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8-(4-bromo-2,3-dioxobutylthio)-NAD+ + isocitrate
2-oxoglutarate + CO2 + 8-(4-bromo-2,3-dioxobutylthio)-NADH
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-
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?
D-homoisocitrate + NAD+
? + NADH
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-
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?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
-
very low activity
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-
?
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
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?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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-
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-
r
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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-
r
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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-
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-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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-
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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-
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-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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-
-
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?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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-
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-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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-
-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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-
-
?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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-
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ir
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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ir
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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catalytic residues binding isocitrate are located on subunit IDH2, while regulatory residues binding isocitrate are located on subunit IDH1
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?
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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ir
D-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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-
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?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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isocitrate binds at 2 functionally distinct sites
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?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
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r
isocitrate + APAD+
2-oxoglutarate + CO2 + APADH
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55% activity compared to NAD+
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-
r
isocitrate + APAD+
2-oxoglutarate + CO2 + APADH
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55% activity compared to NAD+
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r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
key enzyme in the Krebs cycle
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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subunit IDH-I can substitute for a deficient mutant subunit IDH-II
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
key enzyme in the Krebs cycle
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-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
subunit IDH-I can substitute for a deficient mutant subunit IDH-II
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
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-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
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-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
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-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
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-
?
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+
-
-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
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-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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100% activity
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-
r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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100% activity
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r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
the enzyme is NAD+-dependent
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
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-
?
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+
-
-
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-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
pyridine nucleotide contents in mitochondria and cytosol, regulation, overview
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ir
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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?
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+
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?
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+
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
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?
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+
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-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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enzyme has a regulatory role in the tricarboxylic cycle
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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enzyme performs the rate-limiting step in the mitochondrial tricarboxylic cycle and is subject to complex allosteric regulation
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
Sarcophaga barbata
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
the enzyme has considerably high activity with NAD+ compared with NADP+ as electron acceptor
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
the enzyme has considerably high activity with NAD+ compared with NADP+ as electron acceptor
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
waterbug
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
poor performance of the recombinant ZmIDH in decarboxylation
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
poor performance of the recombinant ZmIDH in decarboxylation
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?
isocitrate + NAD+
2-oxoglutarate + NADH + H+ + CO2
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-
-
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?
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
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?
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
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?
isocitrate + NAD+
2-oxoglutarate + NADH + H+ + CO2
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-
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?
isocitrate + NAD+
2-oxoglutarate + NADH + H+ + CO2
-
-
-
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?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
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-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
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-
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-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
the enzyme has weak activity with NADP+
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?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
the enzyme has weak activity with NADP+
-
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?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
very low activity
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-
?
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
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-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
activity with enzyme mutant D487R/L488H, not the wild-type enzyme
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?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
very low activity
-
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?
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+
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-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
the enzyme has considerably high activity with NAD+ compared with NADP+ as electron acceptor
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-
?
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+
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-
r
isocitrate + NHD+
2-oxoglutarate + CO2 + NHDH
-
4.0% activity compared to NAD+
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-
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
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?
additional information
?
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-
the enzyme has no detectable activity with NADP+
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-
additional information
?
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the enzyme has no detectable activity with NADP+
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additional information
?
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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
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?
additional information
?
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the enzyme is also active with NADP+ and NADPH, cf. EC 1.1.1.42
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?
additional information
?
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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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?