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EC Tree
IUBMB Comments Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+), oxalosuccinate can be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm . The enzyme from some species can also use NAD+ but much more slowly [6,7].
The taxonomic range for the selected organisms is: Escherichia coli The enzyme appears in selected viruses and cellular organisms
Synonyms
isocitrate dehydrogenase 1, nadp-isocitrate dehydrogenase, nadp-dependent isocitrate dehydrogenase, isocitrate dehydrogenase-1, nadp-icdh, nadp-idh, nadp+-dependent isocitrate dehydrogenase, nadp-linked isocitrate dehydrogenase, nadp-specific isocitrate dehydrogenase, nadp+-specific isocitrate dehydrogenase,
more
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isocitrate dehydrogenase
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NADP+-isocitrate dehydrogenase
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isocitrate dehydrogenase (NADP)
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isocitrate dehydrogenase (NADP-dependent)
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isocitrate dehydrogenase (nicotinamide adenine dinucleotide phosphate)
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NADP isocitric dehydrogenase
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NADP+-dependent isocitrate dehydrogenase
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NADP+-linked isocitrate dehydrogenase
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NADP+-specific ICDH
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NADP-dependent isocitrate dehydrogenase
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NADP-dependent isocitric dehydrogenase
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NADP-isocitrate dehydrogenase
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NADP-linked isocitrate dehydrogenase
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NADP-specific isocitrate dehydrogenase
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oxalosuccinate decarboxylase
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oxalsuccinic decarboxylase
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oxidative decarboxylation
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reductive carboxylation
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-, -, -, -, -, -, -, -, -, -, -, -
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isocitrate:NADP+ oxidoreductase (decarboxylating)
Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+), oxalosuccinate can be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm [6]. The enzyme from some species can also use NAD+ but much more slowly [6,7].
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2-oxoglutarate + NADPH + H+
2-hydroxyglutarate + NADP+
the reaction is catalyzed by mutant enzymes R153H and R153C
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isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
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isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
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isopropylmalate + NADP+
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additional information
?
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does not use citrate as substrate
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isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
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isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
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isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
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isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
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isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
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NADP+
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Mn2+
2 mM used in assay conditions
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Diethylenetriaminepentaacetic acid
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manganese(III) 5,10,15,20-tetrakis(N-methylpyridinium-2-yl)porphyrin
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a superoxide dismutase mimic, ICD is inactivated by superoxide, but the inactivated enzyme is replaced by de novo protein synthesis
phosphoenolpyruvate
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allosteric inhibition. Phosphoenolpyruvate enhances the uncompetitive inhibition of isocitrate lyase by increasing isocitrate, which protects isocitrate dehydrogenase from the inhibition, and contributes to the control through the tricarboxylic acid cycle and glyoxylate shunt
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0.0217 - 0.0405
isocitrate
additional information
additional information
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2.2
2-oxoglutarate
mutant enzyme R153C, at pH 7.5 and 25°C
3.3
2-oxoglutarate
mutant enzyme R153H, at pH 7.5 and 25°C
0.0217
isocitrate
mutant enzyme R153H, at pH 7.5 and 25°C
0.0242
isocitrate
wild type enzyme, at pH 7.5 and 25°C
0.0318
isocitrate
mutant enzyme R153C, at pH 7.5 and 25°C
0.0405
isocitrate
40°C, pH 8.0
0.011
NADP+
mutant enzyme R153H, at pH 7.5 and 25°C
0.0121
NADP+
wild type enzyme, at pH 7.5 and 25°C
0.0176
NADP+
mutant enzyme R153C, at pH 7.5 and 25°C
0.0392
NADP+
40°C, pH 8.0
0.00071
NADPH
mutant enzyme R153H, at pH 7.5 and 25°C
0.00072
NADPH
mutant enzyme R153C, at pH 7.5 and 25°C
additional information
additional information
Km-values of wild-type and chimeric enzymes
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additional information
additional information
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Km-values of wild-type and chimeric enzymes
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additional information
additional information
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1
2-oxoglutarate
mutant enzyme R153C, at pH 7.5 and 25°C
1
2-oxoglutarate
mutant enzyme R153H, at pH 7.5 and 25°C
0.18
isocitrate
mutant enzyme R153H, at pH 7.5 and 25°C
0.3
isocitrate
mutant enzyme R153C, at pH 7.5 and 25°C
51.8
isocitrate
wild type enzyme, at pH 7.5 and 25°C
106.4
isocitrate
40°C, pH 8.0
additional information
additional information
turnover numbers of wild-type and chimeric enzymes
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additional information
additional information
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turnover numbers of wild-type and chimeric enzymes
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0.3 - 0.45
2-oxoglutarate
additional information
additional information
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0.3
2-oxoglutarate
mutant enzyme R153H, at pH 7.5 and 25°C
0.45
2-oxoglutarate
mutant enzyme R153C, at pH 7.5 and 25°C
8
isocitrate
mutant enzyme R153H, at pH 7.5 and 25°C
9
isocitrate
mutant enzyme R153C, at pH 7.5 and 25°C
2100
isocitrate
wild type enzyme, at pH 7.5 and 25°C
2600
isocitrate
40°C, pH 8.0
additional information
additional information
turnover numbers of wild-type and chimeric enzymes
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additional information
additional information
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turnover numbers of wild-type and chimeric enzymes
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0.31
phosphoenolpyruvate
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pH 7.1
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Uniprot
brenda
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brenda
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46200
2 * 46200, estimated from amino acid sequence
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homodimer
2 * 46200, estimated from amino acid sequence
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R153C
the mutation dramatically reduces the catalytic efficiency of the enzyme for isocitrate oxidation, which drops to 1.5% of the wild type enzyme. The mutant acquires a neomorphic ability of producing 2-hydroxyglutarate from 2-oxoglutarate
R153H
the mutation dramatically reduces the catalytic efficiency of the enzyme for isocitrate oxidation, which drops to 0.6% of the wild type enzyme. The mutant acquires a neomorphic ability of producing 2-hydroxyglutarate from 2-oxoglutarate
C201M
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higher affinity for NAD+ than for NADP+
C201N
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higher affinity for NAD+ than for NADP+
C201V
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higher affinity for NAD+ than for NADP+
S113E
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affinity for isopropylmalate is 37-fold compared to wild-type
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additional information
thermal stability of wild-type and chimeric enzymes
additional information
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thermal stability of wild-type and chimeric enzymes
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His-tagged enzyme is purified by TALON resin column chromatography, ICDH fused maltose-binding protein is purified by amylose resin chromatography
TALON metal affinity resin column chromatography
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expressed in Escherichia coli Rosetta (DE3) cells
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Ramaley, R.F.; Hudock, M.O.
Purification and properties of isocitrate dehydrogenase (NADP) from Thermus aquaticus YT-1, Bacillus subtilis-168 and Chlamydomonas reinhardti-Y-2
Biochim. Biophys. Acta
315
22-36
1973
Azotobacter vinelandii, Geobacillus stearothermophilus, Bacillus subtilis, Chlamydomonas reinhardtii, Escherichia coli, Thermus aquaticus
brenda
Seelig, G.F.; Colman, R.F.
Characterization of the physicochemical and catalytic properties of human heart NADP-dependent isocitrate dehydrogenase
Arch. Biochem. Biophys.
188
394-409
1978
Escherichia coli, Homo sapiens
brenda
Vasquez, B.; Reeves, H.C.
NADP-specific isocitrate dehydrogenase from Escherichia coli. V. Multiple forms of the enzyme
Biochim. Biophys. Acta
660
16-22
1981
Escherichia coli
brenda
Doyle, S.A.; Beernink, B.T.; Koshland, Jr., D.E.
Structural basis for a change in substrate specificity: crystal structur of S113E isocitrate dehydrogenase in a complex with isopropylmalate, Mg2+, and NAPD
Biochemistry
40
4234-4241
2001
Escherichia coli
brenda
Chen, R.; Greer, A.F.; Dean, A.M.
Structural constrains in protein engineering. The coenzyme specificity of Escherichia coli isocitrate dehydrogenase
Eur. J. Biochem.
250
578-582
1997
Escherichia coli
brenda
Ogawa, T.; Murakami, K.; Mori, H.; Ishii, N.; Tomita, M.; Yoshin, M.
Role of phosphoenolpyruvate in the NADP-isocitrate dehydrogenase and isocitrate lyase reaction in Escherichia coli
J. Bacteriol.
189
1176-1178
2007
Escherichia coli
brenda
Tsuchiya, D.; Shimizu, N.; Tomita, M.
Versatile architecture of a bacterial aconitase B and its catalytic performance in the sequential reaction coupled with isocitrate dehydrogenase
Biochim. Biophys. Acta
1784
1847-1856
2008
Escherichia coli (P08200)
brenda
Batinic-Haberle, I.; Benov, L.T.
An SOD mimic protects NADP+-dependent isocitrate dehydrogenase against oxidative inactivation
Free Radic. Res.
42
618-624
2008
Escherichia coli, Rattus norvegicus
brenda
Stokke, R.; Karlstroem, M.; Yang, N.; Leiros, I.; Ladenstein, R.; Birkeland, N.K.; Steen, I.H.
Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers
Extremophiles
11
481-493
2007
Archaeoglobus fulgidus (O29610), Archaeoglobus fulgidus, Escherichia coli (P08200), Escherichia coli
brenda
Song, P.; Li, S.; Wu, Y.; Lv, C.; Wang, P.; Zhu, G.
Point mutation (R153H or R153C) in Escherichia coli isocitrate dehydrogenase Biochemical characterization and functional implication
J. Basic Microbiol.
57
41-49
2017
Escherichia coli (P08200), Escherichia coli
brenda