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Information on EC 1.1.1.42 - isocitrate dehydrogenase (NADP+) and Organism(s) Plasmodium falciparum

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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].
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Plasmodium falciparum
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Word Map
The taxonomic range for the selected organisms is: Plasmodium falciparum
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CtIDP1
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CtIDP2
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IDH
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IDP
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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+-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-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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PS-NADP-IDH
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidative decarboxylation
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redox reaction
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reductive carboxylation
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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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SUBSTRATE
PRODUCT                       
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
NATURAL SUBSTRATE
NATURAL PRODUCT
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
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enzyme is an integral part of the mitochondrial TCA cycle, and it is involved in providing NADPH for reductive reactions in the cell
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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specific for, no activity with NAD+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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dependent on divalent metal ions
Mg2+
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dependent on divalent metal ions, preferred metal ion
Mn2+
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dependent on divalent metal ions
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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applied oxidative stress leads to upregulation of enzyme expression in erythrocytic stages
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
D-isocitrate
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recombinant enzyme, pH 8.0, 30°C
0.013
Mg2+
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recombinant enzyme, pH 8.0, 30°C
0.022
Mn2+
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recombinant enzyme, pH 8.0, 30°C
0.09
NADP+
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recombinant enzyme, pH 8.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
138
D-isocitrate
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recombinant enzyme, pH 8.0, 30°C
138
NADP+
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recombinant enzyme, pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
162
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purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51000
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2 * 51000, about, recombinant enzyme, SDS-PAGE
90000
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recombinant enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 51000, about, recombinant enzyme, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble enzyme from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression as Strep-tagged protein in Escherichia coli BLR(DE3) exclusively in inclusion bodies, removal of 27 amino acids from the N-terminus results in expression of partially soluble protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wrenger, C.; Mueller, S.
Isocitrate dehydrogenase of Plasmodium falciparum. Energy metabolism or redox control?
Eur. J. Biochem.
270
1775-1783
2003
Plasmodium falciparum
Manually annotated by BRENDA team