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Information on EC 1.1.1.42 - isocitrate dehydrogenase (NADP+) and Organism(s) Saccharomyces cerevisiae and UniProt Accession P21954
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1.1.1.42 isocitrate dehydrogenase (NADP+)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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progression-free
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proneural
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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+-specific isocitrate dehydrogenase
NADP-dependent isocitrate dehydrogenase
NADP-dependent isocitric dehydrogenase
-
-
-
-
NADP-linked isocitrate dehydrogenase
-
-
-
-
NADP-specific isocitrate dehydrogenase
-
-
-
-
oxalosuccinate decarboxylase
-
-
-
-
oxalsuccinic decarboxylase
-
-
-
-
PS-NADP-IDH
-
-
-
-
IDP
-
-
-
-
NADP-dependent isocitrate dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidative decarboxylation
-
-
-
-
reductive carboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -
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
9028-48-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
-
-
-
-
?
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
-
the reaction is reversible for isozyme IDP2
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
isozymes are compartment interchangeable for glutamate synthesis, although mitochondrial localization has a positive impact on this function during fermentative growth
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
reaction is reversible for isozymes IDP1 and IDP2
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
-
the reaction is reversible for isozyme IDP2
-
-
r
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
isozymes are compartment interchangeable for glutamate synthesis, although mitochondrial localization has a positive impact on this function during fermentative growth
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
activity is not affected by the nonspecific binding of the mitochondrial isozyme, not the cytosolic one, to 5'-untranslated regions of yeast mitochondrial mRNAs
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
glucose induces epression of isozyme IDP1, glycerol induces epression of isozymes IDP1 and IDP2, fatty acids induce epression of isozymes IDP1, IDP2, and IDP3
-
additional information
-
isozyme IDP3 is inducible by fatty acids, isozyme IDP2 by non-fermentable carbon sources, expression of isozyme IDP1 is constitutive
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics of isozymes IDP1 and IDP2
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
pH 7.0: about 60% of maximal activity, pH 9.0: about 95% of maximal activity, isoenzyme IDP1
6.5 - 9
pH 6.5: about 40% of maximal activity, pH 9.0: about 70% of maximal activity, isoenzyme IDP3
7 - 8
pH 7.0: about 60% of maximal activity, pH 8.0: about 40% of maximal activity, isoenzyme IDP2
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
IDP2 carrying a type I peroxisomal targeting sequence, IDP2+CKL, is only partially localized to peroxisomes, the enzyme is able to function either instead of peroxisomal IDP3 or as cytosolic IDP2
-
IDP3 contains a canonical type I peroxisomal targeting sequence, a carboxyl-terminal Cys-Lys-Leu tripeptide. IDP3 is normally strictly peroxisomal
additional information
-
influence of subcellular localization on isozyme activities, overview
-
additional information
-
subcellular localization study of isozymes, overview
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
IDP3 provides the NADPH required for beta-oxidation of some fatty acids in the peroxisome
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46381
-
x * 46381, isozyme IDP1, mass spectrometry, x * 46562, isozyme IDP2, mass spectrometry, x * 47856, isozyme IDP3, mass spectrometry
46562
-
x * 46381, isozyme IDP1, mass spectrometry, x * 46562, isozyme IDP2, mass spectrometry, x * 47856, isozyme IDP3, mass spectrometry
47856
-
x * 46381, isozyme IDP1, mass spectrometry, x * 46562, isozyme IDP2, mass spectrometry, x * 47856, isozyme IDP3, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 46381, isozyme IDP1, mass spectrometry, x * 46562, isozyme IDP2, mass spectrometry, x * 47856, isozyme IDP3, mass spectrometry
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of Saccharomyces cerevesiae mitochondrial NADP-IDH Idp1p in binary complexes with coenzyme NADP+, or substrate isocitrate, or product 2-oxoglutarate, and in a quaternary complex with NADPH, 2-oxoglutarate, and Ca2+, which represent different enzymatic states during the catalytic reaction. Crystallization is carried out at 20°C using the hanging-drop vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
construction of IDP1, IDP2, and IDP3 disruption mutants, and of double and triple disruption mutants in haploid strain MMY011. Complementation study in disruption mutants expressing the full-length IDPA enzyme from Aspergillus nidulans, which behaves similar to the yeast IDP2 harboring a type I peroxisomal targeting sequence, PTS1, and occurs in cytosol and peroxisomes, subcellular localization study, overview. Expression of IDPA lacking the mitochondrial targeting sequence and containing a different PTS1 results in the same expression level and subcellular orientation
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
isozyme IDP3 shows highest defense against endogeneous oxidative stress
-
654367
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged isozymes IDP1 and IDP2 by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
exchange of promotors and altering of organellar targeting for expression of isozymes IDO2 and IDO3 in mitochondria, and of isozymes IDP1 and IDP3 in the cytosol, functional complementation studies using mutant strains
-
expression of isozyme IDP1 and IDP2 as His-tagged enzymes in a disruption mutant
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Plaut, G.W.E.
Isocitrate dehydrogenase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
7
105-126
1963
Aspergillus niger, Saccharomyces cerevisiae, Citrobacter freundii, Mycobacterium tuberculosis, Sus scrofa, Trypanosoma cruzi
-
Contreras-Shannon, V.; McAlister-Henn, L.
Influence of compartmental localization on the function of yeast NADP+-specific isocitrate dehydrogenases
Arch. Biochem. Biophys.
423
235-246
2004
Saccharomyces cerevisiae
Anderson, S.L.; Schirf, V.; McAlister-Henn, L.
Effect of AMP on mRNA binding by yeast NAD+-specific isocitrate dehydrogenase
Biochemistry
41
7065-7073
2002
Saccharomyces cerevisiae
Xu, X.; Zhao, J.; Xu, Z.; Peng, B.; Huang, Q.; Arnold, E.; Ding, J.
Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity
J. Biol. Chem.
279
33946-33957
2004
Saccharomyces cerevisiae, Homo sapiens
Lu, Q.; Minard, K.I.; McAlister-Henn, L.
Dual compartmental localization and function of mammalian NADP+-specific isocitrate dehydrogenase in yeast
Arch. Biochem. Biophys.
472
17-25
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P21954), Saccharomyces cerevisiae (P41939), Mus musculus (O88844), Mus musculus (P54071), Mus musculus
Peng, Y.; Zhong, C.; Huang, W.; Ding, J.
Structural studies of Saccharomyces cerevesiae mitochondrial NADP-dependent isocitrate dehydrogenase in different enzymatic states reveal substantial conformational changes during the catalytic reaction
Protein Sci.
17
1542-1554
2008
Saccharomyces cerevisiae (P21954)
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