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Information on EC 1.1.1.42 - isocitrate dehydrogenase (NADP+) and Organism(s) Corynebacterium glutamicum and UniProt Accession P50216

for references in articles please use BRENDA:EC1.1.1.42
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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].
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Corynebacterium glutamicum
UNIPROT: P50216
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The taxonomic range for the selected organisms is: Corynebacterium glutamicum
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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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
NADP+-specific isocitrate dehydrogenase
-
CtIDP1
-
-
-
-
CtIDP2
-
-
-
-
IDH
-
-
-
-
IDP
-
-
-
-
isocitrate dehydrogenase (NADP)
-
-
-
-
isocitrate dehydrogenase (NADP-dependent)
-
-
-
-
isocitrate dehydrogenase (nicotinamide adenine dinucleotide phosphate)
-
-
-
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NADP isocitric dehydrogenase
-
-
-
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NADP+-linked isocitrate dehydrogenase
-
-
-
-
NADP+-specific ICDH
-
-
-
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NADP-dependent isocitrate dehydrogenase
-
-
-
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NADP-dependent isocitric dehydrogenase
-
-
-
-
NADP-linked isocitrate dehydrogenase
-
-
-
-
NADP-specific isocitrate dehydrogenase
-
-
-
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oxalosuccinate decarboxylase
-
-
-
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oxalsuccinic decarboxylase
-
-
-
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PS-NADP-IDH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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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
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 + CO2 + NADPH + H+
show the reaction diagram
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADP+-binding site in the interdomain interface, the enzyme shows high specificity for NADP+ mediated by interactions with the negatively charged 2'-phosphate group, which is surrounded by the side chains of two arginines, one histidine and, via a water, one lysine residue, forming ion pairs and hydrogen bonds
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, 0.001 ml of 10 mg/ml protein in 12.5 mM 2-morpholinoethanesulfonic acid, pH 6.2, with 1.25 mM MnSO4, 1.25 mM dithiothreitol and 10% glycerol, is mixed with 0.001 ml of reservoir solution containing 25% w/v PEG 2000 MME, 0.2 M Tris-HCl, pH 7.3, and 0.2 M MgCl2, and with or without 0.001 ml of 10 mM NADP+, 3 days to 2 months, X-ray diffrcation structure determination and analysis at 1.8-1.9 A resolution, molecular replacement
crystallization with polyethylene glycol 2000 monomethyl ether
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substrate/cofactor-free structure in presence of Mg2+ shows a distinct open conformation and suggests the presence of low-energy conformers
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Audette, G.F.; Quail, J.W.; Hayakawa, K.; Bai, C.; Chen, R.; Delbaere, L.T.
Crystallization and preliminary X-ray diffraction studies of monomeric isocitrate dehydrogenase from Corynebacterium glutamicum
Acta Crystallogr. Sect. D
55
1584-1585
1999
Corynebacterium glutamicum
Manually annotated by BRENDA team
Imabayashi, F.; Aich, S.; Prasad, L.; Delbaere, L.T.
Substrate-free structure of a monomeric NADP isocitrate dehydrogenase: an open conformation phylogenetic relationship of isocitrate dehydrogenase
Proteins
63
100-112
2006
Corynebacterium glutamicum
Manually annotated by BRENDA team
Sidhu, N.S.; Delbaere, L.T.; Sheldrick, G.M.
Structure of a highly NADP+-specific isocitrate dehydrogenase
Acta Crystallogr. Sect. D
67
856-869
2011
Corynebacterium glutamicum (P50216), Corynebacterium glutamicum
Manually annotated by BRENDA team