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Information on EC 1.1.1.42 - isocitrate dehydrogenase (NADP+) and Organism(s) Archaeoglobus fulgidus and UniProt Accession O29610

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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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This record set is specific for:
Archaeoglobus fulgidus
UNIPROT: O29610
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The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
isocitrate
+
NADP+
=
2-oxoglutarate
+
CO2
+
NADPH
+
H+
+
=
+
+
+
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
-
-
-
-
CtIDP2
-
-
-
-
IDH
-
-
-
-
IDP
-
-
-
-
isocitrate dehydrogenase (NADP)
-
-
-
-
isocitrate dehydrogenase (NADP-dependent)
-
-
-
-
isocitrate dehydrogenase (nicotinamide adenine dinucleotide phosphate)
-
-
-
-
NADP isocitric dehydrogenase
-
-
-
-
NADP+-linked isocitrate dehydrogenase
-
-
-
-
NADP+-specific ICDH
-
-
-
-
NADP-dependent isocitrate dehydrogenase
-
-
-
-
NADP-dependent isocitric dehydrogenase
-
-
-
-
NADP-linked isocitrate dehydrogenase
-
-
-
-
NADP-specific isocitrate dehydrogenase
-
-
-
-
oxalosuccinate decarboxylase
-
-
-
-
oxalsuccinic decarboxylase
-
-
-
-
PS-NADP-IDH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidative decarboxylation
-
-
-
-
reductive carboxylation
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
show the reaction diagram
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
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
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
absolute requirement for divalent cations
Mn2+
absolute requirement for divalent cations
Zn2+
a zinc ion is tightly bound to Asp301, Asp305, Asp277 in the active site of subunit A and subunit B
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.118
D,L-isocitrate
-
0.332
isocitrate
60°C, pH 8.0
0.0165 - 0.03
NADP+
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
255
isocitrate
60°C, pH 8.0
219
NADP+
60°C, pH 8.0
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
700
isocitrate
60°C, pH 8.0
13300
NADP+
60°C, pH 8.0
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.04
-
pH 7.5, 65°C, cell extract
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
alpha2, 2 * 42000, SDS-PAGE
80000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
alpha2, 2 * 42000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion technique with reservoir solution consisting of 0.6 M ZnSO4 and 0.1 M Na cacodylate, pH 6.3
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
half life of 22 min in 50 mM tricine-KOH buffer, pH 8
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, several months, under oxic conditions
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Steen, I.H.; Lien.T.; Birkeland, N-K.
Biochemical and phylogenetic characterization of isocitrate dehydrogenase from a hyperthermophilic archaeon, Archaeoglobus fulgidus
Arch. MIcrobiol.
168
412-420
1997
Archaeoglobus fulgidus (O29610)
Manually annotated by BRENDA team
Vornolt, J.; Kunow, J.; Stetter, K.; Thauer, R.
Enzymes and coenzymes of the carbon monoxide dehydrogenase pathway for autotrophic CO2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus
Arch. Microbiol.
163
112-118
1995
Archaeoglobus fulgidus, Archaeoglobus lithotrophicus, Archaeoglobus lithotrophicus TF-2, Archaeoglobus profundus, Archaeoglobus profundus DSM 5631
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team