Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.1.1.42 - isocitrate dehydrogenase (NADP+) and Organism(s) Aeropyrum pernix and UniProt Accession Q9YE81

for references in articles please use BRENDA:EC1.1.1.42
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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].
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Aeropyrum pernix
UNIPROT: Q9YE81
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Aeropyrum pernix
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 + NADP+
2-oxoglutarate + CO2 + NADPH + H+
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 + CO2 + NADPH + H+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0444
NADP+
pH 8.0, 70°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47900
2 * 47900, calculated from sequence
70000
analytical ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
dissociation from dimer to monomer at pH 3.0
homodimer
monomer
dissociation from dimer to monomer at pH 3.0
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of a native enzyme at 2.2 A, a pseudo-native enzyme at 2.1 A, and of the enzyme in complex with NADP+, Ca2+ and D-isocitrate at 2.3 A
crystallization is carried out by the hanging-drop method at 20°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R211M
disruption of the seven-membered inter-domain ionic network. In wild-type enzyme the unfolding and folding transitions occurrs at slightly different denaturant concentrations even after prolonged equilibration time. The difference between the folding and the unfolding profiles is decreased in the mutant R211M
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110
the Tm-value is 109.9°C
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the inter-domain ionic network might be responsible for additional stabilization through a significant kinetic barrier in the unfolding pathway that can explain the larger difference observed between the folding and unfolding transitions of the wild type comparted to the mutant enzyme R211M
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Karlstrm, M.; Chiaraluce, R.; Giangiacomo, L.; Steen, I.H.; Birkeland, N.K.; Ladenstein, R.; Consalvi, V.
Thermodynamic and kinetic stability of a large multi-domain enzyme from the hyperthermophile Aeropyrum pernix
Extremophiles
14
213-223
2010
Aeropyrum pernix (Q9YE81), Aeropyrum pernix DSM 11879 (Q9YE81)
Manually annotated by BRENDA team
Steen, I.H.; Madern, D.; Karlstrm, M.; Lien, T.; Ladenstein, R.; Birkeland, N.K.
Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation
J. Biol. Chem.
276
43924-43931
2001
Thermotoga maritima (Q9X0N2), Thermotoga maritima, Aeropyrum pernix (Q9YE81), Aeropyrum pernix, Aeropyrum pernix DSM 11879 (Q9YE81), Thermotoga maritima DSM 3109 (Q9X0N2)
Manually annotated by BRENDA team
Karlstrm, M.; Stokke, R.; Steen, I.H.; Birkeland, N.K.; Ladenstein, R.
Isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix: X-ray structure analysis of a ternary enzyme-substrate complex and thermal stability
J. Mol. Biol.
345
559-577
2005
Aeropyrum pernix (Q9YE81), Aeropyrum pernix, Aeropyrum pernix DSM 11879 (Q9YE81)
Manually annotated by BRENDA team
Jeong, J.J.; Sonoda, T.; Fushinobu, S.; Shoun, H.; Wakagi, T.
Crystal structure of isocitrate dehydrogenase from Aeropyrum pernix
Proteins
55
1087-1089
2004
Aeropyrum pernix (Q9YE81), Aeropyrum pernix DSM 11879 (Q9YE81)
Manually annotated by BRENDA team