Information on EC 1.1.1.42 - isocitrate dehydrogenase (NADP+)

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.42
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RECOMMENDED NAME
GeneOntology No.
isocitrate dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
oxalosuccinate = 2-oxoglutarate + CO2
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidative decarboxylation
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-
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redox reaction
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reductive carboxylation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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Carbon fixation pathways in prokaryotes
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Citrate cycle (TCA cycle)
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citric acid cycle
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ethylene biosynthesis V (engineered)
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Glutathione metabolism
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L-glutamine biosynthesis III
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Metabolic pathways
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methylaspartate cycle
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Microbial metabolism in diverse environments
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mixed acid fermentation
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NAD/NADP-NADH/NADPH cytosolic interconversion (yeast)
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partial TCA cycle (obligate autotrophs)
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reductive TCA cycle I
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TCA cycle I (prokaryotic)
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TCA cycle IV (2-oxoglutarate decarboxylase)
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TCA cycle V (2-oxoglutarate:ferredoxin oxidoreductase)
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TCA cycle VII (acetate-producers)
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TCA cycle VIII (helicobacter)
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SYSTEMATIC NAME
IUBMB Comments
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9028-48-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aeropyrum pernix DSM 11879
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UniProt
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia ecotype
gene icdh
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Manually annotated by BRENDA team
from 3 different altitudes of a stream of 700-1920 m, 2 polymorphic isozymes IDHP-A and IDHP-B, isozymes show allelic variants in populations belonging to different living heights in the stream, overview
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Manually annotated by BRENDA team
Azotobacter sp.
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
gene NADP-ICDH
UniProt
Manually annotated by BRENDA team
Capsicum annuum CMS-9704A
gene NADP-ICDH
UniProt
Manually annotated by BRENDA team
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Uniprot
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain SN-G42 and 124A
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Manually annotated by BRENDA team
strain SN-G42 and 124A
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Manually annotated by BRENDA team
gene Rv3339c
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Pinus spp.
Scots pine
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Manually annotated by BRENDA team
i.e. Rhodobacter sphaeroides
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Manually annotated by BRENDA team
strain 285
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Manually annotated by BRENDA team
strain 285
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
CA340
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Manually annotated by BRENDA team
duck weed, isozymes ICDH1 and ICDH2
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain TK54
UniProt
Manually annotated by BRENDA team
strain TK54
UniProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
PCC 6803
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Manually annotated by BRENDA team
YS-4
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Uniprot
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Y-4
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Manually annotated by BRENDA team
strain ABE-1
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Manually annotated by BRENDA team
Vibrio sp. ABE-1
strain ABE-1
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Manually annotated by BRENDA team
citrate-overproducing yeast
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3S)-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
show the reaction diagram
(2R,3S)-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
3-fluoroisocitrate + NADP+
3-fluoro-2-oxoglutarate + NADPH + CO2
show the reaction diagram
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-
-
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?
3-hydroxyisocitrate + NADP+
3-hydroxy-2-oxoglutarate + NADPH + CO2
show the reaction diagram
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?
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
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-
-
?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
show the reaction diagram
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
show the reaction diagram
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Ds-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
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-
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
show the reaction diagram
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
isopropylmalate + NADP+
?
show the reaction diagram
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-
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?
threo-Ds-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Q9SRZ6
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-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
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-
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?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
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the activity of the enzyme is markedly dependent on the concentration of NaCl or KC1 in the Tris/EDTA/Mg2+ buffer, being maximal in 0.5 M NaCl or KCl. The stimulatory effect of KCl is greater than that of NaCl
Na+
-
can substitute for Mg2+ by 20%
NaCl
-
the activity of the enzyme is markedly dependent on the concentration of NaCl or KC1 in the Tris/EDTA/Mg2+ buffer, being maximal in 0.5 M NaCl or KCl. The stimulatory effect of KCl is greater than that of NaCl
Ni2+
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absolute requirement for divalent cations
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2',5'-ADP
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2,3-Butanedione
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2-mercaptoethanol
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2-oxoglutarate
3-morpholinosydnonimine
44% inhibition at 5 mM of leaf and root enzymes
3-phosphoglycerate
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4-hydroxynonenal
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50% inhibition at 37°C, after 1 h at 0.5 mM, lipid peroxidation product, enzyme becomes susceptible to oxidative damage leading to structural alterations, carbonylation
5'-ADP
adenosine-3',5'-cyclic monophosphate
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cis-aconitate
citrate
Citric acid
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50% inhibition at 1 mM
desferroxamine
Diamide
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Diethylenetriaminepentaacetic acid
Diphenylchloroarsine
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dithiothreitol
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Fe2+
; the inhibitory effect of the Fe2+ and H2O2 mixture associated with the generation of hydroxyl radicals is lower in enzyme from ischemic heart compared to enzyme from normoxic heart
glutamate
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80% inhibition of isozyme ICDH2 at 2 mM
glutathione
glutathione disulfide
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incubation with 5 mM glutathione disulfide for 30 min completely eliminates activity
glyceraldehyde-3-phosphate
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glyoxalate
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20% inhibition at 1 mM, presence of 1 mM oxaloacetate results in 50% inhibition
glyoxylate
GSH
inhibits the leaf enzyme by 40% at 5 mM, but not the root enzyme
GTP
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10% inhibition at 1 mM
isocitrate
Itaconate
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18% inhibition at 5 mM
Li+
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slight inhibition
lipid hydroperoxide
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50% inhibition at 37°C, after 1 h at 0.05 mM, lipid peroxidation product, enzyme becomes susceptible to oxidative damage leading to structural alterations, carbonylation
malate
noncompetitive versus NADP+ and isocitrate
Maleate
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malondialdehyde
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50% inhibition at 37°C, after 1 h at 5 mM, lipid peroxidation product, enzyme becomes susceptible to oxidative damage leading to structural alterations, carbonylation
manganese(III) 5,10,15,20-tetrakis(N-methylpyridinium-2-yl)porphyrin
monoiodoacetate
N-ethylmaleimide
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NaCl
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isoform ICD-2, increase in activity in up to 200 mM NaCl. Isoform ICD-1, no influence of NaCl. Above 200 mM, NaCl is inhibitory
NAD+
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NADH
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noncompetitive
NaHCO3
nicotinamide mononucleotide
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oxalate
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18% inhibition at 5 mM
oxaloacetate
Oxalomalate
oxalylglycine
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p-chloromercuribenzoate
p-hydroxymercuribenzoate
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decarboxylation of isocitrate and oxalosuccinate
peroxynitrite
Phenarsazines
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Phenylglyoxal
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Phenylmercuric nitrate
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phosphoenolpyruvate
propanetricarboxylate
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pyridoxal 5'-phosphate
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Rb+
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slight inhibition
S-nitrosoglutathione
; 70.5% inhibtion at 5 mM of the leaf enzyme, 37.3% of the root enzyme
Selenite
-
inactivates IDPm
succinate
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isozymes ICDH2 and ICDH1
Threo-L-Isocitrate
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trans-aconitate
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isozyme ICDH1, not isozyme ICDH2
Urea
-
low molecular weight form
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetic acid
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mutant Y140T, 106fold activation compared to the wild-type enzyme
cis-aconitate
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isozyme ICDH2, not isozyme ICDH1
citrate
-
isozymes ICDH2 and ICDH1
ethylamine
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mutant K212Q, 4fold activation compared to the wild-type enzyme
glutamate
isocitrate
-
isozymes ICDH2 and ICDH1
NaCl
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isoform ICD-2, increase in activity in up to 200 mM NaCl. Isoform ICD-1, no influence of NaCl. Above 200 mM, NaCl is inhibitory
paraquat
administration at 0.01 mM to roots results in remarkable induction of enzyme gene expression and dramatic increase of gene activity
Phenol
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mutant Y140T, 88fold activation compared to the wild-type enzyme
succinic acid
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019 - 0.202
(2R,3S)-isocitrate
0.017 - 1.92
2-oxoglutarate
0.2 - 1.6
CO2
0.0017 - 0.118
D,L-isocitrate
0.028 - 0.239
D-isocitrate
0.00013 - 0.1243
DL-isocitrate
0.0006 - 2.07
isocitrate
0.012 - 0.31
Mg2+
0.00004 - 0.252
Mn2+
0.0179 - 18.6
NAD+
0.000028 - 19.6
NADP+
0.009 - 0.04
NADPH
11.68 - 13.82
NaHCO3
0.56 - 26
oxalosuccinate
additional information
additional information