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(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + NADH + H+ + CO2
(2R,3S)-3-(2-hydroxyethyl)malate + NAD+
?
(2R,3S)-3-(3-aminopropyl)malate + NAD+
?
(2R,3S)-3-(3-hydroxypropyl)malate + NAD+
?
(2R,3S)-3-(4-hydroxybutyl)malate + NAD+
?
(2R,3S)-3-(4-pentenyl)malic acid + NAD+
?
(2R,3S)-3-allylmalic acid + NAD+
?
(2R,3S)-3-propylmalic acid + NAD+
?
1-hydroxy-1,2,3-propanetricarboxylate + NAD+
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
2(R),3(S)-homoisocitrate + NAD+
alpha-ketoadipate + NADH + CO2 + H+
-
with homoisocitrate as the substrate, no primary deuterium isotope effect is observed, and a small 13C kinetic isotope effect indicates that the decarboxylation step contributes only slightly to rate limitation
-
-
?
3-carboxy-2-hydroxyadipate + NAD+
2-oxoadipate + CO2 + NADH
3-isopropylmalate + NAD+
?
3-isopropylmalate + NAD+
alpha-ketoisocaproate + NADH + H+ + CO2
homoisocitrate + NAD+
2-oxoadipate + CO2 + NADH + H+
homoisocitrate + NAD+
alpha-ketoadipate + NADH + CO2
-
-
-
-
r
homoisocitrate + NAD+
alpha-ketoadipate + NADH + CO2 + H+
-
-
-
-
r
homoisocitrate + NAD+
alpha-ketoadipate + NADH + H+ + CO2
homoisocitrate + NADP+
alpha-ketoadipate + NADPH + H+ + CO2
-
-
-
-
r
isocitrate + NAD+
? + NADH + H+
-
low activity
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
isopropylmalate + NAD+
?
-
-
-
-
?
threo-D-isocitric acid + NAD+
?
-
with isocitrate as the substrate, primary deuterium and 13C isotope effects indicate that hydride transfer and decarboxylation steps contribute to rate limitation, and that the decarboxylation step is the more rate-limiting of the two. The multiple-substrate deuterium/13C isotope effects suggest a stepwise mechanism with hydride transfer preceding decarboxylation
-
-
?
trisodium (2S,3R)-2-(carboxylatomethoxy)-3-hydroxybutanedioate + NAD+
? + NADH + CO2
-
-
-
-
?
trisodium (2S,3R)-2-[(carboxylatomethyl)amino]-3-hydroxybutanedioate + NAD+
? + NADH + CO2
-
-
-
-
?
additional information
?
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
strict specificity for homoisocitrate
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
strict specificity for homoisocitrate, the enzyme selectively binds the Mg(II):homoisocitrate complex
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
strict specificity for homoisocitrate
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
strict specificity for homoisocitrate, the enzyme selectively binds the Mg(II):homoisocitrate complex
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
i.e. (2R,3S)-homoisocitrate
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + NADH + H+ + CO2
-
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + NADH + H+ + CO2
-
homoisocitrate dehydrogenase catalyzes the Mg2+- and K+-dependent oxidative decarboxylation of homoisocitrate to alpha-ketoadipate using NAD as the oxidant, it utilizes a Lys-Tyr pair to catalyze the acid-base chemistry of the reaction, the active site Lys-Tyr pair consists of lysine 206 and tyrosine 150
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + NADH + H+ + CO2
-
substitution of potassium acetate for KCl changes the kinetic mechanism of HIcDH from a steady state random to a fully ordered mechanism with the binding of Mg-HIc followed by K+ and NAD+
-
-
?
(2R,3S)-3-(2-hydroxyethyl)malate + NAD+
?
-
-
-
-
?
(2R,3S)-3-(2-hydroxyethyl)malate + NAD+
?
-
-
-
-
?
(2R,3S)-3-(3-aminopropyl)malate + NAD+
?
-
-
-
-
?
(2R,3S)-3-(3-aminopropyl)malate + NAD+
?
-
-
-
-
?
(2R,3S)-3-(3-hydroxypropyl)malate + NAD+
?
-
-
-
-
?
(2R,3S)-3-(3-hydroxypropyl)malate + NAD+
?
-
-
-
-
?
(2R,3S)-3-(4-hydroxybutyl)malate + NAD+
?
-
-
-
-
?
(2R,3S)-3-(4-hydroxybutyl)malate + NAD+
?
-
-
-
-
?
(2R,3S)-3-(4-pentenyl)malic acid + NAD+
?
-
-
-
-
?
(2R,3S)-3-(4-pentenyl)malic acid + NAD+
?
-
-
-
-
?
(2R,3S)-3-allylmalic acid + NAD+
?
-
-
-
-
?
(2R,3S)-3-allylmalic acid + NAD+
?
-
-
-
-
?
(2R,3S)-3-propylmalic acid + NAD+
?
-
-
-
-
?
(2R,3S)-3-propylmalic acid + NAD+
?
-
-
-
-
?
1-hydroxy-1,2,3-propanetricarboxylate + NAD+
?
-
more effective substrate than 1-hydroxy-1,2,4-butanetricarboxylate
-
-
?
1-hydroxy-1,2,3-propanetricarboxylate + NAD+
?
-
more effective substrate than 1-hydroxy-1,2,4-butanetricarboxylate
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
-
r
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
i.e. homoisocitrate
-
r
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
Saccharomycopsis lipolytica
-
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
Saccharomycopsis lipolytica
-
production of 2-oxoadipic acid, a precursor of lysine biosynthesis
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
alpha-aminoadipate pathway for biosynthesis of lysine
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
involved in lysine biosynthesis through alpha-aminoadipate
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
involved in lysine biosynthesis through alpha-aminoadipate
-
-
?
3-carboxy-2-hydroxyadipate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
-
?
3-carboxy-2-hydroxyadipate + NAD+
2-oxoadipate + CO2 + NADH
-
intermediate in lysine biosynthesis
-
-
?
3-isopropylmalate + NAD+
?
-
-
-
-
?
3-isopropylmalate + NAD+
?
-
-
-
?
3-isopropylmalate + NAD+
alpha-ketoisocaproate + NADH + H+ + CO2
-
the enzyme has low catalytic efficiency toward 3-isopropylmalate
-
-
?
3-isopropylmalate + NAD+
alpha-ketoisocaproate + NADH + H+ + CO2
-
the enzyme has low catalytic efficiency toward 3-isopropylmalate
-
-
?
3-vinylmalate + NAD+
?
-
-
-
-
?
3-vinylmalate + NAD+
?
-
-
-
-
?
D-malate + NAD+
?
-
weak activity
-
-
?
D-malate + NAD+
?
-
weak activity
-
-
?
ethylmalate + NAD+
?
-
-
-
-
?
ethylmalate + NAD+
?
-
-
-
-
?
homoisocitrate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
-
-
-
r
homoisocitrate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
-
-
r
homoisocitrate + NAD+
?
-
-
-
-
?
homoisocitrate + NAD+
?
-
1.5fold preferred to isocitrate
-
-
?
homoisocitrate + NAD+
?
-
-
-
?
homoisocitrate + NAD+
?
-
-
-
-
?
homoisocitrate + NAD+
?
-
-
-
-
?
homoisocitrate + NAD+
alpha-ketoadipate + NADH + H+ + CO2
-
highest activity
-
-
r
homoisocitrate + NAD+
alpha-ketoadipate + NADH + H+ + CO2
-
highest activity
-
-
r
isocitrate + NAD+
?
-
-
-
-
?
isocitrate + NAD+
?
-
-
-
?
isocitrate + NAD+
?
-
-
-
-
r
isocitrate + NAD+
?
-
20fold preferred to homoisocitrate
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
-
-
-
-
?
additional information
?
-
-
substrate docking study
-
-
?
additional information
?
-
-
substrate docking study
-
-
?
additional information
?
-
-
no activity with tartrate
-
-
?
additional information
?
-
-
retinol dehydrogenase 10 activity is critical for spatiotemporal synthesis of retinoic acid during embrogenesis
-
-
?
additional information
?
-
the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway
-
-
?
additional information
?
-
-
the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway
-
-
?
additional information
?
-
-
catalyzes keto-enol tautomerization of tritiated alpha-ketoadipate, not: ethanol, isocitrate, malate, glutamate
-
-
?
additional information
?
-
-
no activity with isocitrate, isopropylmalate, and tartrate
-
-
?
additional information
?
-
the wild-type enzyme with isocitrate as the substrate is about 200times slower than with homoisocitrate
-
-
?
additional information
?
-
-
the wild-type enzyme with isocitrate as the substrate is about 200times slower than with homoisocitrate
-
-
?
additional information
?
-
-
no activity with L-tartrate
-
-
-
additional information
?
-
-
no activity with L-tartrate
-
-
-
additional information
?
-
-
no activity with 3-isopropylmalate
-
-
?
additional information
?
-
-
substrate binding site structure, the substrate specificity is determined by residue Arg85, no activity with 3-isopropylmalate
-
-
?
additional information
?
-
-
no activity with 3-isopropylmalate
-
-
?
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(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + NADH + H+ + CO2
-
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
3-carboxy-2-hydroxyadipate + NAD+
2-oxoadipate + CO2 + NADH
-
intermediate in lysine biosynthesis
-
-
?
3-isopropylmalate + NAD+
?
-
-
-
?
homoisocitrate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
-
-
r
homoisocitrate + NAD+
?
-
-
-
?
isocitrate + NAD+
?
-
-
-
?
additional information
?
-
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
strict specificity for homoisocitrate
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
strict specificity for homoisocitrate
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
-
r
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
Saccharomycopsis lipolytica
-
production of 2-oxoadipic acid, a precursor of lysine biosynthesis
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
alpha-aminoadipate pathway for biosynthesis of lysine
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
involved in lysine biosynthesis through alpha-aminoadipate
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
involved in lysine biosynthesis through alpha-aminoadipate
-
-
?
additional information
?
-
-
retinol dehydrogenase 10 activity is critical for spatiotemporal synthesis of retinoic acid during embrogenesis
-
-
?
additional information
?
-
the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway
-
-
?
additional information
?
-
-
the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(2R,3S)-3-(p-carboxybenzyl)malate
-
-
(2S,3S)-(-)-3-methylmercaptomalic acid
-
(2S,3S)-thiahomoisocitrate
interacts through hydrogen bonding to Arg 118, Tyr 125 and Lys 171 in the active site, enzyme binding structure, overview
(R,E)-(3-carboxypropylidene)malic acid
(R,E)-(3-hydroxypropylidene)malic acid
(R,Z)-(3-carboxypropylidene)malic acid
(R,Z)-(3-hydroxypropylidene)malic acid
2-oxoadipate
Saccharomycopsis lipolytica
-
-
3-acetylpyridine adenine dinucleotide 3'-phosphate
3-AcPyrADP, competitive versus NAD+
3-carboxypropylidenemalate
-
-
3-[(carboxymethyl)sulfanyl]-2-oxopropanoic acid
-
-
acetate
-
slight inhibition
NAD+
-
substrate inhibition at high concentrations and in absence of K+, kinetics, overview
Oxaloglutarate
Saccharomycopsis lipolytica
-
-
thiahomoisocitrate
competitive versus homoisocitrate
trisodium (2S,3R)-2-(carboxylatomethoxy)-3-hydroxybutanedioate
-
-
trisodium (2S,3R)-2-[(carboxylatomethyl)amino]-3-hydroxybutanedioate
-
-
trisodium (2S,3S)-2-[(carboxylatomethyl)sulfanyl]-3-hydroxybutanedioate
-
-
(R,E)-(3-carboxypropylidene)malic acid
-
competitive
(R,E)-(3-carboxypropylidene)malic acid
-
competitive
(R,E)-(3-hydroxypropylidene)malic acid
-
competitive
(R,E)-(3-hydroxypropylidene)malic acid
-
competitive
(R,Z)-(3-carboxypropylidene)malic acid
-
competitive
(R,Z)-(3-carboxypropylidene)malic acid
-
competitive
(R,Z)-(3-hydroxypropylidene)malic acid
-
competitive
(R,Z)-(3-hydroxypropylidene)malic acid
-
competitive
homoisocitrate
-
1.2 mM
homoisocitrate
Saccharomycopsis lipolytica
-
-
additional information
-
inhibitor docking study, molecular modeling of CaHIcDH-inhibitor interaction, overview
-
additional information
-
synthesis and inhibition potency of substrate analogue inhibitors derived from 3-hydroxyalkylidene- and 3-carboxyalkylidenemalate derivatives, overview
-
additional information
-
synthesis and inhibition potency of substrate analogue inhibitors derived from 3-hydroxyalkylidene- and 3-carboxyalkylidenemalate derivatives, overview, no inhibition by 3-vinylmalate
-
additional information
-
product and dead-end inhibition studies in the absence of K+
-
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.
0.074 - 7.5
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
0.59 - 2.1
(2R,3S)-3-(2-hydroxyethyl)malate
0.51 - 0.58
(2R,3S)-3-(3-hydroxypropyl)malate
0.44 - 0.47
(2R,3S)-3-(4-hydroxybutyl)malate
2.7 - 9.4
(2R,3S)-3-(4-pentenyl)malic acid
0.41 - 2.8
(2R,3S)-3-allylmalic acid
0.29 - 0.78
(2R,3S)-3-propylmalic acid
0.4
1-hydroxy-1,2,3-propanetricarboxylate
-
purified enzyme, pH 8.0, 60°C
7.5
1-hydroxy-1,2,4-butanetricarboxylate
-
purified enzyme, pH 8.0, 60°C
1.4
3-carboxy-2-hydroxyadipate
-
-
0.05 - 1.33
3-isopropylmalate
0.083 - 3.4
3-vinylmalate
1.5
alpha-ketoadipate
-
-
16.3
CO2
-
reductive carboxylation of alpha-ketoadipate
4.5
D-malate
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.0042 - 3.2
homoisocitrate
1.4
homoisocitric acid
-
-
1.33
isopropylmalate
-
pH 7.8, 28°C, recombinant enzyme
7.6
NADP+
-
wild type enzyme, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.02
trisodium (2S,3R)-2-(carboxylatomethoxy)-3-hydroxybutanedioate
-
-
0.15
trisodium (2S,3R)-2-[(carboxylatomethyl)amino]-3-hydroxybutanedioate
-
-
additional information
additional information
-
0.074
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
-
recombinant His-tagged enzyme, pH 7.8, 20°C
0.45
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
-
native enzyme, pH 7.8, 20°C
7.5
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
pH 7.8, 60°C
0.59
(2R,3S)-3-(2-hydroxyethyl)malate
-
pH 7.8, 28°C, recombinant enzyme
2.1
(2R,3S)-3-(2-hydroxyethyl)malate
-
pH 7.8, 36°C, recombinant enzyme
0.51
(2R,3S)-3-(3-hydroxypropyl)malate
-
pH 7.8, 28°C, recombinant enzyme
0.58
(2R,3S)-3-(3-hydroxypropyl)malate
-
pH 7.8, 36°C, recombinant enzyme
0.44
(2R,3S)-3-(4-hydroxybutyl)malate
-
pH 7.8, 36°C, recombinant enzyme
0.47
(2R,3S)-3-(4-hydroxybutyl)malate
-
pH 7.8, 28°C, recombinant enzyme
2.7
(2R,3S)-3-(4-pentenyl)malic acid
-
pH 7.8, 28°C, recombinant enzyme
9.4
(2R,3S)-3-(4-pentenyl)malic acid
-
pH 7.8, 36°C, recombinant enzyme
0.41
(2R,3S)-3-allylmalic acid
-
pH 7.8, 36°C, recombinant enzyme
2.8
(2R,3S)-3-allylmalic acid
-
pH 7.8, 28°C, recombinant enzyme
0.29
(2R,3S)-3-propylmalic acid
-
pH 7.8, 36°C, recombinant enzyme
0.78
(2R,3S)-3-propylmalic acid
-
pH 7.8, 28°C, recombinant enzyme
0.05
3-isopropylmalate
-
mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.31
3-isopropylmalate
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.68
3-isopropylmalate
-
mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.71
3-isopropylmalate
-
mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
1.33
3-isopropylmalate
-
pH 7.8, 25°C, recombinant wild-type enzyme
0.083
3-vinylmalate
-
pH 7.8, 28°C, recombinant enzyme
3.4
3-vinylmalate
-
pH 7.8, 36°C, recombinant enzyme
0.6
ethylmalate
-
pH 7.8, 36°C, recombinant enzyme
1
ethylmalate
-
pH 7.8, 28°C, recombinant enzyme
0.0042
homoisocitrate
-
oxidate decarboxylation of homoisocitrate
0.0073
homoisocitrate
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.01
homoisocitrate
-
value below
0.018
homoisocitrate
-
pH 7.8, 36°C, recombinant enzyme
0.0183
homoisocitrate
pH 7.8, 70°C, recombinant enzyme
0.037
homoisocitrate
-
mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.042
homoisocitrate
-
mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.064
homoisocitrate
-
wild type enzyme, with NADP+ as cosubstrate, at pH 8.0 and 60°C
0.17
homoisocitrate
-
mutant enzyme L83R, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.211
homoisocitrate
-
pH 7.8, 25°C, recombinant wild-type enzyme
0.211
homoisocitrate
-
pH 7.8, 28°C, recombinant enzyme
0.46
homoisocitrate
-
mutant enzyme I82N, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.819
homoisocitrate
-
pH 7.8, 25°C, recombinant mutant A80del
0.94
homoisocitrate
-
mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
1
homoisocitrate
-
pH 7.8, 25°C, recombinant mutant R87V
1.5
homoisocitrate
-
pH 7.8, 25°C, recombinant mutant R87T
3.2
homoisocitrate
-
reductive carboxylation of alpha-ketoadipate
0.014
isocitrate
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.0164
isocitrate
pH 7.8, 70°C, recombinant enzyme
0.161
isocitrate
-
pH 7.5, 60°C, recombinant mutant V135M
0.291
isocitrate
-
pH 7.8, 25°C, recombinant wild-type enzyme
0.291
isocitrate
-
pH 7.8, 28°C, recombinant enzyme
0.3
isocitrate
-
mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.465
isocitrate
-
pH 7.8, 25°C, recombinant mutant A80del
0.5
isocitrate
-
mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.521
isocitrate
-
pH 7.5, 60°C, recombinant wild-type enzyme
0.58
isocitrate
-
mutant enzyme L83R, with NAD+ as cosubstrate, at pH 8.0 and 60°C
1.2
isocitrate
-
mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
2.2
isocitrate
-
mutant enzyme I82N, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.036
NAD+
-
wild type enzyme, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.042
NAD+
-
native enzyme, pH 7.8, 20°C
0.1
NAD+
-
wild type enzyme, with isocitrate as cosubstrate, at pH 8.0 and 60°C
0.16
NAD+
-
mutant enzyme L83R, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.25
NAD+
-
mutant enzyme T71V, with isocitrate as cosubstrate, at pH 8.0 and 60°C
0.3
NAD+
-
pH 8.0, 25°C, in presence of K+
0.32
NAD+
-
mutant enzyme L81P, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.45
NAD+
-
oxidate decarboxylation of homoisocitrate
0.6
NAD+
-
mutant enzyme L81P, with isocitrate as cosubstrate, at pH 8.0 and 60°C
0.62
NAD+
-
mutant enzyme L83R, with isocitrate as cosubstrate, at pH 8.0 and 60°C
0.64
NAD+
-
mutant enzyme I82N, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.76
NAD+
-
mutant enzyme S80A, with isocitrate as cosubstrate, at pH 8.0 and 60°C
0.92
NAD+
-
mutant enzyme S80A, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.92
NAD+
-
wild type enzyme, with D-malate as cosubstrate, at pH 8.0 and 60°C
1
NAD+
-
mutant enzyme T71V, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
1.09
NAD+
-
recombinant His-tagged enzyme, pH 7.8, 20°C
1.2
NAD+
-
mutant enzyme S80A, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
1.3
NAD+
-
mutant enzyme L81P, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
1.5
NAD+
-
mutant enzyme T71V, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
1.5
NAD+
-
wild type enzyme, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
1.8
NAD+
-
mutant enzyme I82N, with isocitrate as cosubstrate, at pH 8.0 and 60°C
9
NAD+
-
pH 8.0, 25°C, in absence of K+
0.065
NADH
-
-
0.09
NADH
-
reductive carboxylation of alpha-ketoadipate
additional information
additional information
-
mutant enzymes kinetic analysis and pH-dependencies, overview
-
additional information
additional information
-
substitution of potassium acetate for KCl changes the kinetic mechanism of HIcDH from a steady state random to a fully ordered mechanism with the binding of Mg-HIc followed by K+ and NAD+, increase in the affinity of enzyme for Mg-HIc as a result of elimination of the inhibitory effect of Cl-, kinetic analysis, overview
-
additional information
additional information
Michaelis-Menten kinetics, the enzyme shows a steady-state random kinetic mechanism with a preferred order of addition of Mg2+ prior to NAD+. The same step(s) limit the reaction at limiting and saturating Mg2+ concentrations. Solvent kinetic deuterium isotope effects and viscosity effects are consistent with a rate-limiting pre-catalytic conformational change at saturating reactant concentrations
-
additional information
additional information
-
Michaelis-Menten kinetics, the enzyme shows a steady-state random kinetic mechanism with a preferred order of addition of Mg2+ prior to NAD+. The same step(s) limit the reaction at limiting and saturating Mg2+ concentrations. Solvent kinetic deuterium isotope effects and viscosity effects are consistent with a rate-limiting pre-catalytic conformational change at saturating reactant concentrations
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.38 - 0.4
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
0.78 - 25
(2R,3S)-3-(2-hydroxyethyl)malate
4.8 - 29
(2R,3S)-3-(3-hydroxypropyl)malate
2 - 8
(2R,3S)-3-(4-hydroxybutyl)malate
0.14 - 3
(2R,3S)-3-(4-pentenyl)malic acid
0.34 - 37
(2R,3S)-3-allylmalic acid
0.7 - 53
(2R,3S)-3-propylmalic acid
171
1-hydroxy-1,2,3-propanetricarboxylate
-
purified enzyme, pH 8.0, 60°C
171
1-hydroxy-1,2,4-butanetricarboxylate
-
purified enzyme, pH 8.0, 60°C
0.371 - 9.4
3-isopropylmalate
0.099
D-malate
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
4.8 - 46.2
homoisocitrate
0.37
isopropylmalate
-
pH 7.8, 28°C, recombinant enzyme
12
NADP+
-
wild type enzyme, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.59
trisodium (2S,3R)-2-(carboxylatomethoxy)-3-hydroxybutanedioate
-
-
2
trisodium (2S,3R)-2-[(carboxylatomethyl)amino]-3-hydroxybutanedioate
-
-
0.38
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
-
recombinant His-tagged enzyme, pH 7.8, 20°C
0.4
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
-
native enzyme, pH 7.8, 20°C
0.78
(2R,3S)-3-(2-hydroxyethyl)malate
-
pH 7.8, 36°C, recombinant enzyme
25
(2R,3S)-3-(2-hydroxyethyl)malate
-
pH 7.8, 28°C, recombinant enzyme
4.8
(2R,3S)-3-(3-hydroxypropyl)malate
-
pH 7.8, 36°C, recombinant enzyme
29
(2R,3S)-3-(3-hydroxypropyl)malate
-
pH 7.8, 28°C, recombinant enzyme
2 - 8
(2R,3S)-3-(4-hydroxybutyl)malate
-
pH 7.8, 28°C, recombinant enzyme
2.1
(2R,3S)-3-(4-hydroxybutyl)malate
-
pH 7.8, 36°C, recombinant enzyme
0.14
(2R,3S)-3-(4-pentenyl)malic acid
-
pH 7.8, 36°C, recombinant enzyme
3
(2R,3S)-3-(4-pentenyl)malic acid
-
pH 7.8, 28°C, recombinant enzyme
0.34
(2R,3S)-3-allylmalic acid
-
pH 7.8, 36°C, recombinant enzyme
37
(2R,3S)-3-allylmalic acid
-
pH 7.8, 28°C, recombinant enzyme
0.7
(2R,3S)-3-propylmalic acid
-
pH 7.8, 36°C, recombinant enzyme
53
(2R,3S)-3-propylmalic acid
-
pH 7.8, 28°C, recombinant enzyme
0.371
3-isopropylmalate
-
pH 7.8, 25°C, recombinant wild-type enzyme
1.5
3-isopropylmalate
-
mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
2.3
3-isopropylmalate
-
mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
4.8
3-isopropylmalate
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
9.4
3-isopropylmalate
-
mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.5
3-vinylmalate
-
pH 7.8, 36°C, recombinant enzyme
0.77
3-vinylmalate
-
pH 7.8, 28°C, recombinant enzyme
0.61
ethylmalate
-
pH 7.8, 36°C, recombinant enzyme
43
ethylmalate
-
pH 7.8, 28°C, recombinant enzyme
4.8
homoisocitrate
-
mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
5.46
homoisocitrate
-
pH 7.8, 25°C, recombinant mutant A80del
6.9
homoisocitrate
-
mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
12
homoisocitrate
-
wild type enzyme, with NADP+ as cosubstrate, at pH 8.0 and 60°C
13
homoisocitrate
-
mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
13.7
homoisocitrate
pH 7.8, 70°C, recombinant enzyme
17
homoisocitrate
-
pH 7.8, 36°C, recombinant enzyme
17
homoisocitrate
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
20.8
homoisocitrate
-
pH 7.8, 25°C, recombinant mutant R87V
27.8
homoisocitrate
-
pH 7.8, 25°C, recombinant mutant R87T
43
homoisocitrate
-
mutant enzyme L83R, with NAD+ as cosubstrate, at pH 8.0 and 60°C
45
homoisocitrate
-
mutant enzyme I82N, with NAD+ as cosubstrate, at pH 8.0 and 60°C
46
homoisocitrate
-
pH 7.8, 28°C, recombinant enzyme
46.2
homoisocitrate
-
pH 7.8, 25°C, recombinant wild-type enzyme
0.22
isocitrate
-
mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.71
isocitrate
-
mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
1
isocitrate
-
mutant enzyme I82N, with NAD+ as cosubstrate, at pH 8.0 and 60°C
1.1
isocitrate
-
mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
5
isocitrate
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
6.6
isocitrate
-
mutant enzyme L83R, with NAD+ as cosubstrate, at pH 8.0 and 60°C
10.9
isocitrate
-
pH 7.8, 25°C, recombinant mutant A80del
14.8
isocitrate
pH 7.8, 70°C, recombinant enzyme
42.8
isocitrate
-
pH 7.8, 25°C, recombinant wild-type enzyme
43
isocitrate
-
pH 7.8, 28°C, recombinant enzyme
211
isocitrate
-
pH 7.5, 60°C, recombinant mutant V135M
438
isocitrate
-
pH 7.5, 60°C, recombinant wild-type enzyme
0.099
NAD+
-
wild type enzyme, with D-malate as cosubstrate, at pH 8.0 and 60°C
0.38
NAD+
-
recombinant His-tagged enzyme, pH 7.8, 20°C
0.4
NAD+
-
native enzyme, pH 7.8, 20°C
4.8
NAD+
-
wild type enzyme, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
5
NAD+
-
wild type enzyme, with isocitrate as cosubstrate, at pH 8.0 and 60°C
17
NAD+
-
wild type enzyme, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5.16 - 8.75
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
2.2 - 46
3-isopropylmalate
0.022
D-malate
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
5.1 - 2300
homoisocitrate
1.6
NADP+
-
wild type enzyme, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
5.16
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
-
recombinant His-tagged enzyme, pH 7.8, 20°C
8.75
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
-
native enzyme, pH 7.8, 20°C
2.2
3-isopropylmalate
-
mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
13
3-isopropylmalate
-
mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
15
3-isopropylmalate
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
46
3-isopropylmalate
-
mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
5.1
homoisocitrate
-
mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
98
homoisocitrate
-
mutant enzyme I82N, with NAD+ as cosubstrate, at pH 8.0 and 60°C
190
homoisocitrate
-
mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
190
homoisocitrate
-
wild type enzyme, with NADP+ as cosubstrate, at pH 8.0 and 60°C
250
homoisocitrate
-
mutant enzyme L83R, with NAD+ as cosubstrate, at pH 8.0 and 60°C
310
homoisocitrate
-
mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
2300
homoisocitrate
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.44
isocitrate
-
mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.45
isocitrate
-
mutant enzyme I82N, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.92
isocitrate
-
mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
2.4
isocitrate
-
mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
11
isocitrate
-
mutant enzyme L83R, with NAD+ as cosubstrate, at pH 8.0 and 60°C
360
isocitrate
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.11
NAD+
-
wild type enzyme, with D-malate as cosubstrate, at pH 8.0 and 60°C
0.35
NAD+
-
recombinant His-tagged enzyme, pH 7.8, 20°C
0.44
NAD+
-
native enzyme, pH 7.8, 20°C
0.56
NAD+
-
mutant enzyme I82N, with isocitrate as cosubstrate, at pH 8.0 and 60°C
0.88
NAD+
-
mutant enzyme T71V, with isocitrate as cosubstrate, at pH 8.0 and 60°C
0.93
NAD+
-
mutant enzyme S80A, with isocitrate as cosubstrate, at pH 8.0 and 60°C
1.2
NAD+
-
mutant enzyme L81P, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
1.8
NAD+
-
mutant enzyme L81P, with isocitrate as cosubstrate, at pH 8.0 and 60°C
1.9
NAD+
-
mutant enzyme S80A, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
3.2
NAD+
-
mutant enzyme T71V, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
3.2
NAD+
-
wild type enzyme, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
7.5
NAD+
-
mutant enzyme S80A, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
9.4
NAD+
-
mutant enzyme T71V, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
11
NAD+
-
mutant enzyme L83R, with isocitrate as cosubstrate, at pH 8.0 and 60°C
41
NAD+
-
mutant enzyme L81P, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
50
NAD+
-
wild type enzyme, with isocitrate as cosubstrate, at pH 8.0 and 60°C
70
NAD+
-
mutant enzyme I82N, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
270
NAD+
-
mutant enzyme L83R, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
470
NAD+
-
wild type enzyme, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.013
(2S,3S)-thiahomoisocitrate
pH 7.8, 60°C
0.79 - 3.1
(R,E)-(3-carboxypropylidene)malic acid
1.4 - 5.2
(R,E)-(3-hydroxypropylidene)malic acid
0.072 - 0.26
(R,Z)-(3-carboxypropylidene)malic acid
0.51 - 15.3
(R,Z)-(3-hydroxypropylidene)malic acid
0.088
3-vinylmalate
-
pH 7.8, 28°C, recombinant enzyme
12
3-[(carboxymethyl)sulfanyl]-2-oxopropanoic acid
-
-
0.002
Mg-homoisocitrate
-
oxidate decarboxylation of homoisocitrate
77
NAD+
-
pH 8.0, 25°C, in absence of KOAc
0.01
trisodium (2S,3R)-2-(carboxylatomethoxy)-3-hydroxybutanedioate
-
-
0.000097
trisodium (2S,3S)-2-[(carboxylatomethyl)sulfanyl]-3-hydroxybutanedioate
-
-
0.79
(R,E)-(3-carboxypropylidene)malic acid
-
pH 7.8, 36°C, recombinant enzyme
3.1
(R,E)-(3-carboxypropylidene)malic acid
-
pH 7.8, 28°C, recombinant enzyme
1.4
(R,E)-(3-hydroxypropylidene)malic acid
-
pH 7.8, 36°C, recombinant enzyme
5.2
(R,E)-(3-hydroxypropylidene)malic acid
-
pH 7.8, 28°C, recombinant enzyme
0.072
(R,Z)-(3-carboxypropylidene)malic acid
-
pH 7.8, 36°C, recombinant enzyme
0.26
(R,Z)-(3-carboxypropylidene)malic acid
-
pH 7.8, 28°C, recombinant enzyme
0.51
(R,Z)-(3-hydroxypropylidene)malic acid
-
pH 7.8, 36°C, recombinant enzyme
15.3
(R,Z)-(3-hydroxypropylidene)malic acid
-
pH 7.8, 28°C, recombinant enzyme
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.
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.
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A80del
-
site-directed mutagenesis, the mutant shows altered substrate specificity preferring isocitrate to homoisocitrate, it is unable to oxidize 3-isopropylmalate, the specificity is similar to the enzyme from Thermus thermophilus
R87T
-
site-directed mutagenesis, the mutant oxidizes homoisocitrate, but not isocitrate and 3-isopropylmalate
R87V
-
site-directed mutagenesis, the mutant oxidizes homoisocitrate, but not isocitrate and 3-isopropylmalate
D271N
site-directed mutagenesis, mutation of a metal ion ligand and binding determinant for Mg2+, to N. The mutant enzyme shows a decrease of 520fold in V and V/Km_Mg2+, suggesting that the same step(s) limit the reaction at limiting and saturating MgHIc concentrations
I82N
-
the mutant shows decreased catalytic efficiency with homoisocitrate and isocitrate compared to the wild type enzyme and has no activity with 3-isopropylmalate
L81P
-
the mutant shows decreased catalytic efficiency with homoisocitrate, isocitrate and 3-isopropylmalate compared to the wild type enzyme
L83R
-
the mutant shows decreased catalytic efficiency with homoisocitrate and isocitrate compared to the wild type enzyme and has no activity with 3-isopropylmalate
S80A
-
the mutant shows decreased catalytic efficiency with homoisocitrate, isocitrate and 3-isopropylmalate compared to the wild type enzyme
T71V
-
the mutant shows decreased catalytic efficiency with homoisocitrate and isocitrate, as well as increased catalytic efficiency with 3-isopropylmalate compared to the wild type enzyme
I82N
-
the mutant shows decreased catalytic efficiency with homoisocitrate and isocitrate compared to the wild type enzyme and has no activity with 3-isopropylmalate
-
L81P
-
the mutant shows decreased catalytic efficiency with homoisocitrate, isocitrate and 3-isopropylmalate compared to the wild type enzyme
-
L83R
-
the mutant shows decreased catalytic efficiency with homoisocitrate and isocitrate compared to the wild type enzyme and has no activity with 3-isopropylmalate
-
S80A
-
the mutant shows decreased catalytic efficiency with homoisocitrate, isocitrate and 3-isopropylmalate compared to the wild type enzyme
-
T71V
-
the mutant shows decreased catalytic efficiency with homoisocitrate and isocitrate, as well as increased catalytic efficiency with 3-isopropylmalate compared to the wild type enzyme
-
R85V
-
complete loss of activity with isocitrate, significant activity with 3-isopropylmalate, no effect on activity with homoisocitrate
V135M
-
site-directed mutagenesis, tetramer-to-dimer structural transition enhances the activity with isocitrate 1.6fold
R85V
-
complete loss of activity with isocitrate, significant activity with 3-isopropylmalate, no effect on activity with homoisocitrate
-
K206M
site-directed mutagenesis, inactive mutant
K206M
-
site-directed mutagenesis, the active site mutant shows about 2400fold reduced activity compared to the wild-type enzyme, the Km for HIc does not change significantly
Y150F
site-directed mutagenesis, inactive mutant
Y150F
-
site-directed mutagenesis, the active site mutant shows about 680fold reduced activity compared to the wild-type enzyme, the Km for HIc does not change significantly
additional information
-
modulation of the broad substrate specificity of the trifunctional enzyme through site-directed mutagenesis, overview
additional information
-
trex mutant allele, T to C exchange at nucleotide 251. Midgestation lethal mutant which displays craniofacial, limb, and organ abnormalities due to insufficient retinoic acid signaling
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