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8-(4-bromo-2,3-dioxobutylthio)-NAD+ + isocitrate
2-oxoglutarate + CO2 + 8-(4-bromo-2,3-dioxobutylthio)-NADH
-
-
-
-
?
D-homoisocitrate + NAD+
? + NADH
-
-
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
-
very low activity
-
-
?
isocitrate + APAD+
2-oxoglutarate + CO2 + APADH
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
isocitrate + NAD+
2-oxoglutarate + NADH + H+ + CO2
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
isocitrate + NHD+
2-oxoglutarate + CO2 + NHDH
threo-Ds-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
additional information
?
-
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
r
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
r
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
ir
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
ir
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
catalytic residues binding isocitrate are located on subunit IDH2, while regulatory residues binding isocitrate are located on subunit IDH1
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
ir
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
isocitrate binds at 2 functionally distinct sites
-
-
?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
r
isocitrate + APAD+
2-oxoglutarate + CO2 + APADH
-
55% activity compared to NAD+
-
-
r
isocitrate + APAD+
2-oxoglutarate + CO2 + APADH
-
55% activity compared to NAD+
-
-
r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
key enzyme in the Krebs cycle
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
subunit IDH-I can substitute for a deficient mutant subunit IDH-II
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
key enzyme in the Krebs cycle
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
subunit IDH-I can substitute for a deficient mutant subunit IDH-II
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
100% activity
-
-
r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
100% activity
-
-
r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
the enzyme is NAD+-dependent
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
pyridine nucleotide contents in mitochondria and cytosol, regulation, overview
-
-
ir
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
wild-type enzyme is specific for NAD+, low activity with NADP+ as cofactor, mutant D328K shows dual coenzyme specificity, cofactor preference of mutant D328K/I329Y is shifted from NAD+ to NADP+
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
low activity with NADP+. Km-value for NADP+ is about 65fold higher than the KM-value for NAD+
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
enzyme has a regulatory role in the tricarboxylic cycle
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
enzyme performs the rate-limiting step in the mitochondrial tricarboxylic cycle and is subject to complex allosteric regulation
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
Sarcophaga barbata
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
the enzyme has considerably high activity with NAD+ compared with NADP+ as electron acceptor
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
the enzyme has considerably high activity with NAD+ compared with NADP+ as electron acceptor
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
waterbug
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
poor performance of the recombinant ZmIDH in decarboxylation
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
poor performance of the recombinant ZmIDH in decarboxylation
-
-
?
isocitrate + NAD+
2-oxoglutarate + NADH + H+ + CO2
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + NADH + H+ + CO2
-
IDH1 is an enzyme that catalyzes the oxidative decarboxylation of isocitrate into alpha-ketoglutarate utilizing either NAD+ or NADP+ as cosubstrates
-
-
?
isocitrate + NAD+
2-oxoglutarate + NADH + H+ + CO2
-
residue Y137 of subunit beta is involved in NAD+ binding and allosteric activation by ADP, residue Y126 of subunit alpha is required for catalytic activity and likely acts as a general acid in the reaction, gammaY135 is also required for catalytic activity and may be involved in proper folding of the enzyme. The corresponding tyrosines in the three dissimilar subunits of NAD-IDH thus have distinctive functions
-
-
?
isocitrate + NAD+
2-oxoglutarate + NADH + H+ + CO2
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + NADH + H+ + CO2
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
the enzyme has weak activity with NADP+
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
the enzyme has weak activity with NADP+
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
very low activity
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
very low activity
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
very low activity
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
very low activity
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
activity with enzyme mutant D487R/L488H, not the wild-type enzyme
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
activity with enzyme mutant D487R/L488H, not the wild-type enzyme
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
very low activity
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
very low activity
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
very low activity
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
very low activity
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
wild-type enzyme is specific for NAD+, low activity with NADP+ as cofactor, mutant D328K shows dual coenzyme specificity, cofactor preference of mutant D328K/I329Y is shifted from NAD+ to NADP+
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
the enzyme has considerably high activity with NAD+ compared with NADP+ as electron acceptor
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
the enzyme has considerably high activity with NAD+ compared with NADP+ as electron acceptor
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
poor performance of the recombinant ZmIDH in decarboxylation
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
poor performance of the recombinant ZmIDH in decarboxylation
-
-
?
isocitrate + NHD+
2-oxoglutarate + CO2 + NHDH
-
4.0% activity compared to NAD+
-
-
r
isocitrate + NHD+
2-oxoglutarate + CO2 + NHDH
-
4.0% activity compared to NAD+
-
-
r
threo-Ds-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
?
threo-Ds-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
-
-
-
-
ir
additional information
?
-
-
isocitrate dehydrogenase is an essential enzyme for riboflavin production in Ashbya gossypii
-
-
?
additional information
?
-
-
the enzyme has no detectable activity with NADP+
-
-
-
additional information
?
-
-
the enzyme has no detectable activity with NADP+
-
-
-
additional information
?
-
-
allosteric regulation, enzyme specifically binds to 5'-untranslated regions of yeast mitochondrial mRNAs, and transcripts containing these regions allosterically inhibit the enzyme, which can be relieved by activator AMP in presence of isocitrate, complex formation, overview
-
-
?
additional information
?
-
-
the enzyme is also active with NADP+ and NADPH, cf. EC 1.1.1.42
-
-
?
additional information
?
-
-
enzyme is involved in tricarboxylic acid cycle and plays a key role in the regulation of biosynthesis of citrate and isocitrate, yeast is overproducing citrate under nitrogen deficiency in presence of glucose
-
-
?
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0.03 - 0.45
D,L-isocitrate
0.002 - 0.385
DL-isocitrate
0.0183
homoisocitrate
-
6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2, 1mM NAD+
additional information
additional information
-
0.03
D,L-isocitrate
-
-
0.09
D-isocitrate
-
octameric wild-type enzyme with AMP, without DTT, pH 7.4, 24°C
0.1
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C150S with AMP, with or without DTT, pH 7.4, 24°C
0.1
D-isocitrate
-
octameric wild-type enzyme with AMP and DTT, pH 7.4, 24°C
0.17
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C150S/C242S with AMP, without DTT, pH 7.4, 24°C
0.19
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C150S/C242S with AMP and DTT, pH 7.4, 24°C
0.2
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C242S with AMP and DTT, pH 7.4, 24°C
0.32
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C242S with AMP, without DTT, pH 7.4, 24°C
0.48
D-isocitrate
-
octameric enzyme IDH1G15D/IDH2 with AMP and DTT, pH 7.4, 24°C
0.5
D-isocitrate
-
octameric enzyme IDH1G15D/IDH2 with AMP, without DTT, pH 7.4, 24°C
0.51
D-isocitrate
-
octameric wild-type enzyme without AMP, with DTT, pH 7.4, 24°C
0.53
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C150S without AMP and DTT, pH 7.4, 24°C
0.54
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C150S without AMP, with DTT, pH 7.4, 24°C
0.56
D-isocitrate
-
octameric wild-type enzyme without AMP and DTT, pH 7.4, 24°C
1.01
D-isocitrate
-
octameric enzyme mutant IDH1G15D/IDH2 without AMP and DTT, pH 7.4, 24°C
1.03
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C150S/C242S without AMP, with or without DTT, pH 7.4, 24°C
1.19
D-isocitrate
-
octameric enzyme IDH1G15D/IDH2 without AMP, with DTT, pH 7.4, 24°C
1.3
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C242S without AMP, with DTT, pH 7.4, 24°C
1.6
D-isocitrate
-
octameric enzyme mutant IDH1/IDH2C56S/C242S without AMP and DTT, pH 7.4, 24°C
0.002
DL-isocitrate
-
at pH 7.4 and 37°C
0.075
DL-isocitrate
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.143
DL-isocitrate
-
pH 7.5, 37°C, recombinant enzyme mutant S102G
0.148
DL-isocitrate
-
pH 7.5, 37°C, recombinant enzyme mutant S102A
0.15
DL-isocitrate
-
pH 7.5, 37°C, recombinant enzyme mutant S102T
0.385
DL-isocitrate
-
pH 7.5, 37°C, recombinant enzyme mutant S102Y
0.009
isocitrate
-
at pH 8.5 and 42°C
0.0164
isocitrate
-
6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2, 1mM NAD+
0.031
isocitrate
-
mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C
0.038
isocitrate
-
wild type enzyme, at pH 7.5 and 25°C
0.09
isocitrate
-
pH 7.2, 25°C, recombinant mutant betaY137E, in presence of 1 mM ADP
0.28
isocitrate
-
pH 7.2, 25°C, recombinant mutant betaY137F, in presence of 1 mM ADP
0.32
isocitrate
-
purified recombinant wild-type enzyme, pH 7.2, 25°C, in presence of 1 mM ADP
0.5
isocitrate
-
pH 7.2, 25°C, recombinant wild-type enzyme, in presence of 1 mM ADP
0.581
isocitrate
-
pH 7.4, 25°C
0.77
isocitrate
-
purified recombinant mutant beta-R99Q, pH 7.2, 25°C, in presence of 1 mM ADP
0.9
isocitrate
-
purified recombinant mutant beta-R99Q, pH 7.2, 25°C
0.92
isocitrate
-
pH 7.2, 25°C, recombinant mutant betaY137S, in presence of 1 mM ADP
1.2
isocitrate
-
pH 7.2, 25°C, recombinant mutant betaY137S
1.8
isocitrate
-
purified recombinant mutant gamma-R97Q, pH 7.2, 25°C, in presence of 1 mM ADP
1.8
isocitrate
-
pH 7.2, 25°C, recombinant mutant betaY137F
2
isocitrate
-
purified recombinant mutant gamma-R97Q, pH 7.2, 25°C
2
isocitrate
-
pH 7.2, 25°C, recombinant wild-type enzyme
2.2
isocitrate
-
purified recombinant wild-type enzyme, pH 7.2, 25°C
2.2
isocitrate
-
wild type enzyme in 20 mM isocitrate and 1mM MnSO4
2.2
isocitrate
-
25°C, pH 7.2, wild-type enzyme
2.4
isocitrate
-
pH 7.2, wild-type enzyme
2.9
isocitrate
-
pH 7.2, beta-subunit mutant enzyme D192N
3.4
isocitrate
-
D234C, alpha-subunit mutant, in 20 mM isocitrate and 1mM MnSO4
3.4
isocitrate
-
25°C, pH 7.2, alpha-subunit mutant enzyme D234C
3.4
isocitrate
-
pH 7.2, 25°C, recombinant mutant betaY137E
3.5
isocitrate
-
D206N, alpha-subunit mutant, in 20 mM isocitrate and 1mM MnSO4
3.5
isocitrate
-
25°C, pH 7.2, alpha-subunit mutant enzyme D206N
5.1
isocitrate
-
D217N, beta-subunit mutant, in 20 mM isocitrate and 1mM MnSO4
5.1
isocitrate
-
25°C, pH 7.2, beta-subunit mutant enzyme D217N
9.1
isocitrate
-
pH 7.2, alpha-subunit mutant enzyme D181N
13
isocitrate
-
pH 7.2, gamma-subunit mutant enzyme D190N
20
isocitrate
-
D230C, alpha-subunit mutant, in 20 mM isocitrate and 1mM MnSO4
20
isocitrate
-
25°C, pH 7.2, alpha-subunit mutant enzyme D230C
41
isocitrate
-
D215N, gamma-subunit mutant, in 20 mM isocitrate and 1mM MnSO4
41
isocitrate
-
25°C, pH 7.2, gamma-subunit mutant enzyme D215N
0.22
Mn2+
-
purified recombinant wild-type enzyme and mutant beta-R99Q, pH 7.2, 25°C
0.39
Mn2+
-
purified recombinant mutant gamma-R97Q, pH 7.2, 25°C
0.004
NAD+
-
purified recombinant mutant gamma-R97Q, pH 7.2, 25°C
0.014
NAD+
-
purified recombinant mutant beta-R99Q, pH 7.2, 25°C
0.0289
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
0.04
NAD+
-
25°C, pH 7.2, alpha-subunit mutant enzyme D234C
0.05
NAD+
-
at pH 7.4 and 37°C
0.06
NAD+
-
pH 7.2, 25°C, recombinant wild-type enzyme
0.066
NAD+
pH 8.0, 70°C, mutant enzyme D328K
0.068
NAD+
pH 8.0, 70°C, wild-type enzyme
0.0683
NAD+
pH 8.0, 70°C, the Km-value for NADP+ is about 65fold higher than the KM-value for NAD+
0.07
NAD+
-
25°C, pH 7.2, wild-type enzyme
0.073
NAD+
-
purified recombinant wild-type enzyme, pH 7.2, 25°C
0.0742
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
0.0771
NAD+
-
6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2
0.08
NAD+
-
pH 7.2, wild-type enzyme
0.088
NAD+
-
wild type enzyme, at pH 7.5 and 25°C
0.09
NAD+
-
pH 7.2, 25°C, recombinant mutant betaY137E
0.099
NAD+
-
7-fold mutant
0.113
NAD+
-
at pH 8.5 and 42°C
0.12
NAD+
-
pH 7.2, 25°C, recombinant mutant betaY137F
0.121
NAD+
-
wild type enzyme, at pH 8.0 and 25°C
0.126
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
0.136
NAD+
-
pH 7.4, 25°C
0.136
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
0.14
NAD+
-
25°C, pH 7.2, alpha-subunit mutant enzyme D206N
0.154
NAD+
-
pH 7.5, 37°C, recombinant enzyme
0.18
NAD+
pH 9.0, 30°C, native enzyme
0.19
NAD+
-
25°C, pH 7.2, gamma-subunit mutant enzyme D215N
0.226
NAD+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mn2+
0.245
NAD+
-
pH 7.5, 37°C, with Mn2+, recombinant enzyme
0.246
NAD+
-
pH 7.5, 37°C, recombinant enzyme mutant S102A
0.263
NAD+
wild-type enzyme, with Mg2+, pH 7.5, 35°C
0.265
NAD+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mg2+
0.295
NAD+
-
pH 7.5, 37°C, recombinant enzyme mutant S102G
0.309
NAD+
wild-type enzyme, with Mn2+, pH 7.5, 35°C
0.312
NAD+
-
pH 7.5, 37°C, with Mg2+, recombinant enzyme
0.33
NAD+
-
membrane-associated ICDH
0.336
NAD+
pH 8.0, 70°C, mutant enzyme D328K/I329Y
0.35
NAD+
-
pH 7.5, 37°C, recombinant enzyme mutant S102T
0.384
NAD+
-
mutant enzyme D268K, at pH 8.0 and 25°C
0.493
NAD+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
0.63
NAD+
-
pH 7.2, 25°C, recombinant mutant betaY137S
0.664
NAD+
mutant D487R/L488H, with Mn2+, pH 7.5, 35°C
0.68
NAD+
-
25°C, pH 7.2, beta-subunit mutant enzyme D217N
0.71
NAD+
-
pH 7.2, beta-subunit mutant enzyme D192N
0.738
NAD+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R, with Mn2+
0.903
NAD+
-
in the presence of Mg2+, at pH 8.0 and 25°C
1.1
NAD+
-
25°C, pH 7.2, alpha-subunit mutant enzyme D230C
1.1325
NAD+
-
in the presence of Mn2+, at pH 8.0 and 25°C
1.2
NAD+
-
pH 7.2, alpha-subunit mutant enzyme D181N
1.5
NAD+
-
pH 7.2, gamma-subunit mutant enzyme D190N
1.56
NAD+
-
pH 7.5, 37°C, recombinant enzyme mutant S102Y
2.948
NAD+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
3.15
NAD+
-
mutant enzymeD268K/I269Y/A275V, at pH 8.0 and 25°C
4.413
NAD+
-
mutant enzyme D268K/I269Y, at pH 8.0 and 25°C
4.5
NAD+
-
mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C
20.65
NAD+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R/M345H, with Mn2+
0.0082
NADP+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
0.0114
NADP+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
0.0139
NADP+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R/M345H, with Mn2+
0.031
NADP+
-
mutant enzymeD268K/I269Y/A275V, at pH 8.0 and 25°C
0.067
NADP+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R, with Mn2+
0.087
NADP+
-
mutant enzyme D268K/I269Y, at pH 8.0 and 25°C
0.101
NADP+
-
mutant enzyme D268K, at pH 8.0 and 25°C
0.157
NADP+
mutant D487R/L488H, with Mn2+, pH 7.5, 35°C
0.162
NADP+
pH 8.0, 70°C, mutant enzyme D328K
0.207
NADP+
-
mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C
0.211
NADP+
pH 8.0, 70°C, mutant enzyme D328K/I329Y
0.476
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
0.513
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
1.827
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
2.211
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
2.339
NADP+
-
wild type enzyme, at pH 8.0 and 25°C
3.354
NADP+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mg2+
4.3
NADP+
-
wild type enzyme, at pH 7.5 and 25°C
4.314
NADP+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mn2+
4.44
NADP+
pH 8.0, 70°C, wild-type enzyme
5.8
NADP+
-
7-fold mutant
6.57
NADP+
pH 9.0, 30°C, native enzyme
7.7
NADP+
-
pH 7.5, 37°C, with Mn2+, recombinant enzyme
8.2
NADP+
-
pH 7.5, 37°C, with Mg2+, recombinant enzyme
additional information
additional information
kinetic properties of the native and the recombinant enzyme are similar
-
additional information
additional information
-
kinetic properties of the native and the recombinant enzyme are similar
-
additional information
additional information
-
kinetics and ligand binding
-
additional information
additional information
-
kinetics and ligand binding
-
additional information
additional information
-
NAD+-specific D-isocitrate dehydrogenase is an allosterically regulated. AMP and NAD+ binding kinetics of enzyme mutants in presence or absence of DTT, overview
-
additional information
additional information
-
yeast NAD+-specific isocitrate dehydrogenase is an allosterically regulated
-
additional information
additional information
-
OtIDH exhibits a sigmoidal kinetic behavior in response to isocitrate unlike other homodimeric enzyme homologues, and a remarkably high affinity for isocitrate unlike other heterooligomeric enzyme homologues
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
13.7
homoisocitrate
-
6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2, 1 mM NAD+
0.27
D-isocitrate
-
D234C, alpha-subunit mutant, in 20 mM isocitrate and 1 mM MnSO4
2.49
D-isocitrate
-
D230C, alpha-subunit mutant, in 20 mM isocitrate and 1 mM MnSO4
11.8
D-isocitrate
-
D215N, gamma-subunit mutant, in 20 mM isocitrate and 1 mM MnSO4
19.6
D-isocitrate
-
D217N, beta-subunit mutant, in 20 mM isocitrate and 1 mM MnSO4
30
D-isocitrate
-
wild type enzyme in 20 mM isocitrate and 1 mM MnSO4
36.8
D-isocitrate
-
D206N, alpha-subunit mutant, in 20 mM isocitrate and 1 mM MnSO4
1.5
DL-isocitrate
-
pH 7.5, 37°C, recombinant enzyme mutant S102Y
3.3
DL-isocitrate
-
pH 7.5, 37°C, recombinant enzyme mutant S102A
4
DL-isocitrate
-
pH 7.5, 37°C, recombinant enzyme mutant S102G
25
DL-isocitrate
-
pH 7.5, 37°C, recombinant enzyme mutant S102T
78.98
DL-isocitrate
-
at pH 7.4 and 37°C
124
DL-isocitrate
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.27
isocitrate
-
25°C, pH 7.2, alpha-subunit mutant enzyme D234C
2.49
isocitrate
-
25°C, pH 7.2, alpha-subunit mutant enzyme D230C
11.8
isocitrate
-
25°C, pH 7.2, gamma-subunit mutant enzyme D215N
14.8
isocitrate
-
6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2, 1 mM NAD+
19.6
isocitrate
-
25°C, pH 7.2, beta-subunit mutant enzyme D217N
30
isocitrate
-
25°C, pH 7.2, wild-type enzyme
36.8
isocitrate
-
25°C, pH 7.2, alpha-subunit mutant enzyme D206N
37
isocitrate
-
mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C
85
isocitrate
-
wild type enzyme, at pH 7.5 and 25°C
0.27
NAD+
-
25°C, pH 7.2, alpha-subunit mutant enzyme D234C
2.49
NAD+
-
25°C, pH 7.2, alpha-subunit mutant enzyme D230C
3
NAD+
-
pH 7.5, 37°C, recombinant enzyme mutant S102A
3.5
NAD+
-
pH 7.5, 37°C, recombinant enzyme mutant S102Y
7
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
9.1
NAD+
-
pH 7.5, 37°C, recombinant enzyme mutant S102G
9.5
NAD+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
9.7
NAD+
mutant D487R/L488H, with Mn2+, pH 7.5, 35°C
10.8
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
11.8
NAD+
-
25°C, pH 7.2, gamma-subunit mutant enzyme D215N
11.8
NAD+
-
mutant enzymeD268K/I269Y/A275V, at pH 8.0 and 25°C
19.6
NAD+
-
25°C, pH 7.2, beta-subunit mutant enzyme D217N
21.8
NAD+
-
6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2
22.5
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
29.1
NAD+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
30
NAD+
-
25°C, pH 7.2, wild-type enzyme
36.7
NAD+
wild-type enzyme, with Mg2+, pH 7.5, 35°C
36.8
NAD+
-
25°C, pH 7.2, alpha-subunit mutant enzyme D206N
37.3
NAD+
-
mutant enzyme D268K/I269Y, at pH 8.0 and 25°C
41
NAD+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R, with Mn2+
45.1
NAD+
pH 9.0, 30°C, native enzyme
52.8
NAD+
-
mutant enzyme D268K, at pH 8.0 and 25°C
56
NAD+
-
pH 7.5, 37°C, recombinant wild-type enzyme
59
NAD+
-
pH 7.5, 37°C, recombinant enzyme mutant S102T
59
NAD+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mg2+
60.4
NAD+
pH 8.0, 70°C, wild-type enzyme
60.6
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
74.6
NAD+
-
wild type enzyme, at pH 8.0 and 25°C
78
NAD+
-
wild type enzyme, at pH 7.5 and 25°C
79
NAD+
-
in the presence of Mg2+, at pH 8.0 and 25°C
79
NAD+
-
mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C
80.9
NAD+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R/M345H, with Mn2+
84.39
NAD+
-
at pH 7.4 and 37°C
84.7
NAD+
wild-type enzyme, with Mn2+, pH 7.5, 35°C
88
NAD+
-
pH 7.5, 37°C, with Mg2+, recombinant enzyme
103.4
NAD+
pH 8.0, 70°C, mutant enzyme D328K
105.6
NAD+
pH 8.0, 70°C, mutant enzyme D328K/I329Y
112
NAD+
-
pH 7.5, 37°C, with Mn2+, recombinant enzyme
115
NAD+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mn2+
166
NAD+
-
at pH 8.5 and 42°C
180.5
NAD+
-
in the presence of Mn2+, at pH 8.0 and 25°C
1.4
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
1.8
NADP+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
1.9
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
2
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
3.9
NADP+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R/M345H, with Mn2+
4.2
NADP+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
6.1
NADP+
-
wild type enzyme, at pH 8.0 and 25°C
6.9
NADP+
-
mutant enzymeD268K/I269Y/A275V, at pH 8.0 and 25°C
10
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
14
NADP+
-
pH 7.5, 37°C, with Mg2+, recombinant enzyme
17
NADP+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mg2+
21.3
NADP+
pH 9.0, 30°C, native enzyme
25
NADP+
-
pH 7.5, 37°C, with Mn2+, recombinant enzyme
30.4
NADP+
-
mutant enzyme D268K/I269Y, at pH 8.0 and 25°C
33
NADP+
-
wild type enzyme, at pH 7.5 and 25°C
38.5
NADP+
-
mutant enzyme D268K, at pH 8.0 and 25°C
43
NADP+
-
mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C
46
NADP+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mn2+
55.1
NADP+
mutant D487R/L488H, with Mn2+, pH 7.5, 35°C
56
NADP+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R, with Mn2+
93
NADP+
pH 8.0, 70°C, wild-type enzyme
133
NADP+
pH 8.0, 70°C, mutant enzyme D328K
168
NADP+
pH 8.0, 70°C, mutant enzyme D328K/I329Y
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000004 - 39500
DL-isocitrate
0.000004
DL-isocitrate
-
pH 7.5, 37°C, recombinant enzyme mutant S102Y
0.000022
DL-isocitrate
-
pH 7.5, 37°C, recombinant enzyme mutant S102A
0.000028
DL-isocitrate
-
pH 7.5, 37°C, recombinant enzyme mutant S102G
0.00017
DL-isocitrate
-
pH 7.5, 37°C, recombinant enzyme mutant S102T
0.00165
DL-isocitrate
-
pH 7.5, 37°C, recombinant wild-type enzyme
39500
DL-isocitrate
-
at pH 7.4 and 37°C
1200
isocitrate
-
mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C
2200
isocitrate
-
wild type enzyme, at pH 7.5 and 25°C
0.000002
NAD+
-
pH 7.5, 37°C, recombinant enzyme mutant S102Y
0.00001
NAD+
-
pH 7.5, 37°C, recombinant enzyme mutant S102A
0.00003
NAD+
-
pH 7.5, 37°C, recombinant enzyme mutant S102G
0.00017
NAD+
-
pH 7.5, 37°C, recombinant enzyme mutant S102T
0.0003
NAD+
-
pH 7.5, 37°C, with Mg2+, recombinant enzyme
0.00036
NAD+
-
pH 7.5, 37°C, recombinant enzyme
0.0005
NAD+
-
pH 7.5, 37°C, with Mn2+, recombinant enzyme
3.9
NAD+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R/M345H, with Mn2+
4
NAD+
-
mutant enzymeD268K/I269Y/A275V, at pH 8.0 and 25°C
8
NAD+
-
mutant enzyme D268K/I269Y, at pH 8.0 and 25°C
10
NAD+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
15
NAD+
mutant D487R/L488H, with Mn2+, pH 7.5, 35°C
17.7
NAD+
-
mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C
19.3
NAD+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
55.6
NAD+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R, with Mn2+
90
NAD+
-
in the presence of Mg2+, at pH 8.0 and 25°C
138
NAD+
-
mutant enzyme D268K, at pH 8.0 and 25°C
140
NAD+
wild-type enzyme, with Mg2+, pH 7.5, 35°C
146
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
160
NAD+
-
in the presence of Mn2+, at pH 8.0 and 25°C
179
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
242
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
261
NAD+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mg2+
270
NAD+
wild-type enzyme, with Mn2+, pH 7.5, 35°C
314
NAD+
pH 8.0, 70°C, mutant enzyme D328K/I329Y
434
NAD+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mn2+
444
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
617
NAD+
-
wild type enzyme, at pH 8.0 and 25°C
886
NAD+
-
wild type enzyme, at pH 7.5 and 25°C
888
NAD+
pH 8.0, 70°C, wild-type enzyme
1500
NAD+
-
at pH 8.5 and 42°C
1567
NAD+
pH 8.0, 70°C, mutant enzyme D328K
1690
NAD+
-
at pH 7.4 and 37°C
0.000002
NADP+
-
pH 7.5, 37°C, with Mg2+, recombinant enzyme
0.000003
NADP+
-
pH 7.5, 37°C, with Mn2+, recombinant enzyme
0.8
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
3
NADP+
-
wild type enzyme, at pH 8.0 and 25°C
4
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
4
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
4.5
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
5.1
NADP+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mg2+
7.7
NADP+
-
wild type enzyme, at pH 7.5 and 25°C
10.7
NADP+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mn2+
20.9
NADP+
pH 8.0, 70°C, wild-type enzyme
208
NADP+
-
mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C
220
NADP+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
223
NADP+
-
mutant enzymeD268K/I269Y/A275V, at pH 8.0 and 25°C
281
NADP+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R/M345H, with Mn2+
349
NADP+
-
mutant enzyme D268K/I269Y, at pH 8.0 and 25°C
350
NADP+
mutant D487R/L488H, with Mn2+, pH 7.5, 35°C
368
NADP+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
381
NADP+
-
mutant enzyme D268K, at pH 8.0 and 25°C
796
NADP+
pH 8.0, 70°C, mutant enzyme D328K/I329Y
821
NADP+
pH 8.0, 70°C, mutant enzyme D328K
836
NADP+
-
pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R, with Mn2+
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evolution
-
efficacy of association mapping for dissecting natural variation in primary metabolic pathways, the considerable genetic diversity observed in maize CCM genes underlies heritable phenotypic variation in enzyme activities and can be useful to identify putative functional sites
evolution
-
the ancient NAD-dependent IDHs might be the underlying origin of phosphorylation mechanism used by their bacterial NADP-dependent homologues
evolution
-
the recombinant ZmIDH is mainly NAD+-dependent and its catalytic efficiency (kcat/Km) is relative low when compared to the prokaryotic NADP+-IDHs
evolution
evolutionary relationships of IDHs, overview
evolution
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and is clustered into a unique clade among the type II subfamily
evolution
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes
evolution
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes
evolution
evolutionary relationships of IDHs, phylogenetic analysis, overview. The enzyme belongs to the IDH enzyme family and the subclade of type II homodimeric enzymes
evolution
-
OtIDH may be an ancestral form of type II IDHs (all other reported members are NADP+-linked enzymes) and may have evolved into NADP+-dependent IDH for adaptation to the increased demand of NADPH under carbon starvation
evolution
phylogenetic analyses divide the IDH protein family into two subgroups: types I and II. Based on cofactor usage, IDHs are either NAD+-specific (NAD-IDH) or NADP+-specific (NADP-IDH). NADP-IDH evolved from NAD-IDH. Type I IDHs include NAD-IDHs and NADP-IDHs. Type II NAD-IDHs is identified from the marine bacterium Congregibacter litoralis KT71, i.e ClIDH. Evolutionary relationships between 151 IDHs from different organisms, overview
evolution
-
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes
-
evolution
-
the recombinant ZmIDH is mainly NAD+-dependent and its catalytic efficiency (kcat/Km) is relative low when compared to the prokaryotic NADP+-IDHs
-
evolution
-
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes
-
evolution
-
evolutionary relationships of IDHs, phylogenetic analysis, overview. The enzyme belongs to the IDH enzyme family and the subclade of type II homodimeric enzymes
-
evolution
-
phylogenetic analyses divide the IDH protein family into two subgroups: types I and II. Based on cofactor usage, IDHs are either NAD+-specific (NAD-IDH) or NADP+-specific (NADP-IDH). NADP-IDH evolved from NAD-IDH. Type I IDHs include NAD-IDHs and NADP-IDHs. Type II NAD-IDHs is identified from the marine bacterium Congregibacter litoralis KT71, i.e ClIDH. Evolutionary relationships between 151 IDHs from different organisms, overview
-
evolution
-
evolutionary relationships of IDHs, overview
-
evolution
-
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and is clustered into a unique clade among the type II subfamily
-
malfunction
-
IDH activity is increased in patients with prolonged cell phone daily use over 4 h/day. Its level correlates negatively with either the motility ratio percentages or the progressive motility percentages in the study groups. NAD+-IDH in human seminal plasma can be one of seminal plasma biomarkers reflecting the mitochondrial function of spermatozoa. Alteration of its level reflect the defective motility of sperms among some cases of cellular phone users
malfunction
overexpression of IDH3alpha increases the phosphorylation level of Akt (protein kinase B) and neutralizes the cellular toxicity induced by aflatoxin B1 (AFB1) or H2O2 and apoptosis induced by AFB1, while the reduced expression of IDH3alpha by siRNA decreases the phosphorylation, indicating that IDH3alpha plays important roles in the oxidative stress-induced PI3K/Akt pathway. AFB1 treatment can increase the expression of IDH3alpha, and the activated PI3K/Akt pathway by IDH3alpha eventually neutralizes the apoptosis induced by AFB1
malfunction
overexpression of IDH3alpha increases the phosphorylation level of Akt (protein kinase B) and neutralizes the cellular toxicity induced by aflatoxin B1 (AFB1) or H2O2 and apoptosis induced by AFB1, while the reduced expression of IDH3alpha by siRNA decreases the phosphorylation, indicating that IDH3alpha plays important roles in the oxidative stress-induced PI3K/Akt pathway. AFB1 treatment can increase the expression of IDH3alpha, and the activated PI3K/Aktpathway by IDH3alpha eventually neutralizes the apoptosis induced by AFB1
malfunction
overexpression of IDH3alpha increases the phosphorylation level of Akt (protein kinase B) and neutralizes the cellular toxicity induced by aflatoxin B1 (AFB1) or H2O2 and apoptosis induced by AFB1, while the reduced expression of IDH3alpha by siRNA decreases the phosphorylation, indicating that IDH3alpha plays important roles in the oxidative stress-induced PI3K/Akt pathway. AFB1 treatment can increase the expression of IDH3alpha, and the activated PI3K/Aktpathway by IDH3alpha eventually neutralizes the apoptosis induced by AFB1
metabolism
regulatory controls of key enzymes during microbial lipid accumulation involving the enzyme, overview
metabolism
-
yeast IDH is regulated both by allostery and by covalent formation of a disulfide bond, and these regulatory mechanisms contribute to modulation of respiratory metabolism in vivo
metabolism
-
NAD-IDH is a key enzyme in the Krebs cycle
metabolism
-
NAD-IDH is a key enzyme in the tricarboxylic acid cycle
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
metabolism
-
regulatory controls of key enzymes during microbial lipid accumulation involving the enzyme, overview
-
metabolism
-
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
-
metabolism
-
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
-
metabolism
-
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
-
metabolism
-
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
-
physiological function
IDH3alpha increases the phosphorylation level and activation of Akt (protein kinase B)
physiological function
IDH3alpha increases the phosphorylation level and activation of Akt (protein kinase B)
physiological function
IDH3alpha increases the phosphorylation level and activation of Akt (protein kinase B)
physiological function
-
the cofactor swapping of the enzyme from NADPH to NADH decreases the biomass yield of Escherichia coli on acetate
additional information
-
reduction of mitochondrial IDH activity has little effect on the relative electron transport or assimilation rates and a minor reduction in the maximum efficiency of PSII
additional information
-
interactions between sulfhydryl side chains of IDH2 Cys150 residues limit access to eight D-isocitrate and four AMP binding sites. In the presence of dithiothreitol, all ligand binding sites except for two potential NAD+ sites can be occupied
additional information
-
Ser102 plays an important role in substrate binding and is required for the enzyme function
additional information
-
the IDH2 Cys-150 residue controls access to isocitrate binding sites. The wild-type enzyme displays four binding sites for isocitrate and two binding sites for AMP in the absence of dithiothreitol, and these numbers increase to eight and four in the presence of dithiothreitol, respectively
additional information
homology modeling and docking studies of the human NAD-IDHalpha, overview
additional information
-
homology modeling and docking studies of the human NAD-IDHalpha, overview
additional information
-
structure homology modelling, overview. Residue Asp344 is clearly a major determinant of coenzyme specificity in OtIDH and residue Met345 plays critical role in NAD+ recognition and binding
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C201M/C332Y/K344D/Y345I/V351A/Y391K/R395S
-
converts the cofactor specificity from 7000-fold preference of NADP+ to a 200-fold preference of NAD+
alphaY126E
-
site-directed mutagenesis of subunit alpha, almost inactive mutant, shows low activity at pH 6.1 instead of pH 7.2, Km,Mn2+ is 30fold higher in the alphaY126E mutant as compared with the wild-type. Km,NAD+ for the alphaY126E mutant is 29fold higher than that of the wild-type. The Vmax of the wild-type at pH 6.1 is 0.0144 mmol/min/mg, whereas that for the alphaY126E mutant is only 0.00103 mmol/min/mg, suggesting a critical role for the residue in enzyme activity
alphaY126F
-
site-directed mutagenesis of subunit alpha, inactive mutant
alphaY126S
-
site-directed mutagenesis of subunit alpha, inactive mutant
betaY137E
-
site-directed mutagenesis of subunit beta, the mutant shows reduced activity compared to the wild-type enzyme
betaY137F
-
site-directed mutagenesis of subunit beta, the mutant shows reduced activity compared to the wild-type enzyme
betaY137S
-
site-directed mutagenesis of subunit beta, the mutant shows reduced activity compared to the wild-type enzyme
D181N
-
mutation in the alpha-subunit exhibits a 2000fold decrease in Vmax, with increases of 15fold in the Kms for Mn2+ and NAD+ and a much smaller change in the Km for isocitrate. Mutant enzyme fails to respond to ADP by lowering the Km for isocitrate, although it binds to ADP
D190N
-
mutation in the gamma-subunit results in 4-5fold decrease in Vmax as compared to wild-type enzyme. The Km-values for NAD+ and for Mn2+ of the mutant enzyme are 19 and 72 times, respectively, that of the wild-type enzyme with a much smaller effect on the Km for isocitrate. Mutant enzyme fails to respond to ADP by lowering the Km for isocitrate, although it binds to ADP
D192N
-
mutation in the beta-subunit results in 4-5fold decrease in Vmax as compared to wild-type enzyme. The Km-value for NAD+ of the mutant enzyme is 9times that of the normal enzyme with little or no effect on the affinity for Mn2+ or isocitrate. Mutant enzyme fails to respond to ADP by lowering the Km for isocitrate, although it binds to ADP
gammaY135F
-
site-directed mutagenesis of subunit gamma, inactive mutant
L98P
the mutation is associated with retinitis pigmentosa
R132C
-
naturally occuring IDH1 mutation
R132G
-
naturally occuring IDH1 mutation
R132H
-
naturally occuring IDH1 mutation
R132L
-
naturally occuring IDH1 mutation
R132S
-
naturally occuring IDH1 mutation
R132V
-
naturally occuring IDH1 mutation
R88Q
-
site-directed mutagenesis, residue of the alpha-subunit, inactive mutant
R97Q
-
site-directed mutagenesis, residue of the additional mutant gamma-subunit, highly reduced activity compared to the wild-type enzyme
R99Q
-
site-directed mutagenesis, residue of the beta-subunit, reduced activity compared to the wild-type enzyme
D326R/M327H
site-directed mutagenesis, the coenzyme specificity of the mutant CaIDH Asp326/Met327 is completely reversed from NAD+ to NADP+
D326X/M327X
site-directed mutagenesis, the coenzyme specificity of the mutant OlIDH R326H327 is completely reversed from NAD+ to NADP+
D326R/M327H
-
site-directed mutagenesis, the coenzyme specificity of the mutant CaIDH Asp326/Met327 is completely reversed from NAD+ to NADP+
-
D326X/M327X
-
site-directed mutagenesis, the coenzyme specificity of the mutant OlIDH R326H327 is completely reversed from NAD+ to NADP+
-
D344R
-
site-directed mutagenesis, the mutant enzyme retains their native dimeric structure, and the mutant displays a 15fold preference for NADP+ over NAD+ compared to the wild-type enzyme
D344R/M345H
-
site-directed mutagenesis, the mutant enzyme retains their native dimeric structure, the mutant displays a 72fold preference for NADP+ over NAD+ compared to the wild-type enzyme
D459A/N461A/D463A/F465A
-
the mutant maintains comparable specific activity to that of wild type enzyme
IDH1-EF
-
the mutant without the EF-hand domain (deleted Gln424-Val495 in a total of 72 residues) completely lost its catalytic activity
D459A/N461A/D463A/F465A
-
the mutant maintains comparable specific activity to that of wild type enzyme
-
IDH1-EF
-
the mutant without the EF-hand domain (deleted Gln424-Val495 in a total of 72 residues) completely lost its catalytic activity
-
D328K
the mutant shows dual coenzyme specificity
D328K/I329Y
introduction of the double mutation shifts the cofactor preference from NAD+ to NADP+
A108R/F136Y/T241D/N245D
-
site-directed mutagenesis, residues of subunit IDH1 mutant is unable to bind AMP, ligand-binding analysis
A108R/F136Y/T241D/N245D/R114A/Y142F/D248T/D252N
-
site-directed mutagenesis, residues of subunit IDH1 are A108R, F136Y, T241D, and N245D, residues of subunit IDH2 are R114A, Y142F, D248T, and D252N, mutant is unable to bind AMP, ligand-binding analysis
C56S/C150S/C242S
-
site-directed mutagenesis, IDH1/IDH2C150S octameric enzyme
D279A/D280A
-
site-directed mutagenesis, mutation of a IDH1 residue, reduced AMP binding, ligand-binding analysis
D286A/I287A
-
site-directed mutagenesis, mutation of a IDH2 residue, highly reduced NAD+ binding, ligand-binding analysis
H281A
-
site-directed mutagenesis, mutation of a IDH2 residue, mutant cannot bind NAD+, ligand-binding analysis
I221A
residue changes in IDH2 subunits
I221A/V225A/V229A
mutant enzyme IDH1-IDH2(I221A/V225A/V229A) shows an about 6fold decrease in apparent affinity for isocitrate measured in the absence or presence of AMP as compared to wild-type enzyme. Mutant enzyme IDH1-IDH2 (I221A/V225A/V229A) exhibits a moderate decrease in apparent affnity for cofactor (about 2.5fold relative to wild-type) in the absence of AMP. The mutant enzyme has acquired the novel property of cooperativity with respect to NAD+, but this cooperativity is not apparent in the presence of AMP. The mutant enzyme with residue changes in only one subunit are active in vivo
R114A/Y142F/D248T/D252N
-
site-directed mutagenesis, residues of subunit subunit IDH2, ligand-binding analysis
R274A
-
site-directed mutagenesis, mutation of a IDH1 residue, reduced AMP binding, ligand-binding analysis
S220A
residue changes in IDH1 subunits
S92A/S98A
-
site-directed mutagenesis, residue of subunit IDH1 is S92, residue of subunit IDH2 is S98, ligand-binding analysis
V214A
residue changes in IDH1 subunits
V216A/S220A/V224A
IDH1(V216A/S220A/V224A)IDH2 mutant enzyme shows an about 6fold decrease in apparent affinity for isocitrate measured in the absence or presence of AMP as compared to wild-type enzyme. IDH1(V216A/S220A/V224A)IDH2 mutant enzyme exhibits a moderate decrease in apparent affnity for cofactor (about 2.5fold relative to wild-type) in the absence of AMP. The mutant enzyme has acquired the novel property of cooperativity with respect to NAD+, but this cooperativity is not apparent in the presence of AMP. The mutant enzyme with residue changes in only one subunit are active in vivo
V216A/S220A/V224A/I221A/V225A/V229A
in the absence of AMP, the IDH1(V216A/S220A/V224A)-IDH2(I221A/V225A/V229A) mutant enzyme demonstrates an about 30fold decrease in apparent Vmax relative to wild-type and a loss of cooperativity with respect to isocitrate and, in the presence of AMP, the apparent affinity of the enzyme for isocitrate is 35fold lower than that of the wild-type enzyme. This mutant enzyme also exhibits a significant decrease in apparent affinity for NAD+ (about 30fold in the absence of AMP and about 10fold in the presence of AMP relative to wild-type). The mutant enzyme has acquired the novel property of cooperativity with respect to NAD+, but this cooperativity is not apparent in the presence of AMP. The mutant enzyme demonstrates decreases in apparent affnity for isocitrate of about 12fold in the absence of AMP and of about 26fold in the presence of AMP relative to wild-type. For this mutant enzyme, with respect to isocitrate, allosteric activation by AMP and cooperativity in the absence of AMP are no longer apparen. The mutant enzyme is not fully functional in vivo
V224A
residue changes in IDH1 subunits
V225A
residue changes in IDH2 subunits
V229A
residue changes in IDH2 subunits
C150S
-
insensitive to treatment with diamide, the presence of the IDH2 Cys-150 residue (and perhaps the potential for disulfide bond formation) may contribute to cooperativity and may also limit maximal IDH activity
-
C56S/C242S
-
shows activity similar to wild type enzyme and is sensitive to treatment with diamide
-
I221A
-
residue changes in IDH2 subunits
-
K171L
-
mutant IDH1K171L
-
S220A
-
residue changes in IDH1 subunits
-
V214A
-
residue changes in IDH1 subunits
-
V224A
-
residue changes in IDH1 subunits
-
V225A
-
residue changes in IDH2 subunits
-
S102A
-
site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 3.3% of wild-type activity
S102G
-
site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 2.8% of wild-type activity
S102T
-
site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 16% of wild-type activity
S102Y
-
site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 1.1% of wild-type activity
D268K
-
the coenzyme specificity of the mutant is switched from NAD+ to NADP+
D268K/I269Y
-
the coenzyme specificity of the mutant is switched from NAD+ to NADP+
D268K/I269Y/A275V
-
the coenzyme specificity of the mutant is switched from NAD+ to NADP+
L580H/L591R/A640R
-
the mutant has a 21fold lower Km value for NADP+ when compared to the original enzyme. The turnover rate (kcat) towards isocitrate of the mutant is reduced by more than 50% as compared to the wild type enzyme and even though the mutant is capable of using NADP+ for catalysis, ist catalytic efficiency (kcat/Km) for isocitrate is relatively low, being half of that for the wild type enzyme as using NAD+
L580H/L591R/A640R
-
the mutant has a 21fold lower Km value for NADP+ when compared to the original enzyme. The turnover rate (kcat) towards isocitrate of the mutant is reduced by more than 50% as compared to the wild type enzyme and even though the mutant is capable of using NADP+ for catalysis, ist catalytic efficiency (kcat/Km) for isocitrate is relatively low, being half of that for the wild type enzyme as using NAD+
-
L584H/D595R
site-directed mutagenesis, the coenzyme specificity of the mutant CaIDH H584/R595 is completely reversed from NAD+ to NADP+
L584H/D595R
-
site-directed mutagenesis, the coenzyme specificity of the mutant CaIDH H584/R595 is completely reversed from NAD+ to NADP+
-
D487R/L488H
site-directed mutagenesis, the coenzyme specificity of a the ClIDH mutant is altered compared to the wild-type enzyme, and the preference of the mutant for NADP+ is approximately 24fold higher than that for NAD+, suggesting that ClIDH is an NAD+-specific ancestral enzyme in the type II IDH subgroup
D487R/L488H
-
site-directed mutagenesis, the coenzyme specificity of a the ClIDH mutant is altered compared to the wild-type enzyme, and the preference of the mutant for NADP+ is approximately 24fold higher than that for NAD+, suggesting that ClIDH is an NAD+-specific ancestral enzyme in the type II IDH subgroup
-
D206N
-
alpha-subunit mutant
D206N
-
specific activity of the alpha-subunit mutant enzyme is 1.3fold higher than specific activity of wild-type enzyme
D215N
-
gamma-subunit mutant
D215N
-
specific activity of the gamma-subunit mutant enzyme is 17% of specific activity of wild-type enzyme. 100fold increase in KM-value for Mn2+. Km-value for isocitrate is elevated
D217N
-
beta-subunit mutant
D217N
-
specific activity of the beta-subunit mutant enzyme is 33% of specific activity of wild-type enzyme. 16fold increase in KM-vlaue for NAD+
D230C
-
alpha-subunit mutant
D230C
-
specific activity of the alpha-subunit mutant enzyme is 6% of specific activity of wild-type enzyme. 32fold increase in KM-value for Mn2+. Km-value for isocitrate is elevated. 16fold increase in KM-vlaue for NAD+
D230N
-
alpha-subunit mutant
D230N
-
mutation in alpha-subunit results in complete loss of activity
D234C
-
alpha-subunit mutant
D234C
-
specific activity of the alpha-subunit mutant enzyme is 1% of specific activity of wild-type enzyme
D234N
-
alpha-subunit mutant
D234N
-
mutation in alpha-subunit results in complete loss of activity
C150S
-
insensitive to treatment with diamide, the presence of the IDH2 Cys-150 residue (and perhaps the potential for disulfide bond formation) may contribute to cooperativity and may also limit maximal IDH activity
C150S
-
an octameric IDH1/IDH2C150S mutant enzyme, that shows unaltered activity and similar kinetics compared to the wild-type enzyme
C150S
-
site-directed mutagenesis of subunit IDH2, disulfide bridge formation by C150 is abolished
C150S
-
site-directed mutagenesis, IDH1/IDH2C150S octameric enzyme
C56S/C242S
-
shows activity similar to wild type enzyme and is sensitive to treatment with diamide
C56S/C242S
-
an octameric IDH1/IDH2C56S/C242S mutant enzyme, the mutant enzyme shows a reduction in Vmax relative to that of the wild-type enzyme of about 50%, although about 30% activity is restored in the presence of dithiothreitol
C56S/C242S
-
site-directed mutagenesis of subunit IDH2, the mutation does not affect disulfide formation in the enzyme
C56S/C242S
-
site-directed mutagenesis, IDH1/IDH2C150S octameric enzyme
D279A
-
IDH1D279A
D279A
-
site-directed mutagenesis of subunit IDH1, the mutation results in a loss of activation by AMP
D286A
-
IDH2D286A
D286A
-
site-directed mutagenesis of subunit IDH2, the mutation results in a dramatic reduction in Vmax primarily due to a 70fold increase in the S0.5 value for NAD+
G15D
-
a tetrameric IDH1G15D/IDH2 mutant enzyme, that shows reduced activity and altered kinetics compared to the wild-type enzyme
G15D
-
site-directed mutagenesis of subunit IDH1, the tetrameric IDH1G15D/IDH2 enzyme exhibits half-site binding (two sites) for isocitrate in the absence of DTT and full-site binding (four sites) in the presence of DTT
I280A
-
IDH1I280A
I280A
-
site-directed mutagenesis of subunit IDH1, the mutation results in a loss of activation by AMP
I287A
-
IDH1I287A
I287A
-
site-directed mutagenesis of subunit IDH2, the mutation results in a dramatic reduction in Vmax primarily due to a 70fold increase in the S0.5 value for NAD+
S92A
-
site-directed mutagenesis, residue of subunit IDH1, reduction of isocitrate substrate binding sites by half, detrimental effects on isocitrate binding and respective kinetic defects in catalysis and allosteric activation by AMP, ligand-binding analysis
S98A
-
site-directed mutagenesis, residue of subunit IDH2, reduction of isocitrate substrate binding sites by half, detrimental effects on isocitrate binding and respective kinetic defects in catalysis and allosteric activation by AMP, ligand-binding analysis
additional information
-
construction of a knockout mutant of subunit IDH-II, disruption by dissociation insertion element, mutant strain shows normal growth and development, but reduced enzyme activity in mitochondria compared to the wild-type plants, no altered phenotype of the mutant plants, but slightly reduced growth
additional information
characterization of three IDH mutants corresponding to an insertion into a different IDH gene (At5g03290, idhv. At4g35260, idhi. At2g17130, idhii). Analysis of IDH mRNA and protein show that each mutant lacks the corresponding gene products. Leaf IDH activity is reduced by 92%, 60%, and 43% for idhv, idhi, and idhii, respectively
additional information
characterization of three IDH mutants corresponding to an insertion into a different IDH gene (At5g03290, idhv. At4g35260, idhi. At2g17130, idhii). Analysis of IDH mRNA and protein show that each mutant lacks the corresponding gene products. Leaf IDH activity is reduced by 92%, 60%, and 43% for idhv, idhi, and idhii, respectively
additional information
characterization of three IDH mutants corresponding to an insertion into a different IDH gene (At5g03290, idhv. At4g35260, idhi. At2g17130, idhii). Analysis of IDH mRNA and protein show that each mutant lacks the corresponding gene products. Leaf IDH activity is reduced by 92%, 60%, and 43% for idhv, idhi, and idhii, respectively
additional information
-
construction of a knockout mutant of subunit IDH-II, disruption by dissociation insertion element, mutant strain shows normal growth and development, but reduced enzyme activity in mitochondria compared to the wild-type plants, no altered phenotype of the mutant plants, but slightly reduced growth
-
additional information
-
mutational analysis of IDH1 codon 132 in 1185 cancer samples, overview
additional information
enzyme overexpression, or enzyme downregulation by siRNA
additional information
NAD-IDHalpha knockdown by shRNA
additional information
-
NAD-IDHalpha knockdown by shRNA
additional information
enzyme overexpression, or enzyme downregulation by siRNA
additional information
-
the enzyme's coenzyme specificity can be completely converted from NAD+ (ancient trait) to NADP+ (adaptive trait) by rational mutagenesis based on the evolutionary trace. Residues D344 and M345 are the determinants of NAD+ specificity
additional information
enzyme overexpression, or enzyme downregulation by siRNA
additional information
-
transgenic tomato plants expressing the IDH gene in antisense orientation display a mild reduction in the activity of the target enzyme in the leaves but essentially no visible alteration in growth from the wild-type. Fruit size and yield are, however, reduced
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Plaut, G.W.E.
Isocitrate dehydrogenase
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Identification of the subunits and target peptides of pig heart NAD-specific isocitrate dehydrogenase modified by the affinity label 8-(4-bromo-2,3-dioxobutylthio)NAD
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Two NAD+-dependent isocitrate dehydrogenase forms in Phycomyces blakesleeanus. Induction in response to acetate growth and characterization, kinetics, and regulation of both enzyme forms
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Determinants of cofactor specificity in isocitrate dehydrogenase: structure of an engineered NADP+ to NAD+ specificity-reversal mutant
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Effect of AMP on mRNA binding by yeast NAD+-specific isocitrate dehydrogenase
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Regulation of NAD(+)-dependent isocitrate dehydrogenase in the citrate producing yeast Yarrowia lipolytica
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Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in mitochondria and cytosol of pea leaves
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Effect of metabolites of gamma-aminobutyric shunt on activities of NAD- and NADP-isocitrate dehydrogenases and aconitate hydratase from higher plants
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Biochemical and molecular characterization of the NAD(+)-dependent isocitrate dehydrogenase from the chemolithotroph Acidithiobacillus thiooxidans
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Homo sapiens
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Structure and quantum chemical analysis of NAD+-dependent isocitrate dehydrogenase: hydride transfer and co-factor specificity
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PLoS ONE
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Homo sapiens (P50213 and O43837), Homo sapiens
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Methylobacillus flagellatus, Methylobacillus flagellatus ATCC51484
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Escherichia coli
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Homo sapiens (P50213 and O43837 and P51553), Homo sapiens
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Homo sapiens (P50213 and O43837 and P51553), Homo sapiens
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Homo sapiens (P50213 and O43837 and P51553), Homo sapiens
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