.5 and 25°C
0.025
(2R,3S)-3-isopropylmalate
pressure 0.1 MPa, 20°C, pH not specified in the publication
0.025
(2R,3S)-3-isopropylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0257
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172E
0.0257
(2R,3S)-3-isopropylmalate
-
mutant enzyme A172E, at 55°C, pH not specified in the publication
0.026
(2R,3S)-3-isopropylmalate
-
pH 9.0
0.0267
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172Q
0.0267
(2R,3S)-3-isopropylmalate
-
mutant enzyme A172Q, at 55°C, pH not specified in the publication
0.027
(2R,3S)-3-isopropylmalate
-
pressure 50 MPa, 20°C, pH not specified in the publication
0.0278
(2R,3S)-3-isopropylmalate
mutant enzyme D292N, at pH 7.5 and 25°C
0.028
(2R,3S)-3-isopropylmalate
mutant L134F, pH not specified in the publication, temperature not specified in the publication
0.0303
(2R,3S)-3-isopropylmalate
mutant L133F, pH not specified in the publication, temperature not specified in the publication
0.031
(2R,3S)-3-isopropylmalate
60°C, pH 7.6, wild-type enzyme
0.032
(2R,3S)-3-isopropylmalate
pressure 150 MPa, 20°C, pH not specified in the publication
0.032
(2R,3S)-3-isopropylmalate
mutant enzyme E270A, at pH 7.6 and 20°C
0.032
(2R,3S)-3-isopropylmalate
mutant enzyme E270A, in the presence of 25 mM K+, at pH 7.6 and 20°C
0.0344
(2R,3S)-3-isopropylmalate
-
mutant enzyme A266S, at pH 7.6 and 25°C
0.0345
(2R,3S)-3-isopropylmalate
mutant enzyme A268I, at pH 7.6 and 25°C
0.0356
(2R,3S)-3-isopropylmalate
-
mutant enzyme I268A, at pH 7.6 and 25°C
0.038
(2R,3S)-3-isopropylmalate
pressure 200 MPa, 20°C, pH not specified in the publication
0.04
(2R,3S)-3-isopropylmalate
mutant enzyme Y139A, at pH 7.6 and 20°C
0.043
(2R,3S)-3-isopropylmalate
pressure 50 MPa, 20°C, pH not specified in the publication
0.053
(2R,3S)-3-isopropylmalate
-
pressure 150 MPa, 20°C, pH not specified in the publication
0.055
(2R,3S)-3-isopropylmalate
-
pressure 200 MPa, 20°C, pH not specified in the publication
0.0707
(2R,3S)-3-isopropylmalate
mutant enzyme R146A, at pH 7.5 and 25°C
0.092
(2R,3S)-3-isopropylmalate
-
pressure 250 MPa, 20°C, pH not specified in the publication
0.108
(2R,3S)-3-isopropylmalate
pressure 250 MPa, 20°C, pH not specified in the publication
0.119
(2R,3S)-3-isopropylmalate
mutant enzyme R146K, at pH 7.5 and 25°C
0.125
(2R,3S)-3-isopropylmalate
mutant enzyme L133A, at pH 7.5 and 25°C
0.145
(2R,3S)-3-isopropylmalate
mutant enzyme K185A, at pH 7.6 and 20°C
0.255
(2R,3S)-3-isopropylmalate
mutant enzyme D241A, at pH 7.6 and 20°C
0.59
(2R,3S)-3-isopropylmalate
mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
0.753
(2R,3S)-3-isopropylmalate
mutant enzyme R174K, at pH 7.5 and 25°C
0.9
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
0.9
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/V238M/R310M, pH 8.0, 37°C
1
(2R,3S)-3-isopropylmalate
mutant S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
1
(2R,3S)-3-isopropylmalate
wild-type (2R,3S)-3-isopropylmalate dehydrogenase, pH 8.0, 37°C
1
(2R,3S)-3-isopropylmalate
wild-type HICDH, pH 8.0, 37°C
1.5
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M, pH 8.0, 37°C
1.9
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/R310M, pH 8.0, 37°C
2.6
(2R,3S)-3-isopropylmalate
mutant R85V/Y86A, pH 8.0, 37°C
3.73
(2R,3S)-3-isopropylmalate
mutant enzyme R136K, at pH 7.5 and 25°C
0.045
3-(2'-methylthio)ethylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.077
3-(2'-methylthio)ethylmalate
mutant L133F, pH not specified in the publication, temperature not specified in the publication
0.103
3-(2'-methylthio)ethylmalate
mutant L134F, pH not specified in the publication, temperature not specified in the publication
0.323
3-(2'-methylthio)ethylmalate
mutant F137L, pH not specified in the publication, temperature not specified in the publication
0.436
3-(2'-methylthio)ethylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.502
3-(2'-methylthio)ethylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0039
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant F3S/S232G
0.0044
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant L288P
0.0055
3-isopropylmalate
pH 7.5, 70°C, recombinant wild-type enzyme
0.0067
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant F3S/L288P
0.0076
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant F3S
0.008
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant R284G
0.009
3-isopropylmalate
-
wild-type
0.0122
3-isopropylmalate
-
mutant Glu253Leu
0.016
3-isopropylmalate
-
mutant Glu253Ala
0.0189
3-isopropylmalate
-
mutant Glu253Gln
0.0244
3-isopropylmalate
-
mutant Glu253Val
0.0254
3-isopropylmalate
-
mutant Glu253Trp
0.301
D-malate
-
pH 7.5, 37°C
0.41
D-malate
-
kcat/Km: 14000/Msec
0.002
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126G
0.0026
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126A
0.0027
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126T
0.0032
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126S
0.0044
DL-3-isopropylmalate
-
pH 8.0, 60°C, wild-type
0.005
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126M
0.0061
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126E
0.0084
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126I
0.0121
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126L
0.0133
DL-3-isopropylmalate
-
pH 8.0, 60°C, mutant V126F
0.000017
isopropylmalate
-
pH 7.3, 21°C, cofactor: NAD+, wild-type enzyme
0.00048
isopropylmalate
-
pH 7.3, 21°C, cofactor: NAD+, mutant enzyme E87G
0.001
isopropylmalate
-
pH 8.0, 40°C, mutant enzyme C275T
0.0012
isopropylmalate
-
pH 8.0, 40°C, mutant enzyme G376A
0.00125
isopropylmalate
-
pH 8.0, 40°C, wild-type enzyme
0.0013
isopropylmalate
-
pH 8.0, 40°C, mutant enzyme A31G/G43A/A709G
0.0024
isopropylmalate
-
pH 8.0, 40°C, mutant enzyme G43A
0.00298
isopropylmalate
-
pH 7.3, 21°C, cofactor: NADP+, wild-type enzyme
0.0053
isopropylmalate
-
pH 7.3, 21°C, cofactor: NAD+, mutant enzyme E87Q
0.0078
isopropylmalate
-
pH 8.0, 70°C, mutant enzyme C275T
0.0089
isopropylmalate
-
pH 8.0, 70°C, wild-type enzyme
0.0096
isopropylmalate
-
pH 8.0, 70°C, mutant enzyme A31G/G43A/A709G
0.01
isopropylmalate
-
pH 8.0, 70°C, mutant enzyme G376A
0.011
isopropylmalate
-
pH 8.0, 70°C, mutant enzyme G43A
0.044
isopropylmalate
-
pH 7.6, 60°C
0.105
isopropylmalate
-
pH 7.6, 40°C
0.316
isopropylmalate
-
pH 7.6, 40°C
0.0326
malate
-
pH 7.3, 21°C, cofactor: NAD+, isopropylmalate dehydrogenase mutant E87Q
1.51
malate
-
pH 7.3, 21°C, cofactor: NAD+, wild-type enzyme
31.56
malate
-
pH 7.3, 21°C, cofactor: NADP+, wild-type enzyme
35.59
malate
-
pH 7.3, 21°C, cofactor: NAD+, isopropylmalate dehydrogenase mutant E87G
0.0022
NAD+
pH 8.0, 25°C, wild-type enzyme
0.00321
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme
0.0091
NAD+
-
pH 8.0, 40°C, mutant V126S
0.0092
NAD+
-
pH 8.0, 40°C, mutant V126A
0.012
NAD+
pH 8.0, 40°C, wild-type enzyme
0.012
NAD+
-
pH 7.3, 21°C, wild-type enzyme
0.0149
NAD+
-
pH 8.0, 40°C, reaction with 3-D-isopropylmalate, mutant enzyme C275T
0.022
NAD+
-
pH 8.0, 40°C, mutant V126T
0.024
NAD+
-
pH 8.0, 40°C, mutant V126G
0.025
NAD+
-
pH 8.0, 40°C, wild-type
0.0258
NAD+
-
pH 8.0, 40°C, isopropylmalate dehydrogenase wild-type
0.031
NAD+
-
pH 7.3, 21°C, mutant enzyme S226R
0.037
NAD+
-
acIPMDH-ML, pH 8.0, 25°C
0.045
NAD+
-
ancIPMDH-IQ, pH 8.0, 25°C
0.0454
NAD+
-
pH 7.3, 21°C, reaction with tartrate, wild-type enzym
0.0515
NAD+
-
pH 8.0, 40°C, mutant V126E
0.054
NAD+
-
acIPMDH-ML, pH 8.0, 40°C
0.059
NAD+
-
pH 8.0, 60°C, mutant V126A
0.06
NAD+
mutant enzyme Y139A, at pH 7.6 and 20°C
0.062
NAD+
-
pH 8.0, 40°C, mutant V126I
0.064
NAD+
mutant enzyme K185A, at pH 7.6 and 20°C
0.067
NAD+
-
ancIPMDH-IQ, pH 8.0, 40°C
0.0708
NAD+
mutant enzyme L106M, at pH 7.6 and 25°C
0.0725
NAD+
-
pH 8.0, 60°C, mutant V126G
0.0756
NAD+
mutant enzyme S266A, at pH 7.6 and 25°C
0.076
NAD+
-
55°C, mutant enzyme A172D
0.079
NAD+
-
mutant enzyme M106L, at pH 7.6 and 25°C
0.0814
NAD+
wild type enzyme, at pH 7.6 and 25°C
0.094
NAD+
-
55°C, mutant enzyme A172Q
0.095
NAD+
-
pH 8.0, 60°C, mutant V126S
0.1
NAD+
-
55°C, mutant enzyme A172E
0.103
NAD+
-
pH 8.0, 60°C, mutant V126T
0.105
NAD+
-
55°C, mutant enzyme A172N
0.1058
NAD+
-
wild type enzyme, at pH 7.6 and 25°C
0.1065
NAD+
-
pH 7.3, 21°C, reaction with malate, wild-type enzyme
0.109
NAD+
-
pH 8.0, 60°C, mutant V126E
0.111
NAD+
-
pH 8.0, 40°C, mutant V126L
0.116
NAD+
-
55°C, wild-type enzyme
0.12
NAD+
at pH 8.0 and 60°C
0.13
NAD+
60°C, pH 7.6, pH 7.6, mutant enzyme A172V
0.131
NAD+
-
pH 7.3, 21°C, isopropylmalate dehydrogenase mutant E87G
0.139
NAD+
-
pH 7.6, 60°C
0.14
NAD+
60°C, pH 7.6, wild-type enzyme
0.144
NAD+
-
pH 8.0, 40°C, mutant V126F
0.157
NAD+
-
pH 8.0, 40°C, mutant enzyme A31G/G43A/A709G
0.157
NAD+
-
pH 7.6, 40°C
0.16
NAD+
-
pH 8.0, 40°C, mutant enzyme G43A
0.166
NAD+
-
pH 8.0, 60°C, wild-type
0.1707
NAD+
-
mutant enzyme I268A, at pH 7.6 and 25°C
0.171
NAD+
-
mutant Glu253Val
0.172
NAD+
pH 7.6, 70°C, recombinant mutant L134N
0.181
NAD+
-
pH 7.3, 21°C, isopropylmalate dehydrogenase mutant E87Q
0.198
NAD+
-
pH 8.0, 60°C, mutant V126I
0.21
NAD+
pH 8.0, 70°C, wild-type enzyme
0.22
NAD+
pH 7.5, 70°C, recombinant mutant F3S/S232G
0.225
NAD+
-
pH 8.0, 40°C, isopropylmalate dehydrogenase cold-adapted mutant T1155
0.2379
NAD+
-
mutant enzyme A266S, at pH 7.6 and 25°C
0.244
NAD+
-
mutant Glu253Trp
0.246
NAD+
-
mutant Glu253Ala
0.25
NAD+
pH 7.5, 70°C, recombinant mutant R284G
0.25
NAD+
-
pH 7.6, 20°C, stopped flow experiment
0.255
NAD+
pH 7.6, 70°C, recombinant mutant L134N/V181T/P324T/A335E
0.26
NAD+
mutant enzyme N102A, at pH 7.6 and 20°C
0.273
NAD+
-
mutant Glu253Gln
0.2785
NAD+
mutant enzyme A268I, at pH 7.6 and 25°C
0.29
NAD+
wild type enzyme, at pH 7.6 and 20°C
0.29
NAD+
wild type enzyme, in the presence of 25 mM K+, at pH 7.6 and 20°C
0.305
NAD+
mutant enzyme D217A, at pH 7.6 and 20°C
0.32
NAD+
mutant enzyme D241A, at pH 7.6 and 20°C
0.321
NAD+
-
pH 7.6, 40°C
0.336
NAD+
pH 7.6, 70°C, recombinant mutant H197K
0.341
NAD+
-
pH 8.0, 70°C, isopropylmalate wild-type
0.359
NAD+
pH 7.6, 70°C, recombinant mutant A335E
0.37
NAD+
pH 7.5, 70°C, recombinant mutant L288P
0.371
NAD+
pH 7.6, 70°C, recombinant mutant P324T
0.375
NAD+
mutant enzyme D245A, at pH 7.6 and 20°C
0.378
NAD+
-
pH 8.0, 60°C, mutant V126F
0.386
NAD+
-
pH 7.3, 21°C, isopropylmalate dehydrogenase mutant E87G
0.39
NAD+
pH 7.5, 70°C, recombinant wild-type enzyme and mutant F3S
0.391
NAD+
-
pH 8.0, 60°C, mutant V126L
0.4
NAD+
pH 7.5, 70°C, recombinant mutant F3S/L288P
0.401
NAD+
pH 7.6, 70°C, recombinant mutant R58L
0.428
NAD+
pH 7.6, 70°C, recombinant mutant P56E
0.468
NAD+
pH 7.6, 70°C, recombinant mutant F53L
0.474
NAD+
-
mutant Glu253Leu
0.514
NAD+
pH 7.6, 70°C, recombinant wild-type enzyme
0.52
NAD+
pH 7.6, 70°C, recombinant mutant V61I
0.567
NAD+
pH 7.6, 70°C, recombinant mutant V181T/P324T/A335E
0.625
NAD+
pH 7.6, 70°C, recombinant mutant S261N
0.642
NAD+
pH 7.6, 70°C, recombinant mutant V181T
0.66
NAD+
mutant enzyme E270A, at pH 7.6 and 20°C
0.66
NAD+
mutant enzyme E270A, in the presence of 25 mM K+, at pH 7.6 and 20°C
0.673
NAD+
pH 7.6, 70°C, recombinant mutant D184H
0.73
NAD+
-
acIPMDH-ML, pH 8.0, 70°C
0.778
NAD+
-
pH 7.3, 21°C, isopropylmalate dehydrogenase mutant E87Q
0.82
NAD+
-
at 70°C, mutant enzyme G43A
0.9
NAD+
mutant E57V/S72I/R85M/Y86A/M208T/V238M/R310M, pH 8.0, 37°C
0.917
NAD+
-
at 70°C, mutant enzyme A31G/G43A/A709G
0.96
NAD+
-
ancIPMDH-IQ, pH 8.0, 70°C
1.01
NAD+
-
at 40°C, isopropylmalate dehydrogenase cold-adapted mutant P215
1.01
NAD+
-
pH 8.0, 40°C, mutant V126M
1.2
NAD+
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
1.2
NAD+
mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
1.6
NAD+
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M, pH 8.0, 37°C
1.6
NAD+
mutant S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
1.7
NAD+
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/R310M, pH 8.0, 37°C
1.7
NAD+
mutant R85V/Y86A, pH 8.0, 37°C
1.836
NAD+
-
pH 7.3, 21°C, mutant enzyme S226R/D278K/I279Y
1.853
NAD+
-
pH 7.3, 21°C, reaction with malate, mutant enzyme E87Q
1.9
NAD+
wild-type (2R,3S)-3-isopropylmalate dehydrogenase, pH 8.0, 37°C
1.9
NAD+
wild-type HICDH, pH 8.0, 37°C
1.97
NAD+
-
pH 8.0, 60°C, mutant V126M
2.584
NAD+
-
pH 7.3, 21°C, reaction with malate, mutant enzyme E87G
3.56
NAD+
-
70°C, isopropylmalate dehydrogenase cold-adapted mutant P215
0.014
NADP+
-
pH 7.3, 21°C, mutant enzyme S226R/D278K/I279Y
0.02
NADP+
-
pH 7.3, 21°C, mutant enzyme D278K, I279T, P325Y and 395-Arg
0.722
NADP+
-
pH 7.3, 21°C, mutant enzyme S226R
1.573
NADP+
-
pH 7.3, 21°C, reaction with tartrate, wild-type enzyme
1.75
NADP+
-
wild-type enzyme
1.836
NADP+
-
pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme
6.579
NADP+
-
pH 7.3, 21°C, recation with malate, wild-type enzyme
0.0407
Tartrate
-
pH 7.3, 21°C, cofactor: NAD+, wild-type enzyme
0.761
Tartrate
-
pH 7.3, 21°C, cofactor: NAD+, isopropylmalate dehydrogenase mutant E87Q
0.817
Tartrate
-
pH 7.3, 21°C, cofactor: NADP+, wild-type enzyme
1.21
Tartrate
-
pH 7.3, 21°C, cofactor: NAD+, mutant enzyme E87G
0.0061
threo-D,L-isopropylmalate
pH 7.6, 70°C, recombinant wild-type enzyme
0.0063
threo-D,L-isopropylmalate
pH 7.6, 70°C, recombinant mutant V181T/P324T/A335E
0.007
threo-D,L-isopropylmalate
pH 7.6, 70°C, recombinant mutant L134N
0.0161
threo-D,L-isopropylmalate
pH 7.6, 70°C, recombinant mutant L134N/V181T/P324T/A335E
additional information
additional information
-
the Km-value for NAD+ ranges from 0.054 mM to 0.15 mM when enzyme concentration varies from 0.008 mg/ml to 0.16 mg/ml, the Km-value for 3-isopropylmalate ranges from 0.023 mM to 0.042 mM when enzyme concentration varies from 0.008 mg/ml to 0.16 mg/ml
-
additional information
additional information
-
the Km-value for NAD+ ranges from 0.054 mM to 0.15 mM when enzyme concentration varies from 0.008 mg/ml to 0.16 mg/ml, the Km-value for 3-isopropylmalate ranges from 0.023 mM to 0.042 mM when enzyme concentration varies from 0.008 mg/ml to 0.16 mg/ml
-
additional information
additional information
Michaelis-Menten kinetics of recombinant wild-type and mutant enzymes at different temperatures, overview
-
additional information
additional information
-
Michaelis-Menten kinetics of recombinant wild-type and mutant enzymes at different temperatures, overview
-
additional information
additional information
-
thermodynamic and kinetics analysis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0025 - 220
(2R,3S)-3-isopropylmalate
0.016 - 0.85
3-(2'-methylthio)ethylmalate
3.8 - 14.9
3-isopropylmalate
2.7
3-tert-butylmalate
-
-
3.1
D-3-ethylmalate
pH 8.0
3.1
D-3-isobutylmalate
pH 8.0
2.7
D-3-isopentylmalate
pH 8.0
3.6
D-3-isopropylmalate
pH 8.0
3.5
D-3-methylmalate
pH 8.0
0.96
D-3-t-butylmalate
pH 8.0
0.41
D-malate
-
pH 7.5, 37°C
0.26
homoisocitrate
at pH 8.0 and 60°C
0.09 - 69
isopropylmalate
6
tert-butylmalate
-
pH 7.6
additional information
additional information
-
the cold adaption results from the destabilization of the ternary complex caused by increase in the volume of the residue at position 126
-
0.0025
(2R,3S)-3-isopropylmalate
mutant enzyme D241A, at pH 7.6 and 20°C
0.0025
(2R,3S)-3-isopropylmalate
mutant enzyme K185A, at pH 7.6 and 20°C
0.003
(2R,3S)-3-isopropylmalate
mutant enzyme D292N, at pH 7.5 and 25°C
0.017
(2R,3S)-3-isopropylmalate
mutant enzyme Y181A, at pH 7.5 and 25°C
0.023
(2R,3S)-3-isopropylmalate
mutant enzyme R146K, at pH 7.5 and 25°C
0.03
(2R,3S)-3-isopropylmalate
mutant enzyme R146A, at pH 7.5 and 25°C
0.033
(2R,3S)-3-isopropylmalate
mutant enzyme E270A, at pH 7.6 and 20°C
0.033
(2R,3S)-3-isopropylmalate
mutant enzyme E270A, in the presence of K+, at pH 7.6 and 20°C
0.033
(2R,3S)-3-isopropylmalate
mutant enzyme R136K, at pH 7.5 and 25°C
0.045
(2R,3S)-3-isopropylmalate
mutant enzyme D217A, at pH 7.6 and 20°C
0.08
(2R,3S)-3-isopropylmalate
wild-type HICDH, pH 8.0, 37°C
0.108
(2R,3S)-3-isopropylmalate
mutant enzyme Y139A, at pH 7.6 and 20°C
0.233
(2R,3S)-3-isopropylmalate
mutant enzyme Y181F, at pH 7.5 and 25°C
0.3
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/V238M/R310M, pH 8.0, 37°C
0.4
(2R,3S)-3-isopropylmalate
mutant R85V/Y86A, pH 8.0, 37°C
0.433
(2R,3S)-3-isopropylmalate
mutant enzyme D245A, at pH 7.6 and 20°C
0.47
(2R,3S)-3-isopropylmalate
mutant enzyme L132A, at pH 7.5 and 25°C
0.55
(2R,3S)-3-isopropylmalate
mutant enzyme N102A, at pH 7.6 and 20°C
0.583
(2R,3S)-3-isopropylmalate
mutant enzyme Y181H, at pH 7.5 and 25°C
0.6
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M, pH 8.0, 37°C
0.62
(2R,3S)-3-isopropylmalate
mutant L133F, pH not specified in the publication, temperature not specified in the publication
0.622
(2R,3S)-3-isopropylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.73
(2R,3S)-3-isopropylmalate
mutant L134F, pH not specified in the publication, temperature not specified in the publication
1.2
(2R,3S)-3-isopropylmalate
-
acIPMDH-ML, pH 8.0, 25°C
1.6
(2R,3S)-3-isopropylmalate
mutant S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
1.62
(2R,3S)-3-isopropylmalate
mutant enzyme R174K, at pH 7.5 and 25°C
1.7
(2R,3S)-3-isopropylmalate
-
ancIPMDH-IQ, pH 8.0, 25°C
1.8
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/R310M, pH 8.0, 37°C
2
(2R,3S)-3-isopropylmalate
mutant enzyme V235A, at pH 7.5 and 25°C
2.36
(2R,3S)-3-isopropylmalate
-
pH 8.0, 40°C, wild-type enzyme
2.41
(2R,3S)-3-isopropylmalate
-
pH 8.0, 40°C, mutant enzyme C275T
2.9
(2R,3S)-3-isopropylmalate
mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
2.9
(2R,3S)-3-isopropylmalate
-
pH 7.6, 20°C, quenched flow experiment
3.1
(2R,3S)-3-isopropylmalate
-
pressure 250 MPa, 20°C, pH not specified in the publication
3.1
(2R,3S)-3-isopropylmalate
mutant enzyme L133A, at pH 7.5 and 25°C
3.4
(2R,3S)-3-isopropylmalate
-
pH 7.6, 20°C, stopped flow experiment
3.83
(2R,3S)-3-isopropylmalate
mutant F137L, pH not specified in the publication, temperature not specified in the publication
3.97
(2R,3S)-3-isopropylmalate
wild type enzyme, in the presence of K+, at pH 7.6 and 20°C
4.3
(2R,3S)-3-isopropylmalate
-
acIPMDH-ML, pH 8.0, 40°C
4.57
(2R,3S)-3-isopropylmalate
wild type enzyme, at pH 7.5 and 25°C
4.6
(2R,3S)-3-isopropylmalate
-
ancIPMDH-IQ, pH 8.0, 40°C
5.1
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
5.7
(2R,3S)-3-isopropylmalate
wild-type (2R,3S)-3-isopropylmalate dehydrogenase, pH 8.0, 37°C
5.8
(2R,3S)-3-isopropylmalate
-
pressure 200 MPa, 20°C, pH not specified in the publication
6.22
(2R,3S)-3-isopropylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
7.2
(2R,3S)-3-isopropylmalate
-
pH 8.0, 40°C, mutant enzyme A31G/G43A/A709G
7.6
(2R,3S)-3-isopropylmalate
-
pressure 100 MPa, 20°C, pH not specified in the publication
8.4
(2R,3S)-3-isopropylmalate
-
pressure 150 MPa, 20°C, pH not specified in the publication
8.5
(2R,3S)-3-isopropylmalate
at pH 8.0 and 60°C
9.05
(2R,3S)-3-isopropylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
9.6
(2R,3S)-3-isopropylmalate
-
mutant enzyme I268A, at pH 7.6 and 25°C
10
(2R,3S)-3-isopropylmalate
pressure 250 MPa, 20°C, pH not specified in the publication
10.7
(2R,3S)-3-isopropylmalate
-
pH 8.0, 40°C, mutant enzyme G43A
12
(2R,3S)-3-isopropylmalate
-
pH 7.5, 37°C
13
(2R,3S)-3-isopropylmalate
pressure 200 MPa, 20°C, pH not specified in the publication
14
(2R,3S)-3-isopropylmalate
-
pressure 0.1 MPa, 20°C, pH not specified in the publication
14
(2R,3S)-3-isopropylmalate
pressure 100 MPa, 20°C, pH not specified in the publication
14
(2R,3S)-3-isopropylmalate
pressure 150 MPa, 20°C, pH not specified in the publication
14.8
(2R,3S)-3-isopropylmalate
-
mutant enzyme M106L, at pH 7.6 and 25°C
15
(2R,3S)-3-isopropylmalate
pressure 0.1 MPa, 20°C, pH not specified in the publication
15
(2R,3S)-3-isopropylmalate
-
pressure 50 MPa, 20°C, pH not specified in the publication
16.1
(2R,3S)-3-isopropylmalate
mutant enzyme A268I, at pH 7.6 and 25°C
16.4
(2R,3S)-3-isopropylmalate
-
wild type enzyme, at pH 7.6 and 25°C
16.7
(2R,3S)-3-isopropylmalate
mutant enzyme S266A, at pH 7.6 and 25°C
17
(2R,3S)-3-isopropylmalate
pressure 50 MPa, 20°C, pH not specified in the publication
17.4
(2R,3S)-3-isopropylmalate
wild type enzyme, at pH 7.6 and 25°C
17.7
(2R,3S)-3-isopropylmalate
-
pH 8.0, 40°C, mutant enzyme G376A
20.4
(2R,3S)-3-isopropylmalate
-
mutant enzyme A266S, at pH 7.6 and 25°C
22
(2R,3S)-3-isopropylmalate
-
acIPMDH-ML, pH 8.0, 70°C
22
(2R,3S)-3-isopropylmalate
-
ancIPMDH-IQ, pH 8.0, 70°C
28
(2R,3S)-3-isopropylmalate
-
-
40
(2R,3S)-3-isopropylmalate
wild type enzyme, at pH 7.6 and 20°C
44.7
(2R,3S)-3-isopropylmalate
-
pH 8.0, 70°C, mutant enzyme C275T
45.8
(2R,3S)-3-isopropylmalate
-
pH 8.0, 70°C, wild-type enzyme
48.1
(2R,3S)-3-isopropylmalate
mutant enzyme L106M, at pH 7.6 and 25°C
50.1
(2R,3S)-3-isopropylmalate
-
pH 8.0, 70°C, mutant enzyme A31G/G43A/A709G
63.6
(2R,3S)-3-isopropylmalate
-
pH 8.0, 70°C, mutant enzyme G43A
100
(2R,3S)-3-isopropylmalate
-
pH 8.0, 70°C, mutant enzyme G376A
100
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172D
107
(2R,3S)-3-isopropylmalate
-
55°C, wild-type enzyme
111
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172Q
117
(2R,3S)-3-isopropylmalate
-
55°C, mutant enzyme A172E and A172N
163
(2R,3S)-3-isopropylmalate
60°C, pH 7.6, wild-type enzyme
220
(2R,3S)-3-isopropylmalate
60°C, pH 7.6, mutant enzyme A172V
0.016
3-(2'-methylthio)ethylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0167
3-(2'-methylthio)ethylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.033
3-(2'-methylthio)ethylmalate
mutant F137L, pH not specified in the publication, temperature not specified in the publication
0.27
3-(2'-methylthio)ethylmalate
mutant L134F, pH not specified in the publication, temperature not specified in the publication
0.367
3-(2'-methylthio)ethylmalate
mutant L133F, pH not specified in the publication, temperature not specified in the publication
0.85
3-(2'-methylthio)ethylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
3.8
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant F3S/S232G
6
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant R284G
6.8
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant F3S
6.9
3-isopropylmalate
pH 7.5, 70°C, recombinant wild-type enzyme
7.5
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant L288P
7.8
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant F3S/L288P
8.3
3-isopropylmalate
-
mutant Glu253Trp
9.5
3-isopropylmalate
-
mutant Glu253Ala
9.9
3-isopropylmalate
-
mutant Glu253Gln
12.4
3-isopropylmalate
-
mutant Glu253Val
13.7
3-isopropylmalate
-
mutant Glu253Leu
14.9
3-isopropylmalate
-
wild-type
0.09
isopropylmalate
-
pH 7.3, 21°C, reaction with NADP+, mutant enzyme S226R/D278K/I279Y
0.15
isopropylmalate
-
pH 7.3, 21°C, reaction with NAD+, wild-type enzyme
0.2
isopropylmalate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87G
0.21
isopropylmalate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87Q
0.24
isopropylmalate
-
pH 7.3, 21°C, reaction with NAD+, wild-type enzyme
0.26
isopropylmalate
-
pH 7.3, 21°C, reaction with NADP+, wild-type enzyme
0.48
isopropylmalate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme S226R
0.88
isopropylmalate
-
pH 7.3, 21°C, reaction with NADP+, mutant enzyme S226R
1.66
isopropylmalate
-
pH 7.3, 21°C, reaction with NADP+, wild-type enzyme
1.91
isopropylmalate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme S226R/D278K/I279Y
8
isopropylmalate
-
pH 7.6, 70°C
19
isopropylmalate
-
pH 7.6, 40°C
69
isopropylmalate
-
pH 7.6, 40°C
0.19
malate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87Q
0.26
malate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87G
4.69
malate
-
pH 7.3, 21°C, reaction with NADP+, wild-type enzyme
10.6
malate
-
pH 7.3, 21°C, reaction with NAD+, wild-type enzyme
0.15
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme
0.19
NAD+
-
pH 7.3, 21°C, reaction with tartrate, wild-type enzyme or reaction with malate, mutant enzyme E87Q
0.2
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme E87G
0.21
NAD+
-
pH 7.3, 21°C, reaction with tartrate, mutant enzyme E87G
0.21
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme E87Q
0.24
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme
0.26
NAD+
-
pH 7.3, 21°C, reaction with malate, mutant enzyme E87G or reaction with tartrate, mutant enzyme E87Q
0.37
NAD+
pH 8.0, 25°C, wild-type enzyme
0.48
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme S226R
1.2
NAD+
-
pH 8.0, 40°C, mutant V126A
1.2
NAD+
-
acIPMDH-ML, pH 8.0, 25°C
1.5
NAD+
-
pH 8.0, 40°C, mutant V126S
1.7
NAD+
-
pH 8.0, 40°C, mutant V126G
1.7
NAD+
-
ancIPMDH-IQ, pH 8.0, 25°C
1.9
NAD+
-
pH 8.0, 40°C, mutant V126T
1.91
NAD+
-
pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme S226R/D278K/I279Y
2 - 3.7
NAD+
-
mutant enzyme A266S, at pH 7.6 and 25°C
2.36
NAD+
-
pH 8.0, 40°C, wild-type enzyme
2.4
NAD+
pH 8.0, 40°C, wild-type enzyme
2.4
NAD+
-
pH 8.0, 40°C, wild-type
2.41
NAD+
-
pH 8.0, 40°C, mutant enzyme C275T
3.5
NAD+
-
pH 8.0, 40°C, mutant V126E
4.3
NAD+
-
acIPMDH-ML, pH 8.0, 40°C
4.6
NAD+
-
ancIPMDH-IQ, pH 8.0, 40°C
6
NAD+
-
pH 8.0, 40°C, mutant V126I
7.2
NAD+
-
pH 8.0, 40°C, mutant enzyme A31G/G43A/A709G
8
NAD+
-
pH 7.6, 70°C, reaction with isopropylmalate
8.5
NAD+
-
pH 8.0, 40°C, mutant V126L
9
NAD+
-
pH 8.0, 60°C, mutant V126A
10
NAD+
-
pH 8.0, 60°C, V126G
10.2
NAD+
pH 7.6, 70°C, recombinant mutant V181T
10.3
NAD+
-
mutant enzyme I268A, at pH 7.6 and 25°C
10.6
NAD+
-
pH 7.3, 21°C, reaction with malate, wild-type enzyme
10.7
NAD+
-
pH 8.0, 40°C, mutant enzyme G43A
11
NAD+
-
pH 8.0, 40°C, mutant V126F
11.2
NAD+
pH 7.6, 70°C, recombinant mutant D184H
13
NAD+
-
pH 8.0, 60°C, mutant V126S
13.2
NAD+
pH 7.6, 70°C, recombinant mutant V181T/P324T/A335E
13.4
NAD+
pH 7.6, 70°C, recombinant wild-type enzyme
13.8
NAD+
pH 7.6, 70°C, recombinant mutant P324T
14.6
NAD+
pH 7.6, 70°C, recombinant mutant P56E
15
NAD+
-
pH 8.0, 60°C, mutant V126T
15
NAD+
pH 7.6, 70°C, recombinant mutants F53L and V61I
15.2
NAD+
-
mutant enzyme M106L, at pH 7.6 and 25°C
15.6
NAD+
mutant enzyme S266A, at pH 7.6 and 25°C
17.1
NAD+
wild type enzyme, at pH 7.6 and 25°C
17.4
NAD+
mutant enzyme A268I, at pH 7.6 and 25°C
17.7
NAD+
-
pH 8.0, 40°C, mutant enzyme G376A
17.7
NAD+
pH 7.6, 70°C, recombinant mutant R58L
18
NAD+
-
pH 8.0, 40°C, mutant V126M
18.2
NAD+
pH 7.6, 70°C, recombinant mutants S261N and A335E
18.7
NAD+
-
wild type enzyme, at pH 7.6 and 25°C
19
NAD+
-
pH 7.6, 40°C, reaction with isopropylmalate
20
NAD+
-
pH 8.0, 60°C, wild-type
21
NAD+
-
pH 8.0, 60°C, mutant V126E
21.3
NAD+
pH 7.6, 70°C, recombinant mutant H197K
22
NAD+
-
acIPMDH-ML, pH 8.0, 70°C
22
NAD+
-
ancIPMDH-IQ, pH 8.0, 70°C
25.2
NAD+
pH 7.6, 70°C, recombinant mutant L134N/V181T/P324T/A335E
29.9
NAD+
pH 7.6, 70°C, recombinant mutant L134N
30.5
NAD+
-
pH 8.0, 60°C, mutant V126I
42
NAD+
-
pH 8.0, 60°C, mutant V126F
44.5
NAD+
-
pH 8.0, 60°C, mutant V126L
44.7
NAD+
-
pH 8.0, 70°C, mutant enzyme C275T
45.8
NAD+
-
pH 8.0, 70°C, wild-type enzyme
50.1
NAD+
-
pH 8.0, 70°C, mutant enzyme A31G/G43A/A709G
50.5
NAD+
mutant enzyme L106M, at pH 7.6 and 25°C
54
NAD+
-
pH 8.0, 60°C, mutant V126M
63.6
NAD+
-
pH 8.0, 70°C, mutant enzyme G43A
69
NAD+
-
pH 7.6, 40°C, reaction with isopropylmalate
79
NAD+
pH 8.0, 70°C, wild-type enzyme
100
NAD+
-
pH 8.0, 70°C, mutant enzyme G376A
100
NAD+
-
55°C, mutant enzyme A172D
107
NAD+
-
55°C, wild-type enzyme
111
NAD+
-
55°C, mutant enzyme A172Q
117
NAD+
-
55°C, mutant enzyme A172E and A172N
163
NAD+
60°C, pH 7.6, wild-type enzyme
220
NAD+
60°C, pH 7.6, pH 7.6, mutant enzyme A172V
0.09
NADP+
-
pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme S226R/D278K/I279Y
0.1
NADP+
-
pH 7.3, 21°C, reaction with tartrate, wild-type enzyme
0.26
NADP+
-
pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme
0.88
NADP+
-
pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme S226R
1.66
NADP+
-
pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme
4.69
NADP+
-
pH 7.3, 21°C, reaction with malate, wild-type enzyme
0.1
Tartrate
-
pH 7.3, 21°C, reaction with NADP+, wild-type enzyme
0.19
Tartrate
-
pH 7.3, 21°C, reaction with NAD+, wild-type enzyme
0.21
Tartrate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87G
0.26
Tartrate
-
pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87Q
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0.009 - 1700
(2R,3S)-3-isopropylmalate
0.038 - 18.77
3-(2'-methylthio)ethylmalate
1.36
D-malate
-
pH 7.5, 37°C
440
homoisocitrate
at pH 8.0 and 60°C
0.009
(2R,3S)-3-isopropylmalate
mutant enzyme R136K, at pH 7.5 and 25°C
0.109
(2R,3S)-3-isopropylmalate
mutant enzyme D292N, at pH 7.5 and 25°C
0.16
(2R,3S)-3-isopropylmalate
mutant R85V/Y86A, pH 8.0, 37°C
0.18
(2R,3S)-3-isopropylmalate
wild-type (2R,3S)-3-isopropylmalate dehydrogenase, pH 8.0, 37°C
0.192
(2R,3S)-3-isopropylmalate
mutant enzyme R146K, at pH 7.5 and 25°C
0.33
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/V238M/R310M, pH 8.0, 37°C
0.4
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M, pH 8.0, 37°C
0.429
(2R,3S)-3-isopropylmalate
mutant enzyme R146A, at pH 7.5 and 25°C
0.49
(2R,3S)-3-isopropylmalate
mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
0.75
(2R,3S)-3-isopropylmalate
wild-type HICDH, pH 8.0, 37°C
0.94
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/R310M, pH 8.0, 37°C
1.6
(2R,3S)-3-isopropylmalate
mutant S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
1.92
(2R,3S)-3-isopropylmalate
mutant enzyme Y181A, at pH 7.5 and 25°C
2.14
(2R,3S)-3-isopropylmalate
mutant enzyme R174K, at pH 7.5 and 25°C
5.4
(2R,3S)-3-isopropylmalate
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
19.29
(2R,3S)-3-isopropylmalate
mutant enzyme L132A, at pH 7.5 and 25°C
20.3
(2R,3S)-3-isopropylmalate
mutant L133F, pH not specified in the publication, temperature not specified in the publication
24.47
(2R,3S)-3-isopropylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
24.83
(2R,3S)-3-isopropylmalate
mutant enzyme L133A, at pH 7.5 and 25°C
25.7
(2R,3S)-3-isopropylmalate
mutant L134F, pH not specified in the publication, temperature not specified in the publication
32.32
(2R,3S)-3-isopropylmalate
mutant enzyme Y181F, at pH 7.5 and 25°C
34
(2R,3S)-3-isopropylmalate
-
pressure 250 MPa, 20°C, pH not specified in the publication
91.21
(2R,3S)-3-isopropylmalate
mutant enzyme Y181H, at pH 7.5 and 25°C
93
(2R,3S)-3-isopropylmalate
pressure 250 MPa, 20°C, pH not specified in the publication
110
(2R,3S)-3-isopropylmalate
-
pressure 200 MPa, 20°C, pH not specified in the publication
160
(2R,3S)-3-isopropylmalate
-
pressure 150 MPa, 20°C, pH not specified in the publication
180.3
(2R,3S)-3-isopropylmalate
mutant enzyme V235A, at pH 7.5 and 25°C
270
(2R,3S)-3-isopropylmalate
-
mutant enzyme I268A, at pH 7.6 and 25°C
336.3
(2R,3S)-3-isopropylmalate
mutant F137L, pH not specified in the publication, temperature not specified in the publication
340
(2R,3S)-3-isopropylmalate
pressure 200 MPa, 20°C, pH not specified in the publication
400
(2R,3S)-3-isopropylmalate
pressure 50 MPa, 20°C, pH not specified in the publication
440
(2R,3S)-3-isopropylmalate
pressure 150 MPa, 20°C, pH not specified in the publication
560
(2R,3S)-3-isopropylmalate
-
pressure 50 MPa, 20°C, pH not specified in the publication
570
(2R,3S)-3-isopropylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
590
(2R,3S)-3-isopropylmalate
-
mutant enzyme A266S, at pH 7.6 and 25°C
600
(2R,3S)-3-isopropylmalate
pressure 0.1 MPa, 20°C, pH not specified in the publication
620
(2R,3S)-3-isopropylmalate
-
mutant enzyme M106L, at pH 7.6 and 25°C
700
(2R,3S)-3-isopropylmalate
pressure 100 MPa, 20°C, pH not specified in the publication
870
(2R,3S)-3-isopropylmalate
-
pressure 100 MPa, 20°C, pH not specified in the publication
930
(2R,3S)-3-isopropylmalate
-
pressure 0.1 MPa, 20°C, pH not specified in the publication
983.7
(2R,3S)-3-isopropylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
1150
(2R,3S)-3-isopropylmalate
-
pH 7.5, 37°C
1303
(2R,3S)-3-isopropylmalate
wild type enzyme, at pH 7.5 and 25°C
1350
(2R,3S)-3-isopropylmalate
-
wild type enzyme, at pH 7.6 and 25°C
1700
(2R,3S)-3-isopropylmalate
at pH 8.0 and 60°C
0.038
3-(2'-methylthio)ethylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.1
3-(2'-methylthio)ethylmalate
mutant F137L, pH not specified in the publication, temperature not specified in the publication
0.33
3-(2'-methylthio)ethylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
2.59
3-(2'-methylthio)ethylmalate
mutant L134F, pH not specified in the publication, temperature not specified in the publication
4.76
3-(2'-methylthio)ethylmalate
mutant L133F, pH not specified in the publication, temperature not specified in the publication
18.77
3-(2'-methylthio)ethylmalate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.12
NAD+
wild-type (2R,3S)-3-isopropylmalate dehydrogenase, pH 8.0, 37°C
0.23
NAD+
mutant R85V/Y86A, pH 8.0, 37°C
0.25
NAD+
mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
0.33
NAD+
mutant E57V/S72I/R85M/Y86A/M208T/V238M/R310M, pH 8.0, 37°C
0.38
NAD+
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M, pH 8.0, 37°C
0.41
NAD+
wild-type HICDH, pH 8.0, 37°C
1.1
NAD+
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/R310M , pH 8.0, 37°C
1.4
NAD+
mutant S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
4.2
NAD+
mutant E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M, pH 8.0, 37°C
60
NAD+
-
mutant enzyme I268A, at pH 7.6 and 25°C
100
NAD+
-
mutant enzyme A266S, at pH 7.6 and 25°C
180
NAD+
-
wild type enzyme, at pH 7.6 and 25°C
190
NAD+
-
mutant enzyme M106L, at pH 7.6 and 25°C
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D292N
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
F137L
mutation to corresponding residue of isoform IMPDH2, reduces activity toward 3-(2'-methylthio)-ethylmalate by 200fold, but enhances catalytic efficiency with 3-isopropylmalate to levels observed with isoform IPMDH2
L132A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
L133A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
L133F
mutation to corresponding residue of isoform IMPDH1, enhances catalytic efficiency with 3-(2'-methylthio)ethylmalate about100fold and reduces activity for 3-isopropylmalate
L134F
mutation to corresponding residue of isoform IMPDH1, reduces activity toward 3-(2'-methylthio)-ethylmalate, but enhances catalytic efficiency with 3-isopropylmalate
R136K
the mutant shows very strongly reduced catalytic efficiency compared to the wild type enzyme
R146A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R146K
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R174K
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
V235A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y181A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Y181F
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y181H
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E253A
-
specific activity: 4.7 unit/mg, Km: 0.016 mM (3-isopropylmalate), 0.246 mM (NAD), kcat: 14.9/sec
E253F
-
specific activity: 7.6 unit/mg
E253G
-
specific activity: 5.9 unit/mg
E253I
-
specific activity: 7.4 unit/mg
E253K
-
when a lysine is the position 253 the protein dissociates
E253L
-
specific activity: 7.6 unit/mg, Km: 0.0122 mM (3-isopropylmalate), 0.474 mM (NAD), kcat: 13.7/sec
E253Q
-
specific activity: 7 unit/mg, Km: 0.0189 mM (3-isopropylmalate), 0.273 mM (NAD), kcat: 9.9/sec. this mutant is more thermostable than the other mutants
E253V
-
specific activity: 9 unit/mg, Km: 0.0244 mM (3-isopropylmalate), 0.171 mM (NAD), kcat: 12.4/sec
E253W
-
specific activity: 5.2 unit/mg, Km: 0.0254 mM (3-isopropylmalate), 0.244 mM (NAD), kcat: 8.3/sec
M256A
-
mutation increases thermostability by 6°C in comparison to wild-type
M256F
-
mutation decreases thermostability by 4°C in comparison to wild-type
M256V
-
mutation increases thermostability by 2°C in comparison to wild-type
D236R/D289K/I290Y/A296V/G337Y
-
engineering of the enzyme by site-directed mutagenesis in the cofactor binding pocket to utilize NADP+ as cofactor instead of NAD+, specificity change of factor 20000, modified cofactor binding structure, the mutant shows the same specificity for NADP+ as the wild-type enzyme for NAD+, overview
A266S
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I268A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
M106L
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
A266S
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
I268A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
M106L
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
A268I
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
L106M
the mutant shows increased catalytic efficiency compared to the wild type enzyme
S266A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
A268I
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
L106M
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
-
S266A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
A259S/F261P
Tm-value of mutant enzyme is 1.1°C higher than Tm-value of wild-type enzyme
F145S
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
F3S
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
F3S/L288P
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme. The MA153 strain containing a doubly mutated leuB gene grows more rapidly than does Escherichia coli MA153 containing the wild-type leuB gene in leucine-free M9 minimal liquid medium
F3S/S232G
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme. The MA153 strain containing a doubly mutated leuB gene grows more rapidly than does Escherichia coli MA153 containing the wild-type leuB gene in leucine-free M9 minimal liquid medium
G154A
Tm-value of mutant enzyme is 1.9°C higher than Tm-value of wild-type enzyme
I68L/I142T/K335E
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
K152R
Tm-value of mutant enzyme is 0.4°C lower than Tm-value of wild-type enzyme
K152R/G154A
Tm-value of mutant enzyme is 1.2°C higher than Tm-value of wild-type enzyme
L288P
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
L328S
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
L336P
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
M91L/I95L
Tm-value of mutant enzyme is 3.2°C higher than Tm-value of wild-type enzyme
M91L/I95L/K152R/G154A/A259S/F261P/Y282L
Tm-value of mutant enzyme is 0.4°C higher than Tm-value of wild-type enzyme
R284G
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
Y282L
Tm-value of mutant enzyme is 0.3°C lower than Tm-value of wild-type enzyme
Y309H
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
G154A
-
Tm-value of mutant enzyme is 1.9°C higher than Tm-value of wild-type enzyme
-
K152R
-
Tm-value of mutant enzyme is 0.4°C lower than Tm-value of wild-type enzyme
-
K152R/G154A
-
Tm-value of mutant enzyme is 1.2°C higher than Tm-value of wild-type enzyme
-
M91L/I95L
-
Tm-value of mutant enzyme is 3.2°C higher than Tm-value of wild-type enzyme
-
M91L/I95L/K152R/G154A/A259S/F261P/Y282L
-
Tm-value of mutant enzyme is 0.4°C higher than Tm-value of wild-type enzyme
-
A172E
-
enhanced thermostability compared to wild-type enzyme
A172G
-
melting temperature is reduced by 0.3°C compared to wild-type enzyme, crystal structure is similar to that of the wild-type enzyme
A172I
-
melting temperature is increased by 2°C compared to wild-type enzyme
A172N
-
enhanced thermostability compared to wild-type enzyme
A172Q
-
enhanced thermostability compared to wild-type enzyme
A31G/G43A/A709G
-
optimum temperature is shifted to lower temperatures compared to wild-type enzyme, activity is less temperature dependent than that of the wild-type, resulting in higher activity at temperatures below 60°C, improved turnover-numbers at 40°Cm increase in Km-values, slight loss of thermal stability
C275T
-
similar pH-dependence to that of the wild-type enzyme, improved binding affinities for both D-3-isopropylmalate and NAD+ result in an improved catalytic efficiency, mutant enzyme retains thermal stability
D217A
the mutant retains 1.1% of the catalytic activity of the wild type enzyme
D241A
the mutant shows a drastic decrease in the kcat value (0.06% compared to that of the wild type enzyme)
D245A
the mutant retains 10.5% of the catalytic activity of the wild type enzyme
E57V/R85M/Y86A/M208T/F217Y/V238M/R310M
no (2R,3S)-3-isopropylmalate dehydrogenase activity detected
E57V/S72I/R85M/Y86A/F217Y/V238M/R310M
no (2R,3S)-3-isopropylmalate dehydrogenase activity detected
E57V/S72I/R85M/Y86A/M208T/F217Y/R310M
in comparison to mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M this mutant shows a significant decrease in kcat ((2R,3S)-3-isopropylmalate), alteration of Km value only moderate
E57V/S72I/R85M/Y86A/M208T/F217Y/V238M
in comparison to mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M this mutant shows a significant decrease in kcat ((2R,3S)-3-isopropylmalate), alteration of Km value only moderate
E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M
in comparison to mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M this mutant shows a larger kcat ((2R,3S)-3-isopropylmalate) and a larger Km((2R,3S)-3-isopropylmalate) or (NAD+) temperatures giving half of the initial activity is 87.8 °C
E57V/S72I/R85M/Y86A/M208T/V238M/R310M
in comparison to mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M this mutant shows a significant decrease in kcat ((2R,3S)-3-isopropylmalate), alteration of Km value only moderate
E57V/S72I/R85V/Y86A/M208T/F217Y/V238M/R310M
no (2R,3S)-3-isopropylmalate dehydrogenase activity detected
E87G
-
mutation does not affect the dissociation constant from the binary complex, but does greatly increase the KM-values
E87Q
-
mutation does not affect the dissociation constant from the binary complex, but does greatly increase the KM-values
G240A
-
decreased thermostability
G376A
-
optimum temperature is shifted to lower temperatures compared to wild-type enzyme, activity is less temperature dependent than that of the wild-type, resulting in higher activity at temperatures below 60°C, improved turnover-numbers at 40°C, increase in Km-values, mutant enzyme retains thermal stability
G43A
-
optimum temperature is shifted to lower temperatures compared to wild-type enzyme, activity is less temperature dependent than that of the wild-type, resulting in higher activity at temperatures below 60°C, improved turnover-numbers at 40°C, increase ion Km-values, slight loss of thermal stability
H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M
TtHICDH variant with considerably higher IPMDH activity than double mutant R85V/Y86A, Km ((2R,3S)-3-isopropylmalate) or (NAD+) lower than wild-type HICDH but still considerably higher than wild-type (2R,3S)-3-isopropylmalate dehydrogenase, kcat ((2R,3S)-3-isopropylmalate) much higher than wild-type HICDH but still considerably lower than wild-type (2R,3S)-3-isopropylmalate dehydrogenase, temperatures giving half of the initial activity is 79.9 °C, crystal structure determined at 2.4 A, mutant is a homotetramer
K185A
the mutant shows a drastic decrease in the kcat value (0.06% compared to that of the wild type enzyme)
L134N/V181T/P324T/A335E
site-directed mutagenesis, exchange of residues for those of ancestral mutants, the mutant shows increased thermal stability compared to the wild-type enzyme, the mutant shows increased thermal stability compared to the wild-type enzyme
L204F
-
higher thermostability compared to wild-type enzyme, denaturation rates at 68°C and 70°C are slower
L246E/V249M
-
decreased thermostability
N102A
the mutant retains 13% of the catalytic activity of the wild type enzyme
R85V/Y86A
TtHICDH variant with high IPMDH activity, Km ((2R,3S)-3-isopropylmalate) or (NAD+) lower than wild-type HICDH but still considerably higher than wild-type (2R,3S)-3-isopropylmalate dehydrogenase, kcat ((2R,3S)-3-isopropylmalate) higher than wild-type HICDH but still considerably lower than wild-type (2R,3S)-3-isopropylmalate dehydrogenase, temperatures giving half of the initial activity is 92.5 °C
S226R
-
Km-value for NADP+ is about 40% compared to wild-type enzyme, Km-value for NAD+ is 2.6fold higher compared to wild-type enzyme
S226R/D278K/I279Y
-
Km-value for NADP+ is about 0.8% compared to wild-type enzyme, Km-value for NAD+ is 153fold higher compared to wild-type enzyme
S72I/R85M/Y86A/M208T/F217Y/V238M/R310M
in comparison to mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M this mutant shows a significant decrease in kcat ((2R,3S)-3-isopropylmalate), alteration of Km value only moderate
T16V
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
V126A
-
the mutation decreases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126E
-
the mutation increases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126F
-
the mutation increases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126G
-
the mutation decreases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126I
-
the mutation increases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126L
-
the mutation increases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126M
-
the mutation increases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126S
-
the mutation decreases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V126T
-
the mutation decreases the KM value of DL-3-isopropylmalate at 60°C in comparison to wild-type
V181T/P324T/A335E
site-directed mutagenesis, exchange of residues for those of ancestral mutants, the mutant highly shows increased thermal stability compared to the wild-type enzyme, the mutant shows decreased thermal stability compared to the wild-type enzyme
W152F
site-directed mutagenesis, the W152F mutation causes a significant decrease in the amplitude of only the slow part of refolding, without influencing the amplitude of the burst part, the mutant shows an altered tertiary structure compared to the wild-type enzyme conformation
W152F/W195F
site-directed mutagenesis, the W152F mutation causes a significant decrease in the amplitude of only the slow part of refolding, without influencing the amplitude of the burst part, the mutant shows an altered tertiary structure compared to the wild-type enzyme conformation
W77F/W152F
site-directed mutagenesis, the W152F mutation causes a significant decrease in the amplitude of only the slow part of refolding, without influencing the amplitude of the burst part, the mutant shows an altered tertiary structure compared to the wild-type enzyme conformation
Y139A
the mutant retains 2.9% of the catalytic activity of the wild type enzyme
A172L
-
the mutant shows improved thermal stability compared to the wild type enzyme
-
E270A
-
the mutant exhibits largely reduced (about 1%) catalytic activity and negligible activation by K+ compared to the wild type enzyme
-
A172D
-
enhanced thermostability compared to wild-type enzyme
A172D
-
melting temperature is reduced by 2.7°C compared to wild-type enzyme
A172F
-
mutation causes rearrangement in domain structure, which leads to a higher thermostability compared to wild-type enzyme
A172F
-
melting temperature is increased by 1.8°C compared to wild-type enzyme
A172L
-
mutation causes rearrangement in domain structure, which leads to a higher thermostability compared to wild-type enzyme
A172L
-
melting temperature is increased by 3°C compared to wild-type enzyme
A172L
the mutant shows improved thermal stability compared to the wild type enzyme
A172V
-
melting temperature is increased by 1°C compared to wild-type enzyme, crystal structure is similar to that of the wild-type enzyme
A172V
mutation improves thermal stability, without significantly changing its catalytic properties
A335E
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
A335E
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased thermal stability compared to the wild-type enzyme, the mutant shows increased thermal stability compared to the wild-type enzyme
D184H
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
D184H
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased catalytic efficiency with NAD+ compared to the wild-type enzyme
E270A
the mutant exhibits largely reduced (about 1%) catalytic activity and negligible activation by K+ compared to the wild type enzyme
E270A
the mutation leads to a significant increase in the Km value for NAD+ compared to the wild type enzyme
F53L
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows decreased thermal stability compared to the wild-type enzyme
F53L
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased catalytic efficiency with NAD+ compared to the wild-type enzyme
H179K
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows decreased thermal stability compared to the wild-type enzyme
H179K
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased catalytic efficiency with NAD+ compared to the wild-type enzyme
L134N
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
L134N
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased thermal stability compared to the wild-type enzyme, the mutant shows highly increased thermal stability compared to the wild-type enzyme
P324T
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
P324T
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased thermal stability compared to the wild-type enzyme, the mutant shows increased thermal stability compared to the wild-type enzyme
P56E
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
P56E
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased catalytic efficiency with NAD+ compared to the wild-type enzyme
R58L
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows decreased thermal stability compared to the wild-type enzyme
R58L
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows increased catalytic efficiency with NAD+ compared to the wild-type enzyme
S261N
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows decreased thermal stability compared to the wild-type enzyme
S261N
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows slightly increased catalytic efficiency with NAD+ compared to the wild-type enzyme
V181T
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows increased thermal stability compared to the wild-type enzyme
V181T
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows decreased thermal stability compared to the wild-type enzyme, the mutant shows decreased thermal stability compared to the wild-type enzyme
V61I
site-directed mutagenesis, exchange of a cofactor binding residue to the residue of the ancestral mutant, the mutant shows decreased thermal stability compared to the wild-type enzyme
V61I
site-directed mutagenesis, exchange of a residue for that of ancestral mutants, the mutant shows slightly increased catalytic efficiency with NAD+ compared to the wild-type enzyme
additional information
-
results show that, for residues with non-polar side chains, when positioned at residue 253, the thermostabilities of their corresponding mutants correlate positively with the relative hydrophobicities of the side chains
additional information
-
two ancestral sequences of 3-isopropylmalate dehydrogenase are designed by an ancestral sequence reconstruction technique based on a phylogenetic analysis of extant homologous amino acid sequences. Genes encoding the designed sequences are artificially synthesized and expressed in Escherichia coli. The ancestral sequence reconstruction can produce a thermally stable enzyme with catalytic properties adapted to low-temperature reactions
additional information
designing thermostable 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree and ancestral mutant sequences, overview
additional information
-
designing thermostable 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree and ancestral mutant sequences, overview
additional information
one or a combination of amino acid(s) in 3-isopropylmalate dehydrogenase is/are substituted by a residue(s) found in the Escherichia coli enzyme at the same position(s). The best mutant, which contains three amino acid substitutions, shows a 17fold higher specific activity at 25°C compared to the original wild-type enzyme while retaining high thermal stability. The kinetic and thermodynamic parameters of the mutant show similar patterns along the reaction coordinate to those of the mesophilic enzyme
additional information
-
one or a combination of amino acid(s) in 3-isopropylmalate dehydrogenase is/are substituted by a residue(s) found in the Escherichia coli enzyme at the same position(s). The best mutant, which contains three amino acid substitutions, shows a 17fold higher specific activity at 25°C compared to the original wild-type enzyme while retaining high thermal stability. The kinetic and thermodynamic parameters of the mutant show similar patterns along the reaction coordinate to those of the mesophilic enzyme
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