1.1.1.87: homoisocitrate dehydrogenase
This is an abbreviated version!
For detailed information about homoisocitrate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.87
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1.1.1.87
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alpha-aminoadipate
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3-isopropylmalate
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homocitrate
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homoaconitase
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beta-decarboxylating
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alpha-ketoadipate
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medicine
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synthesis
- 1.1.1.87
- alpha-aminoadipate
- 3-isopropylmalate
- homocitrate
- homoaconitase
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beta-decarboxylating
- alpha-ketoadipate
- medicine
- synthesis
Reaction
Synonyms
(-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase (decarboxylating), 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), beta-decarboxylating dehydrogenase, dehydrogenase, homoisocitrate, EC 1.1.1.155, HIc, HIc dehydrogenase, HICDH, homoisocitrate dehydrogenase, homoisocitric dehydrogenase, isocitrate-homoisocitrate dehydrogenase, LYS12, protein PH1722, ScHICDH, TK0280
ECTree
1.1.1.87 homoisocitrate dehydrogenaseAdvanced search results
results (
results (KM Value
KM Value on EC 1.1.1.87 - homoisocitrate dehydrogenase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.4
1-hydroxy-1,2,3-propanetricarboxylate
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purified enzyme, pH 8.0, 60°C
7.5
1-hydroxy-1,2,4-butanetricarboxylate
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purified enzyme, pH 8.0, 60°C
4.5
D-malate
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wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
7.6
NADP+
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wild type enzyme, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.02
trisodium (2S,3R)-2-(carboxylatomethoxy)-3-hydroxybutanedioate
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-
0.15
trisodium (2S,3R)-2-[(carboxylatomethyl)amino]-3-hydroxybutanedioate
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-
0.074
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
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recombinant His-tagged enzyme, pH 7.8, 20°C
0.45
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
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native enzyme, pH 7.8, 20°C
0.59
(2R,3S)-3-(2-hydroxyethyl)malate
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pH 7.8, 28°C, recombinant enzyme
2.1
(2R,3S)-3-(2-hydroxyethyl)malate
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pH 7.8, 36°C, recombinant enzyme
0.51
(2R,3S)-3-(3-hydroxypropyl)malate
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pH 7.8, 28°C, recombinant enzyme
0.58
(2R,3S)-3-(3-hydroxypropyl)malate
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pH 7.8, 36°C, recombinant enzyme
0.44
(2R,3S)-3-(4-hydroxybutyl)malate
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pH 7.8, 36°C, recombinant enzyme
0.47
(2R,3S)-3-(4-hydroxybutyl)malate
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pH 7.8, 28°C, recombinant enzyme
2.7
(2R,3S)-3-(4-pentenyl)malic acid
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pH 7.8, 28°C, recombinant enzyme
9.4
(2R,3S)-3-(4-pentenyl)malic acid
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pH 7.8, 36°C, recombinant enzyme
0.05
3-isopropylmalate
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mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.31
3-isopropylmalate
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wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.68
3-isopropylmalate
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mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.71
3-isopropylmalate
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mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.0073
homoisocitrate
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wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.037
homoisocitrate
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mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.042
homoisocitrate
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mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.064
homoisocitrate
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wild type enzyme, with NADP+ as cosubstrate, at pH 8.0 and 60°C
0.17
homoisocitrate
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mutant enzyme L83R, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.46
homoisocitrate
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mutant enzyme I82N, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.94
homoisocitrate
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mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.014
isocitrate
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wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.3
isocitrate
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mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.5
isocitrate
-
mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.58
isocitrate
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mutant enzyme L83R, with NAD+ as cosubstrate, at pH 8.0 and 60°C
1.2
isocitrate
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mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
2.2
isocitrate
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mutant enzyme I82N, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.036
NAD+
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wild type enzyme, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.1
NAD+
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wild type enzyme, with isocitrate as cosubstrate, at pH 8.0 and 60°C
0.16
NAD+
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mutant enzyme L83R, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.25
NAD+
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mutant enzyme T71V, with isocitrate as cosubstrate, at pH 8.0 and 60°C
0.32
NAD+
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mutant enzyme L81P, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.6
NAD+
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mutant enzyme L81P, with isocitrate as cosubstrate, at pH 8.0 and 60°C
0.62
NAD+
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mutant enzyme L83R, with isocitrate as cosubstrate, at pH 8.0 and 60°C
0.64
NAD+
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mutant enzyme I82N, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.76
NAD+
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mutant enzyme S80A, with isocitrate as cosubstrate, at pH 8.0 and 60°C
0.92
NAD+
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mutant enzyme S80A, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
0.92
NAD+
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wild type enzyme, with D-malate as cosubstrate, at pH 8.0 and 60°C
1
NAD+
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mutant enzyme T71V, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
1.2
NAD+
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mutant enzyme S80A, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
1.3
NAD+
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mutant enzyme L81P, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
1.5
NAD+
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mutant enzyme T71V, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C
1.5
NAD+
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wild type enzyme, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C
1.8
NAD+
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mutant enzyme I82N, with isocitrate as cosubstrate, at pH 8.0 and 60°C
additional information
additional information
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mutant enzymes kinetic analysis and pH-dependencies, overview
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additional information
additional information
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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
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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
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additional information
additional information
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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
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