Information on EC 1.1.1.42 - isocitrate dehydrogenase (NADP+)

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY
1.1.1.42
-
RECOMMENDED NAME
GeneOntology No.
isocitrate dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
active site structure and reaction mechanism, conformational changes at the active site resulting in closed and open forms, regulatory residues are isocitrate-binding Asp279and Ser94
-
isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
active site structure contains a well-ordered Mn2+-isocitrate complex, reaction mechanism
-
isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Ser95, Asn97, and Thr78 are important for the catalysis having distinguishable functions, overview
-
isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Tyr140 and Lys212 are required for catalytic activity, Tyr140 is the general acid that protonates the substrate after decarboxylation, Lys212 lowers as a positively charged residue the pK of the nearby ionizable group in the enzyme-substrate complex and stabilizes the carbanion formed initially on substrate decarboxylation
-
isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
protonation of the enolate to form product 2-oxoglutarate is the rate-limiting step
P9WKL1
isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
protonation of the enolate to form product 2-oxoglutarate is the rate-limiting step
-
-
oxalosuccinate = 2-oxoglutarate + CO2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reductive carboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Carbon fixation pathways in prokaryotes
-
-
Citrate cycle (TCA cycle)
-
-
citric acid cycle
-
-
ethylene biosynthesis V (engineered)
-
-
Glutathione metabolism
-
-
L-glutamine biosynthesis III
-
-
Metabolic pathways
-
-
methylaspartate cycle
-
-
Microbial metabolism in diverse environments
-
-
mixed acid fermentation
-
-
NAD/NADP-NADH/NADPH cytosolic interconversion (yeast)
-
-
reductive TCA cycle I
-
-
TCA cycle I (prokaryotic)
-
-
TCA cycle IV (2-oxoglutarate decarboxylase)
-
-
TCA cycle V (2-oxoglutarate:ferredoxin oxidoreductase)
-
-
TCA cycle VI (obligate autotrophs)
-
-
TCA cycle VII (acetate-producers)
-
-
TCA cycle VIII (helicobacter)
-
-
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].
SYNONYMS
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-dependent isocitrate dehydrogenase
-
-
-
-
NADP-dependent isocitric dehydrogenase
-
-
-
-
NADP-linked isocitrate dehydrogenase
-
-
-
-
NADP-specific isocitrate dehydrogenase
-
-
-
-
oxalosuccinate decarboxylase
-
-
-
-
oxalsuccinic decarboxylase
-
-
-
-
PS-NADP-IDH
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-48-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aeropyrum pernix DSM 11879
-
UniProt
Manually annotated by BRENDA team
gene At1g65930
UniProt
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia ecotype
gene icdh
-
-
Manually annotated by BRENDA team
Archaeoglobus lithotrophicus TF-2
-
-
-
Manually annotated by BRENDA team
from 3 different altitudes of a stream of 700-1920 m, 2 polymorphic isozymes IDHP-A and IDHP-B, isozymes show allelic variants in populations belonging to different living heights in the stream, overview
-
-
Manually annotated by BRENDA team
Azotobacter sp.
-
-
-
Manually annotated by BRENDA team
gene NADP-ICDH
UniProt
Manually annotated by BRENDA team
Capsicum annuum CMS-9704A
gene NADP-ICDH
UniProt
Manually annotated by BRENDA team
formerly Chlorobium thiosulfatophilum, strain L
-
-
Manually annotated by BRENDA team
green sulfur bacterium, strain M1
-
-
Manually annotated by BRENDA team
Escherichia coli K12
-
Uniprot
Manually annotated by BRENDA team
-
Q8X277
SwissProt
Manually annotated by BRENDA team
halophilic archaeon
Q8X277
SwissProt
Manually annotated by BRENDA team
recombinant enzyme
Q8X277
SwissProt
Manually annotated by BRENDA team
Haloferax volcanii DSM 3757
-
-
-
Manually annotated by BRENDA team
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
Moniliella megachiliensis SN-G42
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
26-weeks-old male mice
-
-
Manually annotated by BRENDA team
both mitochondrial and cytosolic isoform, expression in human fibroblast. Inverse relationship between the amount of enzyme expressed in target cells and their susceptibility to senescence as shown by changes in replicative potential, cell cycle, expression of p21 and p53. Lipid peroxidation, oxidative DNA damage, and intracellular peroxide generation is higher and cellular redox status shifts to a prooxidant condition in cells expressing low levels of enzyme
-
-
Manually annotated by BRENDA team
HL-60 cell lines with stable transfections with the cDNA for mouse IDPc
-
-
Manually annotated by BRENDA team
isoforms ICD-1 and ICD-2
-
-
Manually annotated by BRENDA team
Pinus spp.
Scots pine
-
-
Manually annotated by BRENDA team
cv. 294 040 Mrgrt Kelvedon Wonder, one cytosolic and one mitochondrial isozyme
-
-
Manually annotated by BRENDA team
L. cv. Lincoln
-
-
Manually annotated by BRENDA team
L. cv. Lincoln
SwissProt
Manually annotated by BRENDA team
albino
SwissProt
Manually annotated by BRENDA team
cytosolic isozyme; 1 cytosolic and 1 mitochondrial isozyme
SwissProt
Manually annotated by BRENDA team
male Wistar rats, 2 isozymes, ICD1 and ICD2
-
-
Manually annotated by BRENDA team
i.e. Rhodobacter sphaeroides
-
-
Manually annotated by BRENDA team
Rhodopseudomonas palustris 285
strain 285
-
-
Manually annotated by BRENDA team
1 cytosolic, 1 peroxisomal, and 1 mitochondrial isozyme
-
-
Manually annotated by BRENDA team
3 isozymes: mitochondrial IDP1, cytosolic IDP2, peroxisomal IDP3
-
-
Manually annotated by BRENDA team
cytosolic isozyme IDP1, and mitochondrial isozyme IDP2
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae MMY011
-
-
-
Manually annotated by BRENDA team
Saccharopolyspora erythraea CA340
CA340
-
-
Manually annotated by BRENDA team
duck weed, isozymes ICDH1 and ICDH2
-
-
Manually annotated by BRENDA team
Staphylococcus aureus ATCC12600
-
UniProt
Manually annotated by BRENDA team
Streptomyces diastaticus M1033
-
-
-
Manually annotated by BRENDA team
strain TK54
UniProt
Manually annotated by BRENDA team
Streptomyces lividans TK54
strain TK54
UniProt
Manually annotated by BRENDA team
Sulfolobus solfataricus DSM 1616
-
SwissProt
Manually annotated by BRENDA team
PCC 6803
-
-
Manually annotated by BRENDA team
Thermoleophilum minutum YS-4
YS-4
-
-
Manually annotated by BRENDA team
Thermoplasma acidophilum DSMZ 1728
-
UniProt
Manually annotated by BRENDA team
Thermotoga maritima DSM 3109
-
Uniprot
Manually annotated by BRENDA team
strain HB8
UniProt
Manually annotated by BRENDA team
gene Tc00.1047053506925.319 or IDH2; gene idh, two isozymes
UniProt
Manually annotated by BRENDA team
gene Tc00.1047053511575.60 or IDH1; gene idh, isozyme IDH1
UniProt
Manually annotated by BRENDA team
Vibrio parahaemolyticus Y-4
Y-4
-
-
Manually annotated by BRENDA team
strain ABE-1
-
-
Manually annotated by BRENDA team
Vibrio sp. ABE-1
strain ABE-1
-
-
Manually annotated by BRENDA team
citrate-overproducing yeast
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
IDH1 is critical in cellular metabolism
metabolism
O75874
metabolite profiling identifies elevated 2-hydroxyglutarate levels in IDH1 mutant R132H expressing cells compared to wild-type
metabolism
-
NAD(P)+-dependent isocitrate dehydrogenase is a key enzyme in tricarboxylic acid cycle
metabolism
J9Q6L4
NADP-isocitrate dehydrogenase catalyses the first oxidative decarboxylation reaction of the tricarboxic acid cycle, yielding 2-oxoglutarate, CO2, and NADPH from isocitrate via a two-step reaction
metabolism
Streptomyces diastaticus M1033
-
NAD(P)+-dependent isocitrate dehydrogenase is a key enzyme in tricarboxylic acid cycle
-
physiological function
-
part of citric acid cycle
physiological function
-
cICDH is involved in amino acid synthesis, and plays a role in redox signalling linked to pathogen responses, but cICDH is not required for plant development and primary metabolism in optimal growth conditions
physiological function
-
elective pressures in the brain environment may specifically favor the cell growth or survival of tumor cells with mutations in IDH1, regardless of primary tumor site, elective pressures in the brain environment may specifically favor the cell growth or survival of tumor cells with mutations in IDH2, regardless of primary tumor site
physiological function
-
IDH1 mutation predicts outcome in grade 2, 3, and 4 gliomas
physiological function
-
IDH1 regulates HIF-1alpha levels by controlling the level of 2-oxoglutarate. IDH1 appears to function as a tumor suppressor that, when mutationally inactivated, contributes to tumorigenesis in part through induction of the HIF-1 pathway. IDH1 is likely to function as a tumor suppressor gene rather than as an oncogene
physiological function
-
IDP3 provides the NADPH required for beta-oxidation of some fatty acids in the peroxisome
physiological function
-
mutation at R172 in the active site of IDH2 leads to a change in the molecular mechanism of enzyme catalysis, resulting in production and accumulation of elevated 2-hydroxyglutarate in acute myelogenous leukemia. The mutation reduces the affinity for isocitrate, and increases the affinity for NADPH and 2-oxoglutarate, preventing the oxidative decarboxylation of isocitrate to 2-oxoglutarate, and facilitating the conversion of 2-oxoglutarate to 2-hydroxyglutarate, mutations at R132 in the active site of IDH1 lead to a change in the molecular mechanism of enzyme catalysis, resulting in production and accumulation of elevated 2-hydroxyglutarate in acute myelogenous leukemia. The mutations reduce the affinity for isocitrate, and increase the affinity for NADPH and 2-oxoglutarate, preventing the oxidative decarboxylation of isocitrate to 2-oxoglutarate, and facilitating the conversion of 2-oxoglutarate to 2-hydroxyglutarate
physiological function
-
the mitochondrial NADP+-dependent isocitrate dehydrogenase controls the mitochondrial redox balance by supplying NADPH for antioxidant systems
physiological function
-
in the cytoplasm, NADP+-IDH often contributes significantly to the NADPH pool required for reductive fatty acid biosynthesis
physiological function
D7RIE8
isocitrate dehydrogenase plays pivotal role in the growth and pathogenesis of the bacteria
physiological function
Arabidopsis thaliana Columbia ecotype
-
cICDH is involved in amino acid synthesis, and plays a role in redox signalling linked to pathogen responses, but cICDH is not required for plant development and primary metabolism in optimal growth conditions
-
physiological function
Moniliella megachiliensis SN-G42
-
part of citric acid cycle
-
physiological function
Staphylococcus aureus ATCC12600
-
isocitrate dehydrogenase plays pivotal role in the growth and pathogenesis of the bacteria
-
physiological function
Saccharomyces cerevisiae MMY011
-
IDP3 provides the NADPH required for beta-oxidation of some fatty acids in the peroxisome
-
metabolism
Capsicum annuum CMS-9704A
-
NADP-isocitrate dehydrogenase catalyses the first oxidative decarboxylation reaction of the tricarboxic acid cycle, yielding 2-oxoglutarate, CO2, and NADPH from isocitrate via a two-step reaction
-
additional information
-
all tumors with complete 1p19q codeletion are mutated in the IDH1 or IDH2 gene. Glioma patients having IDH1/IDH2 mutations show inproved median overall survival, different outcomes in WHO grade II and III gliomas according to the 1p19q and IDH1/IDH2 statusses, overview
additional information
-
enzyme mutation R132H is involved in myelodysplastic syndrome
additional information
-
heterozygous mutations in the gene encoding IDH1 occur in certain human brain tumors, IDH is a strong factor in the development of gliomas. Tumor-derived IDH1 mutations impair the enzyme's affinity for its substrate and dominantly inhibit wild-type IDH1 activity through the formation of catalytically inactive heterodimers. HIF-1alpha levels are higher in human gliomas harboring an IDH1 mutation than in tumors without a mutation. Rise in HIF-1alpha levels occur, reversible by an 2-oxoglutarate derivative
additional information
-
knockdown of IDPc expression in HEK293 cells greatly enhances apoptosis induced by cadmium. DNA fragmentation is enhanced in IDPc siRNA-transfected HEK293 cells compared to control cells upon exposure to cadmium
additional information
O75874
mutations in the enzyme cytosolic IDH1 at R132 are a common feature of a major subset of primary human brain cancers, especially in grade II-III gliomas and secondary glioblastomas. The mutations result in loss of the enzyme's ability to catalyze conversion of isocitrate to 2-oxoglutarate. Expression of R132H mutant IDH1 results in no measurable production of NADPH from isocitrate, and isocitrate-dependent NADPH production increases with increasing amounts of wild-type enzyme
additional information
-
siRNA-mediated knockdown of IDPm suppresses hypoxia-induced stimulation of HIF-1alpha protein expression in PC-3 human prostate cancer cells
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3S)-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
show the reaction diagram
Streptomyces lividans, Streptomyces lividans TK54
B2ZAA4
slow reaction
-
-
?
(2R,3S)-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
(2R,3S)-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
Q6R6M7
-
-
-
?
(2R,3S)-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
P33197
-
-
-
?
(2R,3S)-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
Streptomyces lividans, Streptomyces lividans TK54
B2ZAA4
-
-
-
?
3-fluoroisocitrate + NADP+
3-fluoro-2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
3-hydroxyisocitrate + NADP+
3-hydroxy-2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
P41562
-
-
-
?
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
enzyme is an integral part of the mitochondrial TCA cycle, and it is involved in providing NADPH for reductive reactions in the cell
-
-
?
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
the reaction is reversible for isozyme IDP2
-
-
r
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Q9SRZ6
-
-
-
?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
show the reaction diagram
-
-
-
-
?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH
show the reaction diagram
Q8X277
NAD+ is only substrate for mutant R291S/K343D/Y344I/V350A/Y390P
-
-
?
DL-isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
show the reaction diagram
Streptomyces diastaticus, Streptomyces diastaticus M1033
-
low activityy with NAD+
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
P56574
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
Q8X277
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
Q8X277
NAD+ is not substrate for mutant R291S/K343D/Y344I/V350A/Y390P
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
Saccharopolyspora erythraea CA340
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Q4DG65, Q4E4L7
-
-
-
ir
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Q4DG65, Q4E4L7
carboxylation of 2-oxoglutarate to produce isocitrate
-
-
ir
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
NADP+ is the highly preferred cofactor
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Streptomyces diastaticus M1033
-
NADP+ is the highly preferred cofactor
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
DS-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
show the reaction diagram
Sulfolobus solfataricus, Sulfolobus solfataricus DSM 1616
Q9UWG7
Km-value for NAD+ is 34fold higher compared to KM-value for NADP+
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
-
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
O29610
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
Azotobacter sp.
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
Pinus spp.
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
Vibrio sp. ABE-1
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
Vibrio parahaemolyticus Y-4
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
Thermoleophilum minutum YS-4
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
P08200
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
P33198
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
P21954, P41939
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
O88844, P54071
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
Q6AQ66
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
P56574
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
A5U813, O53611
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
carbon dioxide-fixing enzyme in the reductive tricarboxylic acid cycle, preference for carboxylation reaction direction
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
cytosolic enzyme is critical in fat and cholesterol biosynthesis, enzyme content correlates with adipogenesis in wild-type adipocytes and in transgenic cells
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
enzyme has a self-regulatory mechanism of activity mimicking the phosphorylation mechanism of bacterial enzymes
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
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
show the reaction diagram
-
key enzyme of the tricarboxylic acid cycle
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
metabolic regulation of the isozymes
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
metabolic regulation, involved in the tricarboxylic acid cycle
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
the cytosolic isozyme supplies 2-oxoglutarate for the photorespiratory ammonia fixation, pyridine nucleotide contents in mitochondria and cytosol, regulation, overview
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
reaction is reversible for isozymes IDP1 and IDP2
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
Ser95, Asn97, and Thr78 are involved in substrate binding
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
isocitrate dehydrogenase is an important NADPH-generating enzyme in the endoplasmic reticulum
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
Q6R6M7
the enzyme could have a protective antioxidant role against certain environmental stresses in plants
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
Rhodopseudomonas palustris 285
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
Rhodopseudomonas palustris 285
-
metabolic regulation, involved in the tricarboxylic acid cycle
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
Escherichia coli K-12 W3110
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
O75874
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
O75874, P48735
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
O65853
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
IDH1 is an enzyme that catalyzes the oxidative decarboxylation of isocitrate into alpha-ketoglutarate utilizing either NAD+ or NADP+ as cosubstrates
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
Arabidopsis thaliana Columbia ecotype
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
Saccharomyces cerevisiae MMY011
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Q9UWG7
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
P9WKL1
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
P50216
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
J9Q6L4
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Q9HLV8
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
D7RIE8
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Q9YE81
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
P50216
the enzyme shows high substrate specificity
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Q9UWG7
Km-value for NAD+ is 34fold higher compared to KM-value for NADP+
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
P96318
strict substrate and coenzyme specificity
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
low activity with NAD+. Km-value for NAD+ is about 140fold higher than the KM-value for NADP+
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Aeropyrum pernix DSM 11879
Q9YE81
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Aeropyrum pernix DSM 11879
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Sulfolobus solfataricus DSM 1616
Q9UWG7
Km-value for NAD+ is 34fold higher compared to KM-value for NADP+
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Thermoplasma acidophilum DSMZ 1728
Q9HLV8
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Capsicum annuum CMS-9704A
J9Q6L4
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Thermotoga maritima DSM 3109
Q9X0N2
low activity with NAD+. Km-value for NAD+ is about 140fold higher than the KM-value for NADP+
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
P9WKL1
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Escherichia coli K12
P08200
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Staphylococcus aureus ATCC12600
D7RIE8
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Haloferax volcanii DSM 3757
-
-
-
-
?
threo-DS-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isopropylmalate + NADP+
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
His319 and His315 are not responsible for enzyme Fe2+-isocitrate cleavage
-
-
-
additional information
?
-
-
86% of total activity in the cell, main factor for synthesis of 2-oxoglutarate. Enzyme and cytoplasmic aspartate aminotransferase are regulated oppositely and the catalytic activity of one enzyme can be stimulated concurrently with a decrease in the activity of the other
-
-
-
additional information
?
-
-
during oxidative stress, enzyme activity appears to be modulated through enzymatic glutathionylation and deglutathionylation
-
-
-
additional information
?
-
-
enzyme plays an important regulatory role in cellular defense against oxidative stress and in senescence
-
-
-
additional information
?
-
P41562
suppression of enzyme activity by small interfering RNA results in impairment of glucose-stimulated insulin secretion, attenuates glucose-induced increments in pyruvate cycling activity and in NADPH levels, and causes increases in lactate production
-
-
-
additional information
?
-
P48735
NADP+-dependent isocitrate dehydrogenase may play an important role in regulating the apoptosis induced by heat shock
-
-
-
additional information
?
-
-
NADP+-dependent isocitrate dehydrogenase may play an important role in regulating the apoptosis induced by TNF-alpha and anticancer drugs
-
-
-
additional information
?
-
-
NADP+-dependent isocitrate dehydrogenase plays an important protective role in apoptosis of HL-60 cells induced by singlet oxygen
-
-
-
additional information
?
-
-
IDPm expression in HepG2 cells regulates ethanol-induced toxicity
-
-
-
additional information
?
-
P08200
does not use citrate as substrate
-
-
-
additional information
?
-
O75874
the R132H mutant IDH1 directly converts 2-oxoglutarate to 2-hydroxyglutarate, that rapidly accumulates in the medium of cells expressing R132H mutant IDH1
-
-
-
additional information
?
-
P9WKL1
Mycobacterium tuberculosis ICDH-1 also catalyzes the formation of 2-hydroxyglutarate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
enzyme is an integral part of the mitochondrial TCA cycle, and it is involved in providing NADPH for reductive reactions in the cell
-
-
?
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
the reaction is reversible for isozyme IDP2
-
-
r
D-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Q9SRZ6
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Q4DG65, Q4E4L7
-
-
-
ir
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Streptomyces diastaticus M1033
-
-
-
-
?
DL-isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
-
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
O29610
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
Azotobacter sp.
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
Pinus spp.
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
P33198
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
carbon dioxide-fixing enzyme in the reductive tricarboxylic acid cycle, preference for carboxylation reaction direction
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
cytosolic enzyme is critical in fat and cholesterol biosynthesis, enzyme content correlates with adipogenesis in wild-type adipocytes and in transgenic cells
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
enzyme has a self-regulatory mechanism of activity mimicking the phosphorylation mechanism of bacterial enzymes
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
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
show the reaction diagram
-
key enzyme of the tricarboxylic acid cycle
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
metabolic regulation of the isozymes
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
metabolic regulation, involved in the tricarboxylic acid cycle
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
the cytosolic isozyme supplies 2-oxoglutarate for the photorespiratory ammonia fixation, pyridine nucleotide contents in mitochondria and cytosol, regulation, overview
-
-
r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
-
isocitrate dehydrogenase is an important NADPH-generating enzyme in the endoplasmic reticulum
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
Q6R6M7
the enzyme could have a protective antioxidant role against certain environmental stresses in plants
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
O75874
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
O75874, P48735
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
-
-
-
r
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
O65853
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
-
IDH1 is an enzyme that catalyzes the oxidative decarboxylation of isocitrate into alpha-ketoglutarate utilizing either NAD+ or NADP+ as cosubstrates
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Q9UWG7
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
P9WKL1
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
P50216
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
J9Q6L4
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Q9HLV8
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
D7RIE8
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
P96318
strict substrate and coenzyme specificity
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Aeropyrum pernix DSM 11879
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH
show the reaction diagram
Rhodopseudomonas palustris 285
-
metabolic regulation, involved in the tricarboxylic acid cycle
-
-
r
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
Vibrio sp. ABE-1
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Sulfolobus solfataricus DSM 1616
Q9UWG7
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Thermoplasma acidophilum DSMZ 1728
Q9HLV8
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
Arabidopsis thaliana Columbia ecotype
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
Vibrio parahaemolyticus Y-4
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Capsicum annuum CMS-9704A
J9Q6L4
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Thermotoga maritima DSM 3109
Q9X0N2
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
P9WKL1
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + CO2
show the reaction diagram
Thermoleophilum minutum YS-4
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Staphylococcus aureus ATCC12600
D7RIE8
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
show the reaction diagram
Haloferax volcanii DSM 3757
-
-
-
-
?
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
show the reaction diagram
Saccharomyces cerevisiae MMY011
-
-
-
-
?
additional information
?
-
-
86% of total activity in the cell, main factor for synthesis of 2-oxoglutarate. Enzyme and cytoplasmic aspartate aminotransferase are regulated oppositely and the catalytic activity of one enzyme can be stimulated concurrently with a decrease in the activity of the other
-
-
-
additional information
?
-
-
during oxidative stress, enzyme activity appears to be modulated through enzymatic glutathionylation and deglutathionylation
-
-
-
additional information
?
-
-
enzyme plays an important regulatory role in cellular defense against oxidative stress and in senescence
-
-
-
additional information
?
-
P41562
suppression of enzyme activity by small interfering RNA results in impairment of glucose-stimulated insulin secretion, attenuates glucose-induced increments in pyruvate cycling activity and in NADPH levels, and causes increases in lactate production
-
-
-
additional information
?
-
P48735
NADP+-dependent isocitrate dehydrogenase may play an important role in regulating the apoptosis induced by heat shock
-
-
-
additional information
?
-
-
NADP+-dependent isocitrate dehydrogenase may play an important role in regulating the apoptosis induced by TNF-alpha and anticancer drugs
-
-
-
additional information
?
-
-
NADP+-dependent isocitrate dehydrogenase plays an important protective role in apoptosis of HL-60 cells induced by singlet oxygen
-
-
-
additional information
?
-
-
IDPm expression in HepG2 cells regulates ethanol-induced toxicity
-
-
-
additional information
?
-
O75874
the R132H mutant IDH1 directly converts 2-oxoglutarate to 2-hydroxyglutarate, that rapidly accumulates in the medium of cells expressing R132H mutant IDH1
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
poor cofactor
NADP+
-
-
NADP+
-
-
NADP+
Pinus spp.
-
-
NADP+
-
Arg314 and the aromatic ring of Tyr316 are important for affinity to the cofactor and catalysis, interaction with 2'-phosphate group of NADP+
NADP+
-
binding of 1 mol NADP+ per enzyme subunit, His309 is highly important for cofactor binding, HIs315 is involved, while His319 is not
NADP+
-
dependent on
NADP+
-
absolutely specific for, forward reaction
NADP+
-
specific for
NADP+
-
preferred cofactor
NADP+
-
specific for, no activity with NAD+
NADP+
Q8X277
-
NADP+
-
dependent on
NADP+
-
binding site structure, interaction with the 2'-phosphate group of the ribose moiety
NADP+
-
essential
NADP+
-
required by both isoforms ICD-1 and ICD-2
NADP+
B2ZAA4
the recombinant IDH displays a 62000fold (kcat/Km) preference for NADP+ over NAD+ with Mn2+, and a 85000fold greater specificity for NADP+ than NAD+ with Mg2+
NADP+
A5U813, O53611
;
NADP+
-
dependent on
NADP+
O75874, P48735
;
NADP+
P50216
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
NADP+
D7RIE8
dependent on
NADP+
Q9HLV8
no activity when NAD+ up to 2 mM
NADP+
J9Q6L4
-
NADP+
Q4DG65, Q4E4L7
;
NADP+
-
dependent on
NADP+
-
purified recombinant MaIDH is completely specific with NADP+, and no NAD+-dependent activity is detectable
NADPH
-
absolutely specific for, reverse reaction
NADPH
-
;
NADPH
-
-
additional information
-
no activity with NAD+ and NADH
-
additional information
-
no activity with NADH
-
additional information
-
NAD+ may not replace NADP+
-
additional information
Q4DG65, Q4E4L7
the enzyme is completely inactive with NAD+; the enzyme is completely inactive with NAD+
-
additional information
-
SdIDH displays a 19000-32000fold (kcat/Km) preference for NADP+ over NAD+ with Mn2+ and Mg2+, respectively
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
divalent metal ion is required, binding structure and conformation at the isocitrate-metal-binding site
Ca2+
-
structure of IDH1 with bound Ca2+, overview
Cd2+
-
absolute requirement for divalent cations
Cd2+
-
absolute requirement for divalent cations
Cd2+
-
absolute requirement for divalent cations
Co2+
-
absolute requirement for divalent cations
Co2+
-
absolute requirement for divalent cations
Co2+
-
absolute requirement for divalent cations
Co2+
-
can substitute for Mg2+ by 25%
Co2+
-
dependent on divalent metal ions
KCl
-
the activity of the enzyme is markedly dependent on the concentration of NaCl or KC1 in the Tris/EDTA/Mg2+ buffer, being maximal in 0.5 M NaCl or KCl. The stimulatory effect of KCl is greater than that of NaCl
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
Pinus spp.
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
required for activity
Mg2+
-
requirement for divalent cations
Mg2+
-
dependent on divalent metal ions, preferred metal ion
Mg2+
Q8X277
-
Mg2+
-
divalent metal ion is required, binding structure and conformation at the isocitrate-metal-binding site
Mg2+
-
-
Mg2+
-
divalent cation is required, optimal activity at 40 mM in the forward reaction, and at 250 mM in the reverse reaction
Mg2+
-
divalent cation is required, optimal activity at 2 mM in the forward reaction, and at 200 mM in the reverse reaction
Mg2+
-
both isoforms ICD-1, ICD-2, saturation at 10 mM
Mg2+
B2ZAA4
the recombinant IDH displays a 85000fold greater specificity for NADP+ than NAD+ with Mg2+
Mg2+
-
activates; activates
Mg2+
-
activates
Mg2+
P50216
required
Mg2+
-
required
Mg2+
Q4DG65, Q4E4L7
activates; activates
Mg2+
-
activates, about 50% activity compared to Mn2+, SdIDH displays a 19000-32000fold (kcat/Km) preference for NADP+ over NAD+ with Mn2+ and Mg2+, respectively
Mg2+
-
can partially substitute for Mn2+
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
required, not bound normally
Mn2+
-
can substitute for Mg2+ by 90%
Mn2+
-
requirement for divalent cations, preferred metal ion
Mn2+
-
dependent on divalent metal ions
Mn2+
-
required
Mn2+
P41562
-
Mn2+
-
divalent cation is required, optimal activity at 10 mM in the forward reaction, and at 50 mM in the reverse reaction
Mn2+
-
divalent cation is required, optimal activity at 1 mM in the forward reaction, and at 20 mM in the reverse reaction
Mn2+
-
as Mn2+-isocitrate complex, Ser95, Asn97, and Thr78 are involved in binding
Mn2+
-
wild-type, Km-value 0.00033 mM
Mn2+
P56574
Km-value: 0.42 mM for enzyme from normoxic heart, 0.15 mM for enzyme from ischemic heart; KM-value for enzyme from normoxic heart, 0.42 mM, for enzyme from ischemic heart 0.15 mM
Mn2+
B2ZAA4
the recombinant IDH displays a 62000fold (kcat/Km) preference for NADP+ over NAD+ with Mn2+
Mn2+
-
activates
Mn2+
P9WKL1
required
Mn2+
Q4DG65, Q4E4L7
activates, preferred divalent cation; activates, preferred divalent cation
Mn2+
-
activates, preferred cation, SdIDH displays a 19000-32000fold (kcat/Km) preference for NADP+ over NAD+ with Mn2+ and Mg2+, respectively
Na+
-
can substitute for Mg2+ by 20%
NaCl
-
the activity of the enzyme is markedly dependent on the concentration of NaCl or KC1 in the Tris/EDTA/Mg2+ buffer, being maximal in 0.5 M NaCl or KCl. The stimulatory effect of KCl is greater than that of NaCl
Ni2+
-
absolute requirement for divalent cations
Zn2+
-
absolute requirement for divalent cations
Zn2+
-
absolute requirement for divalent cations
Zn2+
-
absolute requirement for divalent cations
Zn2+
-
absolute requirement for divalent cations
Zn2+
-
isoform ICD-1, can replace Mg2+, saturation at 10 mM
Zn2+
-
a zinc ion is tightly bound to Asp301, Asp305, Asp277 in the active site of subunit A and subunit B
Mn2+
-
required
additional information
-
K+ cannot substitute for Mg2+
additional information
-
no acitivty of isoforms with Mn2+ or Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2',5'-ADP
-
-
2,3-Butanedione
-
-
2-mercaptoethanol
-
-
2-oxoglutarate
-
substrate inhibition
2-oxoglutarate
-
substrate inhibition
2-oxoglutarate
-
substrate inhibition
2-oxoglutarate
-
substrate inhibition
2-oxoglutarate
-
substrate inhibition
2-oxoglutarate
-
non-competitive inhibitor
2-oxoglutarate
Pinus spp.
-
inhibition by chelating Mg2+
2-oxoglutarate
-
-
2-oxoglutarate
-
92% inhibition at 5 mM
2-oxoglutarate
-
60% inhibition at 1 mM
2-oxoglutarate
-
isozymes ICDH2 and ICDH1, isozyme ICDH2 is more sensitive to negative feedback inhibition by 2-oxoglutarate
2-oxoglutarate
-
50% inhibition of the forward reaction at 1.5 mM, 99% inhibition at 15 mM
2-oxoglutarate
-
50% inhibition of the forward reaction at 1.5 mM, 95% inhibition at 15 mM
2-oxoglutarate
P56574
;
2-oxoglutarate
P9WKL1
noncompetitive versus NADP+
3-morpholinosydnonimine
Q9SRZ6
44% inhibition at 5 mM of leaf and root enzymes
3-phosphoglycerate
-
-
4-hydroxynonenal
-
50% inhibition at 37C, after 1 h at 0.5 mM, lipid peroxidation product, enzyme becomes susceptible to oxidative damage leading to structural alterations, carbonylation
5'-ADP
-
-
5'-ADP
-
non-competitive inhibitor
5'-ADP
Pinus spp.
-
inhibition by chelating Mg2+
adenosine-3',5'-cyclic monophosphate
-
-
ADP
-
15% inhibition at 2 mM
ADP
-
20% inhibition at 1 mM
Ag+
-
decarboxylation of isocitrate and oxalosuccinate
Ag+
-
decarboxylation of isocitrate and oxalosuccinate
ATP
Pinus spp.
-
inhibition by chelating Mg2+
ATP
-
10% inhibition at 2 mM
ATP
-
50% inhibition at 1 mM
Ca2+
-
in presence of 5 mM Mg2+ 6% of maximal activity is remaining
Ca2+
B2ZAA4
4.94% relative activity at 2 mM
Cd2+
-
complete inhibition at 5 mM in presence of 5 mM Mg2+
Cd2+
-
coadministration with oxalomalate results in inhibition of enzyme and glutaredoxin and enhanced susceptibility to apoptosis
Cd2+
-
binds to C379 of enzyme, resulting in loss of activity and structural alterations. Loss of glutaredoxin activity in cells treated with Cd2+ is more pronounced when cells are transfected with enzyme antisense cDNA
Cd2+
-
inhibits the purified enzyme and the enzyme in cells, NADP+ does not protect. No inhibition of IDPc mutant S269S. DNA fragmentation is enhanced in IDPc siRNA-transfected HEK293 cells compared to control cells upon exposure to cadmium
cis-aconitate
-
-
cis-aconitate
-
35% inhibition at 5 mM
cis-aconitate
-
isozyme ICDH1, not isozyme ICDH2
citrate
-
-
citrate
-
-
citrate
-
30% inhibition at 1 mM and 5 mM
citrate
P56574
;
Citric acid
-
50% inhibition at 1 mM
Co2+
-
92% inhibition in presence of 5 mM Mg2+
Co2+
B2ZAA4
46.47% relative activity at 2 mM
Cu2+
-
-
Cu2+
-
-
Cu2+
-
enzyme is completely inhibited at 5 mM in presence of 5 mM Mg2+, organism is a copper-tolerant basidiomycete
Cu2+
B2ZAA4
complete inhibition at 2 mM
Cu2+
-
complete inhibition
Cu2+
-
complete inhibition
Diamide
-
-
Diethylenetriaminepentaacetic acid
-
-
Diphenylchloroarsine
-
-
dithiothreitol
-
-
EDTA
B2ZAA4
complete inhibition at 2 mM
Fe2+
P56574
; the inhibitory effect of the Fe2+ and H2O2 mixture associated with the generation of hydroxyl radicals is lower in enzyme from ischemic heart compared to enzyme from normoxic heart
glutamate
-
80% inhibition of isozyme ICDH2 at 2 mM
glutathione
-
-
glutathione
-
oxidized glutathione leads to enzyme inactivation with simultaneous formation of a mixed disulfide between glutathione and the cysteine residues of enzyme. Enzymical reactivation by glutaredoxin2 in presence of reduced glutathione
glutathione
P56574
;
glutathione disulfide
-
incubation with 5 mM glutathione disulfide for 30 min completely eliminates activity
glyceraldehyde-3-phosphate
-
-
glyoxalate
-
20% inhibition at 1 mM, presence of 1 mM oxaloacetate results in 50% inhibition
glyoxylate
-
plus oxaloacetate
glyoxylate
-
plus oxaloacetate
glyoxylate
-
plus oxaloacetate
glyoxylate
-
plus oxaloacetate
glyoxylate
-
plus oxaloacetate
glyoxylate
-
plus oxaloacetate
glyoxylate
-
18% inhibition at 5 mM, mixed type inhibition together with oxaloacetate, completely at 5 mM each
glyoxylate
P50216
-
GSH
Q9SRZ6
inhibits the leaf enzyme by 40% at 5 mM, but not the root enzyme
GTP
-
10% inhibition at 1 mM
H2O2
P56574
; the inhibitory effect of the Fe2+ and H2O2 mixture associated with the generation of hydroxyl radicals is lower in enzyme from ischemic heart compared to enzyme from normoxic heart
H2O2
Q9SRZ6
affects the root enzyme slightly but not the enzyme from leaves
Hg2+
-
-
HOCl
-
i.e. hypochlorous acid, the HOCl-mediated damage to NADP+-dependent isocitrate dehydrogenase mayesult in perturbation of the cellular antioxidant defense mechanism and subsequently lead to a pro-oxidant condition
HOCl
-
i.e. hypochlorous acid
Isocitrate
-
competitive inhibition of decarboxylation of oxalosuccinate
Isocitrate
-
reverse reaction
Isocitrate
-
50% inhibition of the reverse reaction at 0.1 mM, 97% inhibition at 1.2 mM
Isocitrate
-
70% inhibition of the reverse reaction at 0.1 mM, 99% inhibition at 1.2 mM
Itaconate
-
18% inhibition at 5 mM
K+
B2ZAA4
3.53% relative activity at 2 mM
K+
-
slight inhibition
Li+
-
slight inhibition
lipid hydroperoxide
-
50% inhibition at 37C, after 1 h at 0.05 mM, lipid peroxidation product, enzyme becomes susceptible to oxidative damage leading to structural alterations, carbonylation
malate
P9WKL1
noncompetitive versus NADP+ and isocitrate
Maleate
-
-
malondialdehyde
-
50% inhibition at 37C, after 1 h at 5 mM, lipid peroxidation product, enzyme becomes susceptible to oxidative damage leading to structural alterations, carbonylation
manganese(III) 5,10,15,20-tetrakis(N-methylpyridinium-2-yl)porphyrin
-
a superoxide dismutase mimic, ICD is inactivated by superoxide, but the inactivated enzyme is replaced by de novo protein synthesis
manganese(III) 5,10,15,20-tetrakis(N-methylpyridinium-2-yl)porphyrin
-
a superoxide dismutase mimic
monoiodoacetate
-
-
N-ethylmaleimide
-
-
Na+
B2ZAA4
4.67% relative activity at 2 mM
Na+
-
slight inhibition
NaCl
-
isoform ICD-2, increase in activity in up to 200 mM NaCl. Isoform ICD-1, no influence of NaCl. Above 200 mM, NaCl is inhibitory
NAD+
-
-
NADH
-
noncompetitive
NADP+
-
reverse reaction
NADP+
-
37% inhibition of the reverse reaction at 4.0 mM
NADP+
-
35% inhibition of the reverse reaction at 4.0 mM
NADPH
-
-
NADPH
-
competitive inhibitor
NADPH
-
-
NADPH
-
forward reaction
NADPH
-
42% inhibition of the forward reaction at 0.5 mM
NADPH
-
66% inhibition of the forward reaction at 0.5 mM
NADPH
-
isoform ICD-2, competitive inhibition
NADPH
P9WKL1
product inhibition competitive versus NADP+ and noncompetitive versus isocitrate
NaHCO3
-
28% inhibition of the forward reaction at 10 mM
NaHCO3
-
9% inhibition of the forward reaction at 10 mM
nicotinamide mononucleotide
-
-
oxalate
-
18% inhibition at 5 mM
oxaloacetate
-
-
oxaloacetate
-
-
oxaloacetate
-
41% inhibition at 5 mM, mixed type inhibition together with glyoxylate, completely at 5 mM each
oxaloacetate
-
25% inhibition at 1 mM, presence of 1 mM glyoxalate results in 50% inhibition
oxaloacetate
-
competitive, inhibits the reverse reaction, over 50% inhibition at 1 mM, synergistically with glyoxylate
oxaloacetate
-
18.6% inhibition at 2.5 mM
oxaloacetate
-
15.5% inhibition at 2.5 mM
oxaloacetate
P50216
-
Oxalomalate
-
-
Oxalomalate
-
competitive, coadministration with CD2+ results in inhibition of enzyme and glutaredoxin and enhanced susceptibility to apoptosis
oxalylglycine
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
decarboxylation of isocitrate and oxalosuccinate
peroxynitrite
-
ethanol toxicity is mediated by peroxynitrite and the peroxynitrite-mediated damage to NADP+-dependent isocitrate dehydrogenase and superoxide dismutase may be resulting in the perturbation of the cellular antioxidant defense systems and subsequently lead to a pro-oxidant condition
peroxynitrite
Q9SRZ6
-
Phenarsazines
-
-
Phenylglyoxal
-
-
Phenylmercuric nitrate
-
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
allosteric inhibition. Phosphoenolpyruvate enhances the uncompetitive inhibition of isocitrate lyase by increasing isocitrate, which protects isocitrate dehydrogenase from the inhibition, and contributes to the control through the tricarboxylic acid cycle and glyoxylate shunt
propanetricarboxylate
-
-
pyridoxal 5'-phosphate
-
-
Rb+
-
slight inhibition
S-nitrosoglutathione
Q9SRZ6
; 70.5% inhibtion at 5 mM of the leaf enzyme, 37.3% of the root enzyme
Selenite
-
inactivates IDPm
succinate
-
isozymes ICDH2 and ICDH1
Threo-L-Isocitrate
-
-
trans-aconitate
-
isozyme ICDH1, not isozyme ICDH2
Urea
-
low molecular weight form
Zn2+
-
-
Zn2+
-
complete inhibition at 5 mM in presence of 5 mM Mg2+
Zn2+
B2ZAA4
1.85% relative activity at 2 mM
Zn2+
-
strong inhibition
monoiodoacetate
-
-
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
-
additional information
-
poor inhibition of the forward reaction by 2-oxoglutarate, no inhibition by CO2
-
additional information
-
enzyme is not affected by gamma-aminobutyric acid and succinate
-
additional information
-
AMP is a no inhibitor, no inhibition by glutamate, pyruvate and succinate
-
additional information
-
no inhibition by phosphoenolpyruvate, fructose 1,6-bisphosphate, and pyruvate
-
additional information
-
no inhibition of carboxylation by citrate, pyruvate, succinate, fumarate, malate, glyoxylate, ATP, and ADP
-
additional information
-
no inhibition by glyoxylate
-
additional information
-
ischemia-reperfusion significantly reduces IDPc expression and activity
-
additional information
-
transfection of HeLa cells with an IDPc small interfering RNA decreases activity of IDPc by 80%, enhancing the susceptibility of staurosporine-induced apoptosis reflected by DNA fragmentation, cellular redox status and the modulation of apoptotic marker proteins
-
additional information
-
5 mM glutathione does not noticeably inhibit IDPc activity
-
additional information
-
tumor-derived mutant IDH1 dominantly inhibits the wild-type IDH1 by forming a catalytically inactive heterodimer, resulting in a decrease of cellular 2-oxoglutarate
-
additional information
P9WKL1
product inhibition patterns for ICDH-1, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetic acid
-
mutant Y140T, 106fold activation compared to the wild-type enzyme
cis-aconitate
-
isozyme ICDH2, not isozyme ICDH1
citrate
-
isozymes ICDH2 and ICDH1
ethylamine
-
mutant K212Q, 4fold activation compared to the wild-type enzyme
glutamate
-
-
glutamate
-
160% stimulation of isozyme ICDH1 at 0.3 mM
NaCl
-
isoform ICD-2, increase in activity in up to 200 mM NaCl. Isoform ICD-1, no influence of NaCl. Above 200 mM, NaCl is inhibitory
paraquat
Q6R6M7
administration at 0.01 mM to roots results in remarkable induction of enzyme gene expression and dramatic increase of gene activity
Phenol
-
mutant Y140T, 88fold activation compared to the wild-type enzyme
succinic acid
-
-
Isocitrate
-
isozymes ICDH2 and ICDH1
additional information
-
isozyme IDP3 is inducible by fatty acids, isozyme IDP2 by non-fermentable carbon sources, expression of isozyme IDP1 is constitutive
-
additional information
-
the mitochondrial isozyme is light-inducible, while the cytosolic one is not
-
additional information
-
enzyme is not affected by gamma-aminobutyric acid and succinate
-
additional information
-
applied oxidative stress leads to upregulation of enzyme expression in erythrocytic stages
-
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
-
no effect by trans-aconitate on isozyme ICDH2
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.019
(2R,3S)-isocitrate
-
pH 7.6, 25C, peroxisomes from senecent leaves
0.202
(2R,3S)-isocitrate
-
pH 7.6, 25C, peroxisomes from young leaves
0.017
2-oxoglutarate
-
mitochondrial isozyme, reverse reaction, pH 7.0
0.026
2-oxoglutarate
-
cytosolic isozyme, reverse reaction, pH 7.0
0.13
2-oxoglutarate
-
-
0.2
2-oxoglutarate
-
isozyme IDP2
0.304
2-oxoglutarate
-
pH 6.5, reverse reaction
0.398
2-oxoglutarate
-
pH 6.5, reverse reaction
1.1
2-oxoglutarate
-
recombinant enyme, pH 7.0
1.92
2-oxoglutarate
-
isozyme IDP1
0.2
CO2
-
mitochondrial isozyme, reverse reaction, pH 7.0
1.3
CO2
-
recombinant enyme, pH 7.0
1.6
CO2
-
cytosolic isozyme, reverse reaction, pH 7.0
0.0017
D,L-isocitrate
-
isozyme 2
0.0022
D,L-isocitrate
-
-
0.0026
D,L-isocitrate
-
-
0.0031
D,L-isocitrate
-
isozyme 1
0.0057
D,L-isocitrate
-
Mn2+-dependent reaction
0.0091
D,L-isocitrate
-
-
0.0097
D,L-isocitrate
-
25C assay temperature
0.0125
D,L-isocitrate
-
-
0.0181
D,L-isocitrate
-
70C assay temperature
0.0204
D,L-isocitrate
-
in presence of Mg2+
0.022
D,L-isocitrate
-
Mn2+-dependent reaction
0.033
D,L-isocitrate
-
-
0.059
D,L-isocitrate
-
Mg2+-dependent reaction
0.07
D,L-isocitrate
-
Mg2+-dependent reaction
0.072
D,L-isocitrate
-
-
0.074
D,L-isocitrate
-
-
0.08
D,L-isocitrate
Pinus spp.
-
-
0.118
D,L-isocitrate
-
-
0.028
D-isocitrate
-
Mg2+-dependent reaction, ICDH2
0.04
D-isocitrate
-
recombinant enzyme, pH 8.0, 30C
0.041
D-isocitrate
-
Mg2+-dependent reaction, ICDH1
0.042
D-isocitrate
Q9SRZ6
pH 7.6, 25C, leaf enzyme
0.239
D-isocitrate
Q9SRZ6
pH 7.6, 25C, root enzyme
0.00013
DL-isocitrate
-
pH 7.5, 30C
0.0064
DL-isocitrate
-
mutant T311S, pH 7.4, 25C
0.0065
DL-isocitrate
-
mutant R83K, pH 7.4, 25C
0.0073
DL-isocitrate
-
mutant T311N, pH 7.4, 25C
0.0083
DL-isocitrate
-
pH 7.4, 25C, recombinant mutant H319Q
0.0084
DL-isocitrate
-
pH 7.4, 25C, recombinant wild-type
0.0084
DL-isocitrate
-
wild-type, pH 7.4, 25C
0.0087
DL-isocitrate
-
pH 7.4, 25C, recombinant mutant H315Q
0.01
DL-isocitrate
-
isoform ICD-1, presence of Mg2+, pH 7.5, 25C
0.011
DL-isocitrate
Q8X277
mutant R291S/K343D/Y344I/V350A/Y390P, pH 8.0, 30C
0.0114
DL-isocitrate
-
mutant N328D, pH 7.4, 25C
0.014
DL-isocitrate
-
mutant R83Q, pH 7.4, 25C
0.0154
DL-isocitrate
-
mutant N328S, pH 7.4, 25C
0.0155
DL-isocitrate
-
mutant T311A, pH 7.4, 25C
0.017
DL-isocitrate
P56574
enzyme from ischemic heart, pH 7.8, 25C
0.018
DL-isocitrate
Q8X277
mutant R291S, pH 8.0, 30C
0.02
DL-isocitrate
-
isoform ICD-2, presence of Mg2+, pH 7.5, 25C
0.021
DL-isocitrate
Q4DG65, Q4E4L7
pH and temperature not specified in the publication
0.022
DL-isocitrate
-
isoform ICD-1, presence of Zn2+, pH 7.5, 25C
0.0326
DL-isocitrate
-
with Mg2+, pH 7.5, 50C
0.036
DL-isocitrate
Q8X277
mutant R291S/K343D/Y390P, pH 8.0, 30C; mutant R291S/Y390P, pH 8.0, 30C
0.04
DL-isocitrate
Q8X277
mutant R291S/K343D/Y344I/Y390P, pH 8.0, 30C
0.045
DL-isocitrate
P56574
enzyme from normoxic heart, pH 7.8, 25C
0.054
DL-isocitrate
Q4DG65, Q4E4L7
pH and temperature not specified in the publication
0.105
DL-isocitrate
Q8X277
recombinant, renatured enzyme, pH 8.0
0.108
DL-isocitrate
Q8X277
wild-type, pH 8.0, 30C
0.1243
DL-isocitrate
-
with Mn2+, pH 7.5, 50C
0.0006
Isocitrate
-
pH 7.4, mutant Y140T
0.0007
Isocitrate
-
pH 7.4, mutant Y140E
0.001
Isocitrate
-
pH 8.0, forward reaction
0.004
Isocitrate
-
mitochondrial isozyme, forward reaction, pH 8.0
0.0042
Isocitrate
P54071
pH 7.5, isoenzyme IDP2
0.0052
Isocitrate
-
pH 7.4, mutant Y140F
0.0053
Isocitrate
-
pH 7.4, mutant Y140K
0.0058
Isocitrate
P54071
pH 7.5, isoenzyme IDP1
0.0059
Isocitrate
-
pH 7.4, recombinant mutant Y316F
0.006
Isocitrate
-
cytosolic isozyme, forward reaction, pH 8.0
0.0062
Isocitrate
-
pH 7.4, recombinant mutant K323Q
0.0062
Isocitrate
-
recombinant wild-type IDH1, pH not specified in the publication, temperature not specified in the publication
0.0074
Isocitrate
-
pH 7.4, recombinant wild-type enzyme
0.0075
Isocitrate
-
pH 7.4, wild-type enzyme
0.0075
Isocitrate
-
recombinant wild-type enzyme, pH 7.4, 25C
0.0082
Isocitrate
D7RIE8
recombinant enzyme, pH 7.5, 30C
0.009
Isocitrate
-
pH 8.0, forward reaction
0.009
Isocitrate
Q9UWG7
pH 8.0, 55C, cofactor: NADP+
0.0092
Isocitrate
-
pH 7.4, mutant K212Y
0.0098
Isocitrate
-
pH 7.4, mutant K212Q
0.01
Isocitrate
-
pH 7.4, recombinant mutant K321Q
0.0127
Isocitrate
-
pH 9.0, 30C
0.014
Isocitrate
-
recombinant mutant N97A, pH 7.4, 25C
0.0147
Isocitrate
-
pH 8.0, 28C
0.015
Isocitrate
P41939
pH 7.5, isoenzyme IDP3
0.017
Isocitrate
P56574
pH 7.8, 25C, enzyme from ischemic heart
0.029
Isocitrate
-
-
0.03
Isocitrate
-
isozyme IDP1
0.03
Isocitrate
P41939
pH 7.5, isoenzyme IDP1
0.0405
Isocitrate
-
40C, pH 8.0
0.045
Isocitrate
-
recombinant enyme, pH 9.0
0.045
Isocitrate
P56574
pH 7.8, 25C, enzyme from normoxic heart
0.05
Isocitrate
-
isozyme IDP3
0.05
Isocitrate
P9WKL1
pH 7.5, temperature not specified in the publication, recombinant His-tagged enzyme
0.066
Isocitrate
-
recombinant mutant T78A, pH 7.4, 25C
0.07
Isocitrate
-
chloroplastic isozyme ICDH2, pH 7.8, 25C
0.072
Isocitrate
-
recombinant mutant N97D, pH 7.4, 25C
0.101
Isocitrate
-
recombinant mutant S95A, pH 7.4, 25C
0.116
Isocitrate
-
pH 7.4, mutant K212R
0.13
Isocitrate
-
pH 8.0, 30C, cofactor: NADP+
0.18
Isocitrate
-
cytosolic isozyme ICDH1, pH 7.8, 25C
0.22
Isocitrate
-
isozyme IDP2
0.22
Isocitrate
P41939
pH 7.5, isoenzyme IDP2
0.332
Isocitrate
-
60C, pH 8.0
0.367
Isocitrate
-
recombinant mutant T78D, pH 7.4, 25C
0.3686
Isocitrate
-
recombinant mutant R132C IDH1, pH not specified in the publication, temperature not specified in the publication
0.4341
Isocitrate
-
recombinant mutant R132S IDH1, pH not specified in the publication, temperature not specified in the publication
0.5824
Isocitrate
-
recombinant mutant R132H IDH1, pH not specified in the publication, temperature not specified in the publication
2.07
Isocitrate
-
recombinant mutant S95D, pH 7.4, 25C
0.012
Mg2+
-
Mg2+-dependent reaction, ICDH2
0.013
Mg2+
-
Mg2+-dependent reaction, ICDH1
0.013
Mg2+
-
recombinant enzyme, pH 8.0, 30C
0.0239
Mg2+
-
pH 9.0, 30C
0.12
Mg2+
-
chloroplastic isozyme ICDH2, pH 7.8, 25C
0.125
Mg2+
-
Mg2+-dependent reaction
0.159
Mg2+
-
Mg2+-dependent reaction
0.31
Mg2+
-
cytosolic isozyme ICDH1, pH 7.8, 25C
0.00004
Mn2+
-
pH 7.4, mutant Y140F
0.000084
Mn2+
-
pH 7.4, mutant Y140E
0.00011
Mn2+
-
pH 7.4, wild-type enzyme
0.00011
Mn2+
-
recombinant wild-type enzyme, pH 7.4, 25C
0.0003
Mn2+
-
pH 7.4, recombinant wild-type enzyme
0.00033
Mn2+
-
pH 7.4, 25C, recombinant wild-type
0.00039
Mn2+
-
pH 7.4, 25C, recombinant mutant H319Q
0.0004
Mn2+
-
pH 7.4, recombinant mutant Y316F and K323Q
0.0004
Mn2+
-
recombinant mutant N97A, pH 7.4, 25C
0.0005
Mn2+
-
pH 7.4, recombinant mutant K321Q
0.00091
Mn2+
-
pH 7.4, mutant K212Q
0.0011
Mn2+
-
pH 7.4, mutant K212Y
0.0024
Mn2+
-
recombinant mutant N97D, pH 7.4, 25C
0.0027
Mn2+
-
pH 7.4, 25C, recombinant mutant H315Q
0.0033
Mn2+
-
recombinant mutant T78A, pH 7.4, 25C
0.004
Mn2+
-
Mn2+-dependent reaction
0.0112
Mn2+
-
recombinant mutant S95A, pH 7.4, 25C
0.022
Mn2+
-
recombinant enzyme, pH 8.0, 30C
0.024
Mn2+
-
Mn2+-dependent reaction
0.0288
Mn2+
-
recombinant mutant T78D, pH 7.4, 25C
0.0668
Mn2+
-
recombinant mutant S95D, pH 7.4, 25C
0.08
Mn2+
-
chloroplastic isozyme ICDH2, pH 7.8, 25C
0.131
Mn2+
-
pH 7.4, mutant Y140K
0.21
Mn2+
-
cytosolic isozyme ICDH1, pH 7.8, 25C
0.0179
NAD+
-
wild-type, 25C, pH 7.4
0.0207
NAD+
-
mutant K260R, 25C, pH 7.4
0.0232
NAD+
-
mutant D375N, 25C, pH 7.4
0.0312
NAD+
-
mutant K260Q, 25C, pH 7.4
0.144
NAD+
Q8X277
mutant R291S/K343D/Y344I/V350A/Y390P, pH 8.0, 30C
2.9
NAD+
Q9UWG7
pH 8.0, 55C
8.49
NAD+
B2ZAA4
in 20 mM Tris-HCl (pH 8.0), at 25C, in the presence of 2 mM Mn2+
18.6
NAD+
B2ZAA4
in 20 mM Tris-HCl (pH 8.0), at 25C, in the presence of 2 mM Mg2+
0.000028
NADP+
-
pH 7.5, 30C
0.00042
NADP+
-
pH 7.4, mutant Y140E
0.00046
NADP+
-
pH 7.4, mutant Y140T
0.00051
NADP+
-
pH 7.4, mutant Y140K
0.0012
NADP+
-
recombinant mutant N97D, pH 7.4, 25C
0.0023
NADP+
-
pH 7.4, mutant Y140F
0.0023
NADP+
-
pH 8.0, 28C
0.00242
NADP+
B2ZAA4
in 20 mM Tris-HCl (pH 8.0), at 25C, in the presence of 2 mM Mg2+
0.0025
NADP+
-
-
0.00278
NADP+
B2ZAA4
in 20 mM Tris-HCl (pH 8.0), at 25C, in the presence of 2 mM Mn2+
0.0029
NADP+
-
pH 9.0, 30C
0.003
NADP+
-
isozyme 2
0.003
NADP+
-
mitochondrial isozyme, forward reaction, pH 8.0
0.0037
NADP+
P54071
pH 7.5, isoenzyme IDP2
0.004
NADP+
-
cytosolic isozyme, forward reaction, pH 8.0
0.0043
NADP+
-
mutant T311N, pH 7.4, 25C
0.0044
NADP+
Q9SRZ6
pH 7.6, 25C, leaf enzyme
0.0049
NADP+
-
recombinant mutant N97A, pH 7.4, 25C
0.0051
NADP+
-
pH 7.4, 25C, recombinant mutant H319Q
0.0051
NADP+
-
recombinant mutant S95A, pH 7.4
0.0053
NADP+
-
recombinant mutant T78A, pH 7.4, 25C
0.0055
NADP+
-
mutant T373S, 25C, pH 7.4
0.0056
NADP+
-
pH 7.4, 25C, recombinant wild-type
0.0056
NADP+
-
wild-type, pH 7.4, 25C
0.0056
NADP+
P54071
pH 7.5, isoenzyme IDP1
0.006
NADP+
-
Mn2+-dependent raction
0.0062
NADP+
-
mutant T373A, 25C, pH 7.4
0.0063
NADP+
-
isozyme 1
0.0068
NADP+
-
recombinant mutant R132C IDH1, pH not specified in the publication, temperature not specified in the publication
0.007
NADP+
-
Mg2+-dependent reaction, ICDH2
0.007
NADP+
-
pH 8.0, forward reaction
0.0073
NADP+
-
-
0.0073
NADP+
-
pH 7.4, mutant K212Y
0.0073
NADP+
-
recombinant wild-type IDH1, pH not specified in the publication, temperature not specified in the publication
0.0075
NADP+
-
Mg2+-dependent reaction, ICDH1
0.0077
NADP+
-
pH 7.4, recombinant mutant K323Q
0.008
NADP+
-
pH 7.4, recombinant mutant Y316F and K321Q
0.0088
NADP+
-
wild-type, 25C, pH 7.4
0.009
NADP+
-
pH 7.4, recombinant wild-type enzyme
0.0097
NADP+
-
mutant T311S, pH 7.4, 25C
0.0099
NADP+
-
pH 7.4, wild-type enzyme
0.0099
NADP+
-
recombinant wild-type enzyme, pH 7.4, 25C
0.01
NADP+
-
-
0.01
NADP+
Pinus spp.
-
-
0.01
NADP+
P41939
pH 7.5, isoenzyme IDP3
0.0102
NADP+
-
in presence of Mg2+
0.0108
NADP+
-
recombinant mutant T78D, pH 7.4, 25C
0.011
NADP+
-
-
0.012
NADP+
-
Mg2+-dependent reaction
0.012
NADP+
-
mutant T373V, 25C, pH 7.4
0.0122
NADP+
-
recombinant mutant R132H IDH1, pH not specified in the publication, temperature not specified in the publication
0.014
NADP+
-
pH 7.4, mutant K212Q
0.0144
NADP+
-
recombinant mutant R132S IDH1, pH not specified in the publication, temperature not specified in the publication
0.015
NADP+
P9WKL1
pH 7.5, temperature not specified in the publication, recombinant His-tagged enzyme
0.0154
NADP+
-
mutant K374Q 25C, pH 7.4
0.0165
NADP+
-
25C assay temperature
0.0165
NADP+
-
60C, pH 8.0
0.017
NADP+
-
pH 8.0, forward reaction
0.018
NADP+
-
pH 7.4, mutant K212R
0.02
NADP+
-
isozyme IDP2 and IDP3
0.02
NADP+
P41939
pH 7.5, isoenzyme IDP2
0.0203
NADP+
-
mutant R83K, pH 7.4, 25C
0.0237
NADP+
-
recombinant mutant S95D, pH 7.4, 25C
0.0246
NADP+
-
mutant N328D, pH 7.4, 25C
0.027
NADP+
-
recombinant enyme, pH 9.0
0.0274
NADP+
-
-
0.03
NADP+
-
isozyme IDP1
0.03
NADP+
P41939
pH 7.5, isoenzyme IDP1
0.031
NADP+
-
70C assay temperature
0.032
NADP+
-
Mg2+-dependent reaction
0.032
NADP+
-
pH 7.4, recombinant mutant Y316L
0.0324
NADP+
-
with Mg2+, pH 7.5, 50C
0.0378
NADP+
-
mutant K260R, 25C, pH 7.4
0.0392
NADP+
-
40C, pH 8.0
0.0444
NADP+
-
pH 8.0, 70C
0.045
NADP+
Q4DG65, Q4E4L7
pH and temperature not specified in the publication
0.046
NADP+
P56574
enzyme from ischemic heart, pH 7.8, 25C; enzyme from normoxic heart, pH 7.8, 25C; pH 7.8, 25C, enzyme from ischemic heart; pH 7.8, 25C, enzyme from normoxic heart
0.05
NADP+
-
Mn2+-dependent reaction
0.053
NADP+
-
-
0.0552
NADP+
-
pH 8.0, 70C, Km-value for NAD+ is about 140fold higher than the KM-value for NADP+
0.056
NADP+
Q4DG65, Q4E4L7
pH and temperature not specified in the publication
0.0616
NADP+
Q9SRZ6
pH 7.6, 25C, root enzyme
0.0675
NADP+
D7RIE8
recombinant enzyme, pH 7.5, 30C
0.0717
NADP+
-
with Mn2+, pH 7.5, 50C
0.0749
NADP+
-
mutant T311A, pH 7.4, 25C
0.08
NADP+
-
chloroplastic isozyme ICDH2, pH 7.8, 25C
0.0811
NADP+
-
mutant R83Q, pH 7.4, 25C
0.085
NADP+
Q9UWG7
pH 8.0, 55C
0.09
NADP+
-
recombinant enzyme, pH 8.0, 30C
0.092
NADP+
-
pH 7.4, recombinant mutant R314Q
0.093
NADP+
Q8X277
recombinant, renatured enzyme, pH 8.0
0.101
NADP+
Q8X277
wild-type, pH 8.0, 30C
0.11
NADP+
-
pH 8.0, 30C
0.111
NADP+
Q9HLV8
60C, pH 7.5
0.119
NADP+
-
mutant N328S, pH 7.4, 25C
0.125
NADP+
-
isoform ICD-1, presence of Mg2+, pH 7.5, 25C
0.133
NADP+
-
mutant D375N, 25C, pH 7.4
0.17
NADP+
-
cytosolic isozyme ICDH1, pH 7.8, 25C
0.203
NADP+
Q8X277
mutant R291S/K343D/Y390P, pH 8.0, 30C
0.218
NADP+
-
pH 7.4, 25C, recombinant mutant H315Q
0.25
NADP+
-
mutant K260Q, 25C, pH 7.4
0.282
NADP+
Q8X277
mutant R291S/K343D/Y344I/Y390P, pH 8.0, 30C
0.327
NADP+
Q8X277
mutant R291S/Y390P, pH 8.0, 30C
0.35
NADP+
Q8X277
mutant R291S, pH 8.0, 30C
19.6
NADP+
-
isoform ICD-2, presence of Mg2+, pH 7.5, 25C
0.009
NADPH
-
mitochondrial isozyme, reverse reaction, pH 7.0
0.0092
NADPH
-
-
0.01
NADPH
-
isozyme IDP1
0.01
NADPH
-
pH 6.5, reverse reaction
0.024
NADPH
-
cytosolic isozyme, reverse reaction, pH 7.0
0.034
NADPH
-
pH 6.5, reverse reaction
0.04
NADPH
-
isozyme IDP2
11.68
NaHCO3
-
pH 6.5, reverse reaction
13.82
NaHCO3
-
pH 6.5, reverse reaction
0.56
oxalosuccinate
-
reductase
1.2
oxalosuccinate
-
decarboxylase
25 - 26
oxalosuccinate
-
decarboxylase
0.252
Mn2+
-
pH 7.4, mutant K212R
additional information
additional information
-
measurement methods, the maltose binding fusion protein of the recombinant enzymes alters the kinetic parameters, overview
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics of isozymes IDP1 and IDP2
-
additional information
additional information
P9WKL1
steady-state kinetics, kinetic mechanism of ICDH-1, overview
-
additional information
additional information
-
Km-values of wild-type and chimeric enzymes
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Q4DG65, Q4E4L7
kinetics, overview; kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
138
D-isocitrate
-
recombinant enzyme, pH 8.0, 30C
0.0005
DL-isocitrate
Q8X277
mutant R291S/Y390P, pH 8.0, 30C
0.0013
DL-isocitrate
Q8X277
mutant R291S/K343D/Y390P, pH 8.0, 30C
0.002
DL-isocitrate
Q8X277
mutant R291S, pH 8.0, 30C
0.0023
DL-isocitrate
Q8X277
wild-type, pH 8.0, 30C
0.0025
DL-isocitrate
Q8X277
mutant R291S/K343D/Y344I/Y390P, pH 8.0, 30C
0.005
DL-isocitrate
Q8X277
mutant R291S/K343D/Y344I/V350A/Y390P, pH 8.0, 30C
1.9
DL-isocitrate
-
isoform ICD-1, presence of Zn2+, pH 7.5, 25C
3.8
DL-isocitrate
-
isoform ICD-1, presence of Mg2+, pH 7.5, 25C
10.29
DL-isocitrate
-
with Mg2+, pH 7.5, 50C
19.6
DL-isocitrate
-
isoform ICD-2, presence of Mg2+, pH 7.5, 25C
43.21
DL-isocitrate
-
with Mn2+, pH 7.5, 50C
4.5
Isocitrate
Q6AQ66
5C
31.4
Isocitrate
Q6AQ66
25C
33
Isocitrate
P9WKL1
pH 7.5, temperature not specified in the publication, recombinant His-tagged enzyme
58.3
Isocitrate
-
oxidative decarboxylation
106.4
Isocitrate
-
40C, pH 8.0
0.0007
NAD+
Q8X277
mutant R291S/K343D/Y344I/V350A/Y390P, pH 8.0, 30C
0.03
NAD+
-
mutant D375N, 25C, pH 7.4
0.47
NAD+
-
mutant K260Q, 25C, pH 7.4
0.5
NAD+
-
mutant K260R, 25C, pH 7.4
0.76
NAD+
-
wild-type, 25C, pH 7.4
1.37
NAD+
B2ZAA4
in 20 mM Tris-HCl (pH 8.0), at 25C, in the presence of 2 mM Mn2+
2.11
NAD+
B2ZAA4
in 20 mM Tris-HCl (pH 8.0), at 25C, in the presence of 2 mM Mg2+
0.0003
NADP+
Q8X277
mutant R291S/K343D/Y344I/Y390P, pH 8.0, 30C
0.001
NADP+
Q8X277
mutant R291S/Y390P, pH 8.0, 30C
0.0024
NADP+
Q8X277
mutant R291S/K343D/Y390P, pH 8.0, 30C
0.003
NADP+
Q8X277
wild-type, pH 8.0, 30C
0.004
NADP+
Q8X277
mutant R291S, pH 8.0, 30C
1.7
NADP+
-
mutant K260Q, 25C, pH 7.4
4
NADP+
-
isoform ICD-1, presence of Mg2+, pH 7.5, 25C
4.5
NADP+
Q6AQ66
5C
5.7
NADP+
-
mutant K260R, 25C, pH 7.4
8.4
NADP+
-
mutant D375N, 25C, pH 7.4
23.2
NADP+
B2ZAA4
in 20 mM Tris-HCl (pH 8.0), at 25C, in the presence of 2 mM Mg2+
25.36
NADP+
-
with Mg2+, pH 7.5, 50C
27.6
NADP+
B2ZAA4
in 20 mM Tris-HCl (pH 8.0), at 25C, in the presence of 2 mM Mn2+
31.4
NADP+
Q6AQ66
25C
32.2
NADP+
-
wild-type, 25C, pH 7.4
33
NADP+
P9WKL1
pH 7.5, temperature not specified in the publication, recombinant His-tagged enzyme
37.4
NADP+
-
isoform ICD-2, presence of Mg2+, pH 7.5, 25C
48.88
NADP+
-
with Mn2+, pH 7.5, 50C
88.1
NADP+
-
40C, pH 8.0
138
NADP+
-
recombinant enzyme, pH 8.0, 30C
219
NADP+
-
60C, pH 8.0
255
Isocitrate
-
60C, pH 8.0
additional information
additional information
-
turnover numbers of wild-type and chimeric enzymes
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00335
DL-isocitrate
-
with Mg2+, pH 7.5, 50C
849
0.00348
DL-isocitrate
-
with Mn2+, pH 7.5, 50C
849
700
Isocitrate
-
60C, pH 8.0
279
0.00613
NADP+
-
with Mn2+, pH 7.5, 50C
10
0.00787
NADP+
-
with Mg2+, pH 7.5, 50C
10
2200
NADP+
-
40C, pH 8.0
10
13300
NADP+
-
60C, pH 8.0
10
2600
Isocitrate
-
40C, pH 8.0
279
additional information
additional information
-
turnover numbers of wild-type and chimeric enzymes
0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
2-oxoglutarate
P56574
enzyme from normoxic heart, pH 7.8, 25C; pH 7.8, 25C,enzyme from normoxic heart
0.127
2-oxoglutarate
-
pH 9.0, 30C
0.25
2-oxoglutarate
P56574
enzyme from ischemic heart, pH 7.8, 25C; pH 7.8, 25C,enzyme from ischemic heart
1
2-oxoglutarate
-
above, cytosolic isozyme, forward reaction, pH 8.0; above, mitochondrial isozyme, forward reaction, pH 8.0
0.159
citrate
P56574
enzyme from normoxic heart, pH 7.8, 25C; pH 7.8, 25C, enzyme from normoxic heart
0.28
citrate
P56574
enzyme from ischemic heart, pH 7.8, 25C; pH 7.8, 25C,enzyme from ischemic heart
0.05
Fe2+
P56574
enzyme from ischemic heart, pH 7.8, 25C; enzyme from normoxic heart, pH 7.8, 25C; pH 7.8, 25C,enzyme from ischemic heart; pH 7.8, 25C, enzyme from normoxic heart
0.15
glutathione
P56574
enzyme from normoxic heart, pH 7.8, 25C; pH 7.8, 25C, enzyme from normoxic heart
0.45
H2O2
P56574
enzyme from normoxic heart, pH 7.8, 25C; pH 7.8, 25C, enzyme from normoxic heart
1.63
H2O2
P56574
enzyme from ischemic heart, pH 7.8, 25C; pH 7.8, 25C,enzyme from ischemic heart
0.005
Isocitrate
-
mitochondrial isozyme, reverse reaction, pH 7.0
0.012
Isocitrate
-
cytosolic isozyme, reverse reaction, pH 7.0
8
NAD+
-
pH 7.4, versus NADPH, recombinant mutant R314Q
11
NAD+
-
pH 7.4, versus NADPH, recombinant wild-type enzyme and mutant Y316L
12
NAD+
-
pH 7.4, versus NADPH, recombinant mutant Y316F
0.06
NADH
-
mitochondrial isozyme, forward reaction, pH 8.0
0.08
NADH
-
cytosolic isozyme, forward reaction, pH 8.0
0.006
NADP+
-
mitochondrial isozyme, reverse reaction, pH 7.0
0.021
NADP+
-
cytosolic isozyme, reverse reaction, pH 7.0
0.0046
NADPH
-
isoform ICD-2, pH 7.5, 25C
0.005
NADPH
-
mitochondrial isozyme, forward reaction, pH 8.0
0.007
NADPH
-
cytosolic isozyme, forward reaction, pH 8.0
0.35
oxaloacetate
-
recombinant enzyme, pH 7.0
0.31
phosphoenolpyruvate
-
pH 7.1
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.003
-
purified recombinant mutant K212Y, forward reaction
0.0046
-
purified chloroplastic isozyme ICDH1
0.038
-
mitochondria from etiolated leaves, forward reaction at pH 7.5
0.038
-
purified cytosolic isozyme ICDH1
0.04
-
purified enzyme, reverse reaction
0.04
-
pH 7.5, 65C, cell extract
0.06
-
purified recombinant mutant S95D
0.065
-
purified recombinant mutant K212Q, forward reaction
0.072
-
mitochondria from green leaves, forward reaction at pH 7.5
0.08
-
purified recombinant mutant Y140E, forward reaction
0.083
-
purified recombinant mutant Y140T, forward reaction
0.102
-
purified recombinant mutant Y140F, forward reaction
0.179
-
purified recombinant mutant Y140K, forward reaction
0.24
-
enzyme extract of cells in stationary growth phase
0.26
-
enzyme extract of cells in growth phase with acid synthesis
0.28
-
purified enzyme, forward reaction
0.3
-
enzyme extract of cells in exponential growth phase
0.44
-
purified recombinant mutant N97D
0.75
-
cell free enzyme extracts of cells grown on glucose, best carbon source
3 - 8
P56574
-
3.16
-
purified recombinant mutant K212R, forward reaction
4.1
-
purified recombinant mutant H315Q
5.29
-
purified recombinant mutant N97A
6.22
-
purified recombinant mutant T78D
7
-
purified recombinant mutant Y316L
7.18
-
purified recombinant mutant S95A
12.7
-
purified recombinant mutant T78A
18.1
-
purified recombinant mutant R314Q
18.5
-
NAD+-linked reaction
18.6
-
ICDH2
18.6
-
wild-type epidydymal fat pad
20.1
-
purified recombinant mutant H319Q
23
-
NADP+-linked reaction
23.7
Q8X277
purified recombinant enzyme
27.2
-
purified enzyme
33.5
-
-
34.6
-
purified enzyme
35.1
-
purified recombinant wild-type enzyme, forward reaction
35.1
-
purified recombinant wild-type enzyme
36
-
purified recombinant enzyme
37.8
-
purified recombinant wild-type enzyme
38.6
-
purified recombinant wild-type enzyme
38.7
-
purified recombinant mutant K323Q
39.6
-
purified recombinant mutant K321Q
40
-
pH 8.0, 30C
40.3
-
purified recombinant mutant Y316F
50
-
transgenic mice epidydymal fat pad
67
Q4DG65, Q4E4L7
purified recombinant N-terminally His6-tagged enzyme, pH and temperature not specified in the publication
75
-
purified enzyme
77.4
-
wild-type liver
108.2
-
transgenic mice liver
152
Q9UWG7
pH 8.0, 55C
162
-
purified recombinant enzyme
219
Q4DG65, Q4E4L7
purified recombinant N-terminally His6-tagged enzyme, pH and temperature not specified in the publication
additional information
-
wild-type and diverse mutant strains
additional information
-
activity in cell free enzyme extracts of cells grown on diffeent carbon sources
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.1
-
reverse reaction
6.3 - 6.5
-
reverse reaction, cytosolic isozyme
6.5 - 9
P54071
more than 90% of optimal Vmax, isoenzyme IDP2
6.5
-
assay at, reverse reaction
6.6
-
2-oxoglutarate + CO2 + NADPH
6.7
-
reverse reaction
6.8 - 7
-
reverse reaction, mitochondrial isozyme
7
-
reverse reaction
7.2 - 8.2
-
-
7.2
-
assay at
7.3
P41562
assay at
7.4
-
-
7.5 - 9.5
-
-
7.5
-
high molecular weight form
7.5
-
isozyme IDP2, forward reaction
7.5
-
both isoforms ICD-1, ICD-2
7.5
P41939
isoenzyme IDP2
7.5
-
assay at; assay at
7.5
D7RIE8
assay at
7.5
P9WKL1
assay at
7.5
-
with Mn2+ or Mg2+
7.5
-
assay at
7.6 - 8
-
isoenzyme I
7.6
Q9SRZ6
assay at
7.8 - 7.9
-
isozymes ICDH2 and ICDH1
7.8
-
isocitrate + NADP+
7.9 - 8.4
-
-
8 - 8.6
-
isoenzyme II
8 - 9
-
forward reaction, cytosolic and mitochondrial isozymes
8
-
low molecular weight form
8
Q8X277
assay at
8
-
isozyme IDP1, forward reaction
8
P41939
isoenzyme IDP1
8
-
assay at
8
-
assay at
8
Q9UWG7
assay at
8
-
assay at
8.1
-
forward reaction
8.3
-
forward reaction
8.5
-
assay at
8.5
P54071
isoenzyme IDP1
8.5
P41939
isoenzyme IDP3
8.5
B2ZAA4
in the presence of 2 mM Mn2+
9
-
forward reaction
9
B2ZAA4
in the presence of 2 mM Mg2+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
-
5 - 8
-
pH-profile of wild-type and alanine-substituted mutant enzymes
5.5 - 9
-
80% of maximal activity in the pH range of pH 7.0-9.0
5.5 - 9.5
-
activity range
5.5
-
isoform ICD-1, 30% of maximum activity, isoform ICD-2, 10% of maximum activity
5.6 - 8.5
-
-
5.8 - 7.5
Q9HLV8
three-fold reduction in activity when the pH is shifted from the pH-optimum at 7.5 to pH 5.8
6 - 9.5
-
-
6.3 - 7.8
-
-
6.5 - 10
-
-
6.5 - 9
P54071
pH 6.5: about 60% of maximal activity, pH 9.0: about 70% of maximal activity, isoenzyme IDP1
6.5 - 9
P41939
pH 6.5: about 40% of maximal activity, pH 9.0: about 70% of maximal activity, isoenzyme IDP3
7 - 11
-
activity range, profile overview
7 - 8
P41939
pH 7.0: about 60% of maximal activity, pH 8.0: about 40% of maximal activity, isoenzyme IDP2
7 - 9
P41939
pH 7.0: about 60% of maximal activity, pH 9.0: about 95% of maximal activity, isoenzyme IDP1
7.5 - 10
-
-
9.5
-
isoform ICD-1, 90% of maximum activity, isoform ICD-2, less than 40% of maximum activity
additional information
-
pH-profile, recombinant wild-type and mutant enzymes
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
isoform ICD-2
20
-
isoenzyme II
22
P41562
assay at room temperature
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
forward reaction, assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
27
-
assay at
28
-
assay at
30
-
assay at
30
D7RIE8
assay at
37
-
reverse reaction, assay at
40
-
isoenzyme I
40
-
isoform ICD-1
40
P56574
enzyme from ischemic heart
40
-
assay at
45
Q9SRZ6
root enzyme
46
B2ZAA4
around 46C
50
P56574
enzyme from normoxic heart
50
-
assay at
55
Q9UWG7
assay at
60
Q9SRZ6
leaf enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
-
activity range, profile overview
25 - 50
P56574
25C: about 50% of maximal activity, 50C: about 70% of maximal activity, enzyme from ischemic heart
25 - 55
-
temperature dependency analysis of the different phenotypes
25 - 60
-
activity range
35 - 70
P56574
35C: about 45% of maximal activity, 70C: about 60% of maximal activity, enzyme from normoxic heart
50 - 80
Q9HLV8
50C: about 50% of maximal activity, 80C: about 65% of maximal activity
60
-
isoform ICD-1, 40% residual activity, ICD-2, 5% residual activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
Q8X277
calculated
4.9
-
isoelectric focusing
5.2
-
isoelectric focusing, isoenzyme ICDH-4
5.4
-
isoelectric focusing, isoenzyme ICDH-3
5.5
-
isozyme IDP2
5.6
-
isoelectric focusing, isoenzyme ICDH-2
6
-
isoelectric focusing
6
-
isoelectric focusing, isoenzyme ICDH-1
6.5
-
IDP2, isoelectric focusing
6.54
J9Q6L4
sequence calculation
7.4
-
IDPA, isoelectric focusing
8.2
-
IDP1, isoelectric focusing
8.5
-
isozyme IDP1
8.9
-
IDP3, isoelectric focusing
10
-
isozyme IDP3
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Pinus spp.
-
-
Manually annotated by BRENDA team
-
epididymal fat pad
Manually annotated by BRENDA team
-
epididymal fat pad, hepatic fat pad
Manually annotated by BRENDA team
J9Q6L4
high expression level
Manually annotated by BRENDA team
O75874
of secondary glioblastomas
Manually annotated by BRENDA team
-
IDH1, diffuse gliomas graded II-IV
Manually annotated by BRENDA team
O75874
of grade II-III gliomas
Manually annotated by BRENDA team
-
progressive gliomas
Manually annotated by BRENDA team
P56574
regulation of enzyme during heart ischemia. Ischemia results in increase in enzyme activity, enzyme from ischemic heart mitochondria demonstrates higher activation energy and lower thermal stability and differs in KM-value and regulation, increase of enzyme activity in the cytosol and mitochondria of ischemic heart
Manually annotated by BRENDA team
-
sensitizing effect of IDPm siRNA on the apoptotic cell death of HeLa cells
Manually annotated by BRENDA team
-
silencing of NADP+-dependent isocitrate dehydrogenase expression in HeLa cells greatly enhances apoptosis induced by heat shock
Manually annotated by BRENDA team
P41562
pancreatic islet beta-cell, suppression of enzyme activity by small interfering RNA results in impairment of glucose-stimulated insulin secretion, attenuates glucose-induced increments in pyruvate cycling activity and in NADPH levels, and causes increases in lactate production
Manually annotated by BRENDA team
-
IDPc expression and activity is highest in the cortex, modest in the outer medulla and lowest in the inner medulla, IDPc is also highly expressed in the mitochondrion-rich intercalatal cells of the collecting duct
Manually annotated by BRENDA team
-
green and etiolated
Manually annotated by BRENDA team
J9Q6L4
low expression level
Manually annotated by BRENDA team
-
young and senescent
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia ecotype
-
-
-
Manually annotated by BRENDA team
Capsicum annuum CMS-9704A
-
low expression level
-
Manually annotated by BRENDA team
P54071
isoenzyme IDP1, isoenzyme IDP2
Manually annotated by BRENDA team
J9Q6L4
high expression level
Manually annotated by BRENDA team
J9Q6L4
moderate expression level
Manually annotated by BRENDA team
Capsicum annuum CMS-9704A
-
moderate expression level
-
Manually annotated by BRENDA team
J9Q6L4
very low expression level
Manually annotated by BRENDA team
Capsicum annuum CMS-9704A
-
very low expression level
-
Manually annotated by BRENDA team
Q6R6M7
a remarkable induction of ICDH gene expression and a dramatic increase of the ICDH activity is observed during the paraquat treatment. ICDH has a key role in NADPH recycling under oxidative stress conditions in pea root nodules
Manually annotated by BRENDA team
J9Q6L4
high expression level
Manually annotated by BRENDA team
Capsicum annuum CMS-9704A
-
high expression level
-
Manually annotated by BRENDA team
J9Q6L4
low expression level
Manually annotated by BRENDA team
Capsicum annuum CMS-9704A
-
low expression level
-
Manually annotated by BRENDA team
-
NADP+-dependent isocitrate dehydrogenase may play an important role in regulating the apoptosis induced by ionizing radiation
Manually annotated by BRENDA team
Pinus spp.
-
-
Manually annotated by BRENDA team
additional information
-
growth-associated specific activity profile, dextrose or fructose are preferred before lactose as sole carbon source
Manually annotated by BRENDA team
additional information
-
isozyme tissue distribution of isozyme ICD1, overview
Manually annotated by BRENDA team
additional information
P41562
RT-PCR and immunohistochemical analysis of brain cells, overview
Manually annotated by BRENDA team
additional information
Q4DG65, Q4E4L7
expression levels of the cytosolic isoform are significantly increased in amastigotes, metacyclic trypomastigotes and cell-derived trypomastigotes compared to epimastigotes
Manually annotated by BRENDA team
additional information
Saccharopolyspora erythraea CA340
-
growth-associated specific activity profile, dextrose or fructose are preferred before lactose as sole carbon source
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isozyme ICDH2, minor form
Manually annotated by BRENDA team
-
86% of total activity in the cell, main factor for synthesis of 2-oxoglutarate. Enzyme and cytoplasmic aspartate aminotransferase are regulated oppositely and the catalytic activity of one enzyme can be stimulated concurrently with a decrease in the activity of the other
Manually annotated by BRENDA team
Pinus spp.
-
-
Manually annotated by BRENDA team
P41562
isozyme cICDH
Manually annotated by BRENDA team
-
isozyme ICDH1, major form
Manually annotated by BRENDA team
P56574
increase in enzyme activity during ischemia
Manually annotated by BRENDA team
-
cytosolic isozyme IDPc, subcellular localization study, overview
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
O75874
isozyme IDH1
Manually annotated by BRENDA team
Q4DG65, Q4E4L7
IDH2 contains a C-terminal PTS1 signal, but this enzyme is mostly localized in the cytosol, expression levels of the cytosolic isoform are significantly increased in amastigotes, metacyclic trypomastigotes and cell-derived trypomastigotes compared to epimastigotes
Manually annotated by BRENDA team
Rhodopseudomonas palustris 285
-
-
-
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia ecotype
-
isozyme cICDH
-
Manually annotated by BRENDA team
Staphylococcus aureus ATCC12600
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae MMY011
-
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
-
Manually annotated by BRENDA team
Q4DG65, Q4E4L7
IDH2 contains a C-terminal PTS1 signal, but this enzyme is mostly localized in the cytosol of epimastigotes
Manually annotated by BRENDA team
Azotobacter sp.
-
-
Manually annotated by BRENDA team
-
isozyme ICD1, mainly
Manually annotated by BRENDA team
-
light-inducible isozyme
Manually annotated by BRENDA team
P56574
increase in enzyme activity during ischemia, enzyme from ischemic heart mitochondria demonstrates higher activation energy and lower thermal stability and differs in KM-value and regulation
Manually annotated by BRENDA team
P54071
isoenzyme IDP1
Manually annotated by BRENDA team
-
mitochondrial NADP+-dependent isocitrate dehydrogenase
Manually annotated by BRENDA team
Q4DG65, Q4E4L7
mitochondrial targeting peptide signal is predicted for IDH1
Manually annotated by BRENDA team
-
isozyme ICD1, minor appearance
Manually annotated by BRENDA team
-
IDP3 contains a canonical type I peroxisomal targeting sequence, a carboxyl-terminal Cys-Lys-Leu tripeptide. IDP3 is normally strictly peroxisomal
Manually annotated by BRENDA team
Capsicum annuum CMS-9704A
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae MMY011
-
IDP3 contains a canonical type I peroxisomal targeting sequence, a carboxyl-terminal Cys-Lys-Leu tripeptide. IDP3 is normally strictly peroxisomal
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae MMY011
-
IDP1
-
Manually annotated by BRENDA team
additional information
-
immunohistochemical determination of the subcellular distribution of isozyme ICD1 in different tissues, overview
-
Manually annotated by BRENDA team
additional information
-
influence of subcellular localization on isozyme activities, overview
-
Manually annotated by BRENDA team
additional information
P41562
subcellular RT-PCR and immunohistochemical analysis of brain cells, overview
-
Manually annotated by BRENDA team
additional information
P54071
the mouse isoenzyme IDP2 colocalizes in cytosol and peroxisomes when expressed in yeast
-
Manually annotated by BRENDA team
additional information
-
subcellular localization study of isozymes, overview
-
Manually annotated by BRENDA team
additional information
Saccharomyces cerevisiae MMY011
-
subcellular localization study of isozymes, overview
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Bacillus subtilis (strain 168)
Burkholderia pseudomallei (strain 1710b)
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Desulfotalea psychrophila (strain LSv54 / DSM 12343)
Desulfotalea psychrophila (strain LSv54 / DSM 12343)
Desulfotalea psychrophila (strain LSv54 / DSM 12343)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Rhizobium meliloti (strain 1021)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
-
PAGE
286789
45000
-
SDS-PAGE
698059
47000
-
SDS-PAGE
695502
53000
-
gel filtration
286786
54200
P33197
calculated from amino acid sequence
696823
55000
-
PAGE
286788
60000 - 70000
-
gel filtration
286779
60000
-
PAGE
286793
60000
-
PAGE and gel filtration
286809
61000 - 64000
-
ultracentrifugation
286749
64400
-
gel filtration
656740
68000
-
gel filtration
286782
68000
-
dimer, analytical ultracentrifugation
727835
69100
-
gel filtration
656740
70000
-
gel filtration
286806
70000
-
gel filtration
723151
70000
-
analytical ultracentrifugation
727835
72000
B2ZAA4
gel filtration
696488
75000 - 80000
-
gel filtration
286779
75000 - 80000
-
PAGE
286802
80000
-
gel filtration
286779
80000
-
gel filtration
286808
80000
-
gel filtration
286811
80000
-
native PAGE
655430
80000
B2ZAA4
SDS-PAGE
696488
81000 - 83000
-
gel filtration
286782
81000
-
gel filtration
655430
82000
-
recombinant mutant Y316F, dynamic light scattering
654341
85000
-
gel filtration, isoenzyme I: dimer
286787, 286791
85000
-
Guinier analysis
696416
86000
-
gel filtration
286784
86000
-
recombinant wild-type enzyme, dynamic light scattering
654341
87000 - 92600
-
gel filtration
286779
87000
-
recombinant mutants K321Q and R314Q, dynamic light scattering
654341
87000
-
recombinant mutant N97A, native PAGE
657309
90000 - 100000
-
gel filtration
286779
90000
-
gel filtration, low molecular weight form
286781
90000
-
gel filtration, ultracentrifugation, PAGE
286783, 286785
90000
-
gel filtration, 3 isoenzymes
286792
90000
-
gel filtration
286794
90000
-
gel filtration
286796
90000
-
gel filtration
286798
90000
-
recombinant maltose binding fusion proteins, wild-type and mutant enzymes, gel filtration
654649
90000
-
recombinant enzyme, gel filtration
655456
92000
-
recombinant wild-type and mutant enzymes, native PAGE
656180
94000
-
recombinant mutant T78A, native PAGE
657309
95000
Pinus spp.
-
gel filtration
286805
97000
-
recombinant mutant N97D, native PAGE
657309
97900
-
recombinant mutant Y316L, native PAGE at pH 5.5
654341
98000
-
recombinant mutant T78D, native PAGE
657309
99800
-
recombinant wild-type enzyme, native PAGE at pH 5.5
654341
100000
-
gel filtration, main peak, isoform ICD-1
668080
101000
-
recombinant mutant S95A, native PAGE
657309
104000
-
recombinant wild-type enzyme and mutant S95D, native PAGE
657309
105000
-
gel filtration
286782
105000
-
gel filtration
723152
107000
-
gel filtration
286799
108000
-
gel filtration
286803
115000
-
gel filtration
655035
117000
-
gel filtration, ICDH1
286810
130000
-
native PAGE
655094
136000
-
gel filtration, ICDH2
286810
174000
-
tetramer, analytical ultracentrifugation
727835
180000
-
gel filtration, isoform ICD-2
668080
200000
-
gel filtration, isoform ICD-1
668080
320000
-
gel filtration, isoform ICD-2
668080
360000
-
gel filtration, high molecular weight form
286781
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 48000, SDS-PAGE
?
-
x * 46000, SDS-PAGE
?
D7RIE8
x * 40000, SDS-PAGE
?
-
x * 45000, isozyme ICD1, SDS-PAGE
?
Q8X277
x * 45837, sequence calculation, x * 60000, recombinant, renatured enzyme, SDS-PAGE
?
-
x * 46381, isozyme IDP1, mass spectrometry, x * 46562, isozyme IDP2, mass spectrometry, x * 47856, isozyme IDP3, mass spectrometry
?
P41562
x * 47000, approximately, cytosolic and mitochondrial isozymes, SDS-PAGE
?
-
x * 46300, SDS-PAGE
?
-
x * 45000, recombinant N-terminally His6-tagged enzyme, SDS-PAGE
?
J9Q6L4
x * 46705 , sequence calculation
?
Capsicum annuum CMS-9704A
-
x * 46705 , sequence calculation
-
?
Staphylococcus aureus ATCC12600
-
x * 40000, SDS-PAGE
-
dimer
Q9UWG7
2 * 45000, SDS-PAGE
dimer
-
2 * 47000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
dimer
-
2 * 62000, SDS-PAGE
dimer
-
alpha2, 2 * 40000, SDS-PAGE
dimer
-
alpha2, 2 * 30500, SDS-PAGE
dimer
-
isoenzyme I
dimer
-
alpha2, 2 * 48000, SDS-PAGE
dimer
Pinus spp.
-
alpha2, 2 * 46000, SDS-PAGE
dimer
-
alpha2, 2 * 53000, SDS-PAGE
dimer
-
alpha2, 2 * 42000, SDS-PAGE
dimer
-
alpha2, 2 * 45000, SDS-PAGE
dimer
-
alpha2, 2 * 57000, SDS-PAGE
dimer
-
2 * 43000, recombinant wild-type and mutant enzymes, SDS-PAGE
dimer
-
2 * 46600, recombinant thrombin cleaved wild-type and mutant enzymes, SDS-PAGE
dimer
-
2 * 51000, about, recombinant enzyme, SDS-PAGE
dimer
-
residues Arg314, Tyr316, Lys321, and Arg323 are not involved in subunit interaction
dimer
-
wild-type and mutant enzymes, circular dichroism and native PAGE
dimer
-
2 * 49000, isoform ICD-1, 2 * 86000, isoform ICD-2, SDS-PAGE. Besides dimers, isoform ICD-1 forms some tetramer, ICD-2 forms trimer
dimer
-
and tetramer, crystallization data and analytical ultracentrifugation
dimer
A5U813, O53611
isoform ICD1, X-ray crystallography
dimer
-
2 * 45400, equilibrium of dimeric and tetrameric species, calculated from sequence
dimer
-
dissociation from dimer to monomer at pH 3.0
dimer
Q8X277
the enzyme is a dimer at high salt concentration. Deactivation due to incubation of the enzyme at low NaCl concentrations is related to irreversible dissociation of the active dimeric species towards a monomer
dimer
Aeropyrum pernix DSM 11879
-
dissociation from dimer to monomer at pH 3.0
-
dimer
Vibrio sp. ABE-1
-
isoenzyme I
-
dimer
Sulfolobus solfataricus DSM 1616
-
2 * 45000, SDS-PAGE
-
dimer
Saccharopolyspora erythraea CA340
-
2 * 60000, SDS-PAGE
-
dimer
Thermotoga maritima DSM 3109
-
2 * 45400, equilibrium of dimeric and tetrameric species, calculated from sequence
-
dimer
Thermoleophilum minutum YS-4
-
alpha2, 2 * 30500, SDS-PAGE
-
dimer
Haloferax volcanii DSM 3757
-
2 * 62000, SDS-PAGE
-
homodimer
-
-
homodimer
-
2 * 46200, estimated from amino acid sequence
homodimer
-
2 * 52600
homodimer
P9WKL1
each subunit has a Rossmann fold, and a common top domain of interlocking beta sheets
homodimer
-
2 * 47900, calculated from sequence
homodimer
Aeropyrum pernix DSM 11879
-
2 * 47900, calculated from sequence
-
homodimer
-
2 * 52600
-
homodimer
-
each subunit has a Rossmann fold, and a common top domain of interlocking beta sheets
-
monomer
-
1 * 80000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
monomer
-
isoenzyme II, 1 * 85000, SDS-PAGE
monomer
-
1 * 80000
monomer
P50216
1 * 80000
monomer
B2ZAA4
1 * 72000, gel filtration
monomer
A5U813, O53611
isoform ICD2, X-ray crystallography
monomer
-
dissociation from dimer to monomer at pH 3.0
monomer
Aeropyrum pernix DSM 11879
-
dissociation from dimer to monomer at pH 3.0
-
monomer
Streptomyces diastaticus M1033
-
1 * 80000, SDS-PAGE
-
monomer
Vibrio sp. ABE-1
-
isoenzyme II, 1 * 85000, SDS-PAGE
-
monomer
Vibrio parahaemolyticus Y-4
-
1 * 80000, SDS-PAGE
-
tetramer
-
4 * 49000, isoform ICD-1, SDS-PAGE. Main form is dimer for isoform ICD-1
tetramer
-
and dimer, crystallization data and analytical ultracentrifugation
tetramer
-
4 * 45400, equilibrium of dimeric and tetrameric species, calculated from sequence
tetramer
Thermotoga maritima DSM 3109
-
4 * 45400, equilibrium of dimeric and tetrameric species, calculated from sequence
-
trimer
-
and dimer, 3 * 86000, SDS-PAGE and chemical crosslinking, isoform ICD-2
monomer
Streptomyces lividans TK54
-
1 * 72000, gel filtration
-
additional information
-
enzyme has 3 different conformational stages
additional information
O75874
exchange of Arg132 to His affects the conformation equilibrium and the reorganization of the active-site. Also, not only the expected loss of key salt-bridge interactions between the guanidinium of R132 and the alpha/beta carboxylates of isocitrate, as well as changes in the network that coordinates the metal ion, but also an unexpected reorganization of the active-site, structure analyis, overview
additional information
J9Q6L4
prediction and analysis of structures and conserved domains of pepper NADP-ICDH containing 172 alpha helices, 84 extended strands, 32 beta turn, and 127 random coils, homology modeling, overview
additional information
P9WKL1
three-dimensional structure of Mtb ICDH-1, overview
additional information
Capsicum annuum CMS-9704A
-
prediction and analysis of structures and conserved domains of pepper NADP-ICDH containing 172 alpha helices, 84 extended strands, 32 beta turn, and 127 random coils, homology modeling, overview
-
additional information
-
three-dimensional structure of Mtb ICDH-1, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glutathionylation
-
Cys269 of IDPc is a target for S-glutathionylation, this modification is reversed by dithiothreitol as well as enzymatically by cytosolic glutaredoxin in the presence of glutathione. Glutathionylated IDPc is significantly less susceptible than native protein to peptide fragmentation by reactive oxygen species and proteolytic digestion. Glutathionylation may play a protective role in the degradation of protein through the structural alterations of IDPc.
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 20C
-
hanging drop vapour diffusion technique with reservoir solution consisting of 0.6 M ZnSO4 and 0.1 M Na cacodylate, pH 6.3
-
crystallization with polyethylene glycol 2000 monomethyl ether
-
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
P50216
substrate/cofactor-free structure in presence of Mg2+ shows a distinct open conformation and suggests the presence of low-energy conformers
-
crystals of native DpIDH are obtained by the sitting-drop, vapour-diffusion method. The crystals are grown at 8C. Crystals of DpIDH in complex with isocitrate (DpIDH-iso) are obtained by the hanging drop method at 8 C
Q6AQ66
hanging drop vapour diffusion method, purified recombinant His-tagged enzyme in complex with NADP+: equal volume of protein solution, containing 15 mg/ml enzyme, 20 mM Tris-HCl, pH 7.4, 100 mM NaCl, and 10 mM NADP+, and of reservoir solution, containing 100 mM MES, pH 6.5, 12% PEG 20000, at 4C, purified recombinant His-tagged enzyme in complex with NADP+, isocitrate and Ca2+: equal volume of protein solution, containing 15 mg/ml enzyme, 20 mM Tris-HCl, pH 7.4, 100 mM NaCl, and 10 mM NADP+, 10 mM DL-isocitrate and 10 mM CaCl2, and of reservoir solution, containing 100 mM MES, pH 5.9, 20% PEG 6000, at 20C, X-ray diffraction structure determination and analysis
-
purified ICDH-1 in complex with NADPH at Mn2+, hanging drop vapor diffusion method, 0.001 ml of protein in 5 mM NADPH, and 5 mM MnCl2 is mixed with 0.001 ml of reservoir solution containing 30% PEG 2000 and 0.1 M Tris-HCl, pH 8.0, room temperature, X-ray diffraction structure determination and analysis at 2.18 A resoltuion
P9WKL1
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 20C using the hanging-drop vapor diffusion method
-
20 mg/ml purified recombinant wild-type and selenomethionine enzyme, complexed with Mn2+ and isocitrate, 4C, hanging drop vapour diffusion method, for the wild-type enzyme: 0.002 ml of enzyme solution containing 0.1 M triethanolamine chloride, pH 7.7, 0.15 M Na2SO4, 8 mM DL-isocitrate, 4 mM MnSO4, plus equal volume of 20% PEG 6000, 3% glycerol, against 0.75 ml reservoir solution containing 0.1 M triethanolamine chloride, pH 7.7, 0.15 M Na2SO4, 8 mM DL-isocitrate, 4 mM MnSO4, and 40% w/v xylitol, for the selenomethionine enzyme: 0.002 ml of enzyme solution containing 0.1 M triethanolamine chloride, pH 7.7, 0.15 M Na2SO4, 8 mM DL-isocitrate, plus equal volume of 18% PEG 6000, 3% glycerol, against 0.75 ml reservoir solution containing 0.1 M triethanolamine chloride, pH 7.7, 0.15 M Na2SO4, and 18% PEG 6000, 7-10 days, X-ray diffraction structure determination and analysis at 2.7 A resolution, modeling
-
in complex with Mn2+ and isocitrate
-
dimeric apoform
-
sitting and hanging drop vapour diffusion method, using 100 mM cacodylate and 1.4 M sodium acetate, 10 mM citric acid , and 10 mM MnCl2, at pH 6.5-7.8 and 25C
P33197
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
Q9HLV8
1 h, 60C, enzyme retains 91% of its activity
722204
6 - 9
-
-
286779
6
-
-
286788
8 - 10
-
-
286796
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
-
isoenzyme II
286791
20
-
isoenzyme II
286787
30
-
50% loss of activity in 1 h
286779
30
-
purified recombinant enzyme, 20 min, stable
723152
35
-
isoenzyme C, half-life 20 min
286792
38 - 50
B2ZAA4
about 50% of IDH activity is preserved at 38C after 20 min of incubation, the enzyme is inactive at 50C
696488
40
-
nearly no activity at 40C or lower
286798
40
-
purified enzyme, 20 min, stable up to 40C
723151
40
-
purified recombinant enzyme, 20 min, loss of 50% of enzyme activity, with Mg2+
723152
45
-
-
286784
45
-
-
286796
45
-
after 10 min completely inactivated in absence of substrate
286806
45
-
purified recombinant enzyme, 20 min, loss of 50% of enzyme activity, with Mn2+
723152
47
-
purified enzyme, 20 min, loss of 50% activity
723151
49
-
isoenzyme A, half-life 20 min
286792
50
-
fully stable
286799
50
-
5 min, complete loss of activity
656740
50
-
t1/2: 24.2 min
722205
50
-
purified enzyme, 20 min, inactivation
723151
52
-
isoenzyme C, half-life 20 min, presence of isocitrate
286792
54
-
50% loss of activity in 1 h
286779
54
-
isoenzyme B, T50-value
286792
58
-
isoenzyme A, T50-value, presence of isocitrate
286792
60
Q8X277
recombinant enzyme, 93% remaining activity after 117 h, in presence of 3 M NaCl
655604
60
Q9HLV8
pH 5, enzyme retains 91% of its activity
722204
65
-
30 min, isoform ICD-1, irreversible thermal inactivation, isoform ICD-2, renaturation of inactivated protein by slow cooling till 55C
668080
65
-
t1/2: 167 min
722205
69
-
isoenzyme B, T50-value, presence of isocitrate
286792
70 - 80
-
stable
726802
70
-
-
286780
70
-
after 1 h incubation retains 57% of initial activity
286809
70
Q6AQ66
melting temperature is 66.9C
688373
70
Q9HLV8
half-life: 88 min
722204
70
-
t1/2: 106 min
722205
74
-
10 min, 50% loss of activity, mutant enzyme A336F
727545
75
Q9HLV8
half-life: 24 min
722204
80
-
no loss in activity
286798
80
Q8X277
recombinant enzyme, inactivation within 2.5 min, in presence of 3 M NaCl
655604
82
Q9HLV8
melting temperature at pH 7.5 is 82.2C
722204
85
Q9HLV8
melting temperature at pH 5.8 is 84.5C
722204
88
-
50% loss of activity in 1 h
286779
88
-
10 min, 50% loss of activity, wild-type enzyme and mutant enzyme Y309I/I310L
727545
89
-
10 min, 50% loss of activity, mutant enzyme I321L
727545
90
-
half life of 22 min in 50 mM tricine-KOH buffer, pH 8
286808
91
-
10 min, 50% loss of activity, mutant enzyme A325P/G326S
727545
98
-
the Tm-value is 98.3C
727835
110
-
the Tm-value is 109.9C
727835
additional information
-
the enzyme is incubated in Tris/EDTA/Mg2+ buffer containing either 0.5 M or 3 M KCl. The thermal stability of the enzyme is substantially reduced at the lower KCl concentration, with concomitant differences in the activation energies for the thermal inactivation process. Omission of Mg2+ from the incubation buffer greatly accelerates the rate of loss of activity, and its presence plus that of 3 M KCl are recommended for storage of the enzyme
719515
additional information
-
thermal stability of wild-type and chimeric enzymes
722205
additional information
-
thermal denaturation is an irreversible process
727835
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
low molecular weight form of Acinetobacter calcoaceticus enzyme more heat stable than high molecular weight form
-
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
-
stabilization by dithiothreitol
-
Mg2+ stabilizes the enzyme during purification
-
3 M NaCl stabilizes the recombinant enzyme
Q8X277
enzyme stability is mainly sensitive to cations and very little or not sensitive to anions. Divalent cations induce a strong shift of the active/inactive transition towards low salt concentration. Deactivation due to incubation of the enzyme at low NaCl concentrations is related to irreversible dissociation of the active dimeric species towards a monomer, which can be described as an extended inactive monomeric species
Q8X277
with a residual amount of secondary structure
Q8X277
instable in solutions of low ionic strength, stabilization by ammonium sulfate
-
instable in solutions of low ionic strength, stabilization by ammonium sulfate
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
isozyme IDP3 shows highest defense against endogeneous oxidative stress
-
654367
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, several months, under oxic conditions
-
-20C, 6 months, 10% loss of activity
-
2C, several weeks
-
-18C, purified enzyme, 50% glycerol, stable for at least 1.5-2 months
-
-80C, partially purified cytosolic and mitochondrial isozymes, several months, stable
-
-18C, purified enzyme, 50% glycerol, stable for at least 1.5-2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged IDPA from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
wild-type and mutant enzymes
-
41fold by ultracentrifugation, ammonium sulfate fractionation, gel filtration and ion exchange chromatography, and desalting
-
recombinant enzyme from Escherichia coli by ion exchange and gel filtration to homogeneity, 1.84fold
-
His-tagged enzyme is purified by TALON resin column chromatography, ICDH fused maltose-binding protein is purified by amylose resin chromatography
-
672fold to homogeneity
-
native enzyme by PEG fractionation, affinity and hydrophobic interaction chromatography
-
recombinant solubilized enzyme by ultrafiltration, and DEAE ion exchange chromatography, 6.4fold
Q8X277
Ni-NTA column chromatography
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged mutant enzymes C269S and C379S from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant IDH1s from Escherichia coli by nickel affinity chromatography
-
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta (DE3) by metal affinity chromatography
-
recombinant N-terminally His6-tagged enzyme by nickel affinity chromatography and gel filtration
P9WKL1
-
Pinus spp.
-
cytosolic and mitochondrial isozymes
-
recombinant soluble enzyme from Escherichia coli
-
NADP-isocitrate dehydrogenase from the normoxic and ischemic rat myocardium
P56574
native isozymes, partially
P41562
partially, isozyme ICD1
-
by ultracentrifugation, ammonium sulfate fractionation, gel filtration and ion exchange chromatography, and desalting
-
recombinant His-tagged isozymes IDP1 and IDP2 by nickel affinity chromatography
-
isozymes ICDH1, 172fold, and ICDH2, 31fold, by ammonium sulfate fractionation, desalting, DEAE ion exchange and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain DH5alpha by nickel affinity chromatography
D7RIE8
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta (DE3)
-
TALON metal affinity resin column chromatography
B2ZAA4
recombinant enzyme variants fused to the maltose binding fusion protein, from Escherichia coli, to homogeneity by amylose affinity, and ion exchange chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli, cleavage of the fusion proteins by thrombin, to homogeneity by amylose affinity chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli, to homogeneity
-
recombinant wild-type and mutant enzymes from Escherichia coli, to homogeneity by amylose affinity chromatography, thrombin digestion, and DEAE ion exchange chromatography
-
recombinant wild-type and mutant maltose binding fusion proteins from Escherichia coli by amylose affinity and size exclusion chromatography
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography; recombinant N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
Q4DG65, Q4E4L7
strain ABE-1
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene At1g65930
Q9SRZ6
isozyme cICDH is encoded by a single gene
-
expression of His-tagged IDPA in Escherichia coli strain BL21(DE3), expression of IDPA inm Saccharomyces cerevisiae, it behaves similar to the yeast IDP2 harboring a type I peroxisomal targeting sequenceand occurs in cytosol and peroxisomes, complementation study in Saccharomyces cerevisiae disruption mutants expressing the full-length IDPA enzyme from Aspergillus nidulans, and IDPA lacking the mitochondrial targeting sequence and containing a different PTS1, which results in the same expression level and subcellular orientation, subcellular localization study, overview
-
2 polymorphic isozymes IDHP-A and IDHP-B, isozymes show allelic variants in populations belonging to different living heights in the stream, analysis of allelic frequencies, overview
-
expression in Escherichia coli
-
expression of the gene in Escherichia coli by connecting it with the T7 promoter
-
wild-type and mutant enzymes are expressed in Escherichia coli
-
gene NADP-ICDH, DNA and amino acid sequence determination and analysis, phylogenetic tree
J9Q6L4
construction of a genomic cDNA library, gene Cl-idh, DNA sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
-
IDCH gene, DNA and amino acid sequence determination by combinated PCR and screening of genomic lambda EMBL3 library, and sequence analysis, overexpression in Escherichia coli BL21(DE3) as insoluble protein in inclusion bodies
Q8X277
expressed in Escherichia coli
-
expressed in HeLa cells
-
expression of C-terminally His-tagged enzyme in Escherichia coli BL21(DE3)
-
expression of His-tagged mutant enzymes C269S and C379S in Escherichia coli
-
expression of myc-tagged wild-type IDH1 and R132H mutant IDH1 in U-87MG glioblastoma cells
O75874
expression of the IDH1R132H mutant at a level similar to the endogenous protein in the cytoplasm of glioblastoma U-87MG cells causes a dose-dependent reduction of 2-oxoglutarate levels. Overexpression of the IDH1R132H mutant in U-87MG cells stimulates expression of HIF-1alpha target genes. Overexpression of wild-type IDH1 reduces HIF-1alpha protein levels in HeLa and U-87MG cells. Expression of FLAG-tagged wild-type and R132 mutants IDH1 in HEK-293T cells and of His-tagged enzymes in Escherichia coli
-
gene idh1, expression of Myc-tagged wild-type and Myc-tagged mutant enzymes in HEK-293T cells
-
genotyping in diverse cancer cell lines, overview
-
IDH1, genotyping and genomic profile, overview
-
IDH1, genotyping in acute myelogenous leukemia patients, overview; IDH2, genotyping in acute myelogenous leukemia patients, overview
-
gene icd, sequence comparisons, expression of His6-tagged in Escherichia coli strain Rosetta (DE3)
-
expressed in Hep-G2 cells
-
expression in Escherichia coli or Saccharomyces cerevisiae; expression of mouse isoenzyme IDP2 in Escherichia coli or Saccharomyces cerevisiae. Mouse enzyme can compensate for loss of yeast cytosolic IDP2 and of peroxisomal IDP3IDP3. Removal of the peroxisomal targeting signal of the mouse enzyme precludes both localization in peroxisomes and compensation for loss of yeast IDP3
P54071
expression of the cDNA in a construct of nucleotides 1-1714 with rat PEPCK promotor and the SV-40 polyadenylation signal, permanant expression in 3T3-L1 cells and in transgenic mice, the latter are constructed by infection of fertilized eggs
-
gene Rv3339c, expression of N-terminally His6-tagged enzyme
P9WKL1
expression in Escherichia coli
-
NADP+-ICDH contains two different translational ATG start sites, fusion of mitochondrial and chloroplastic targeting signals to YFP reporter, and transient expression in Nicotiana tabacum using Agrobacterium tumefaciens transfection method. The chloroplast-tageting signal constructs are localizes in the chloroplast, while the mitochondrial constructs are localized in either in mitochondria and chloroplasts, due to an 50 amino acid additional part that is added in expression in cultivars Xanthi and Petit Havana
O65853
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
-
gene of mitochondrial isozyme, DNA and amino acid sequence determination and analysis, subcellular RT-PCR analysis of brain cells
P41562
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
-
gene idh, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain DH5alpha
D7RIE8
SdIDH, sequence comparisons, expression of His6-tagged enzyme in Escherichia coli strain Rosetta (DE3)
-
expressed in Escherichia coli Rosetta (DE3) cells
B2ZAA4
expression in Escherichia coli as maltose binding fusion protein, wild-type and selenomethionine enzyme variants
-
expression of wild-type and mutant enzymes in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli as maltose binding fusion proteins
-
expression of wild-type and mutant enzymes in Escherichia coli as maltose-binding fusion proteins
-
expression of wild-type and mutant enzymes in Escherichia coli TB1 as maltose binding fusion proteins
-
expressed in Escherichia coli BL21
Q9HLV8
expressed in Escherichia coli strain MV1190
P33197
gene Tc00.1047053506925.319 or IDH2, recombinant expression of the N-terminally His6-tagged enzyme in Escherichia coli; gene Tc00.1047053511575.60 or IDH1, recombinant expression of the N-terminally His6-tagged enzyme in Escherichia coli, co-expression with bacterial GroEL/GroES chaperones is required for IDH1 in order to achieve a soluble enzyme
Q4DG65, Q4E4L7
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transfection of HeLa cells with siRNA leading to decreased activity of IDPm and enhanced susceptibility of the cells to selenite-induced apoptosis, overview
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
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
A325P/G326S
-
50% inactivation after 10 min at 91.3C as compared to 87.5C for wild-type enzyme
A336F
-
50% inactivation after 10 min at 74C as compared to 87.5C or wild-type enzyme
I321L
-
50% inactivation after 10 min at 88.9C as compared to 87.5C for wild-type enzyme
Y309I/I310L
-
50% inactivation after 10 min at 88.4C as compared to 87.5C for wild-type enzyme
Y309I/I310L/I321L/A325P/G326S
-
50% inactivation after 10 min at 90C as compared to 87.5C for wild-type enzyme
C201M
-
higher affinity for NAD+ than for NADP+
C201N
-
higher affinity for NAD+ than for NADP+
C201V
-
higher affinity for NAD+ than for NADP+
S113E
-
affinity for isopropylmalate is 37-fold compared to wild-type
R291S
Q8X277
involved in coenzyme specificity
R291S/K343D/Y344I/V350A/Y390P
Q8X277
switch in coenzyme specificity from NADP+ to NAD+
R291S/K343D/Y344I/Y390P
Q8X277
involved in coenzyme specificity
R291S/K343D/Y390P
Q8X277
involved in coenzyme specificity
R291S/Y390P
Q8X277
involved in coenzyme specificity
C269S
-
activity of the C269S mutant is not affected by glutathione disulfide and no glutathionylated IDPc is observed with 5 mM glutathione disulfide confirming that Cys269 is a target of IDPc glutathionylation
C269S
-
site-directed mutagenesis, is not sensitive to inhibition by Cd2+ in contrast to the wild-type enzyme
C379S
-
glutathionylation of the C379S mutant is similar to that of wild type enzyme
C379S
-
site-directed mutagenesis, is inhibited by Cd2+ in a similar manner to the wild-type
R132C
-
IDH1 R132 mutations cause production and accumulation of 2-hydroxyglutarate in acute myelogenous leukemia cells. The mutation reduces the affinity for isocitrate, and increases the affinity for NADPH and 2-oxoglutarate, preventing the oxidative decarboxylation of isocitrate to 2-oxoglutarate, and facilitating the conversion of 2-oxoglutarate to 2-hydroxyglutarate
R132C
-
naturally occuring IDH1 mutation
R132C
-
naturally occuring mutation C394T, genotyping in glioma samples, overview
R132C
-
naturally occuring mutation of IDH1 in melanoma metastasis of the lung
R132C
-
naturally occuring mutation of IDH1, results in 60fold increased Km for isocitrate compared to the wild-type IDH1
R132G
-
IDH1 R132 mutations cause production and accumulation of 2-hydroxyglutarate in acute myelogenous leukemia cells
R132G
-
naturally occuring IDH1 mutation
R132G
-
naturally occuring mutation C394G, genotyping in glioma samples, overview
R132H
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R132H
-
IDH1 R132 mutations cause production and accumulation of 2-hydroxyglutarate in acute myelogenous leukemia cells
R132H
-
naturally occuring IDH1 mutation
R132H
O75874
naturally occuring mutant of IDH1, the mutation causes loss in binding affinity for both isocitrate and MgCl2 along with a 1000fold decrease in catalytic turnover. The mutant IDH1 directly converts 2-oxoglutarate to 2-hydroxyglutarate, that rapidly accumulates in the medium of cells expressing R132H mutant IDH1, metabolite profiling in comparison to the wild-type IDH1, overview. Mutation to histidine results in a significant shift in position of the highly conserved residues Y139 from the A subunit and K212' from the B subunit both of which are thought to be critical for catalysis by this enzyme family. exchange of Arg132 to His affects the conformation equilibrium and the reorganization of the active-site. Also, not only the expected loss of key salt-bridge interactions between the guanidinium of R132 and the alpha/beta carboxylates of isocitrate, as well as changes in the network that coordinates the metal ion, but also an unexpected reorganization of the active-site, structure analyis, overview
R132H
-
naturally occuring mutation G395A, genotyping in glioma samples, overview
R132H
-
naturally occuring mutation in myelodysplastic syndrome preceding acute myeloid leukemia. R132H alteration can be detected by immunohistochemistry using R132H mutation-specific antibodies, overview
R132H
-
naturally occuring mutation of IDH1, results in 94fold increased Km for isocitrate compared to the wild-type IDH1
R132L
-
naturally occuring IDH1 mutation
R132L
-
naturally occuring mutation G395T, genotyping in glioma samples, overview
R132S
-
naturally occuring IDH1 mutation
R132S
-
naturally occuring mutation C394A, genotyping in glioma samples, overview
R132S
-
naturally occuring mutation of IDH1, results in 70fold increased Km for isocitrate compared to the wild-type IDH1
R132V
-
naturally occuring IDH1 mutation
R132X
-
identification of frequent IDH1 mutations in grade II and IV diffuse gliomas reducing the produciton of NADPH. Forced expression of mutant IDH1 in cultured cells reduces formation of the enzyme product, 2-oxoglutarate, and increases the levels of hypoxia-inducible factor subunit HIF-1alpha, a transcription factor that facilitates tumor growth when oxygen is low and whose stability is regulated by 2-oxoglutarate. IDH1 normally functions as a homodimer, we hypothesized that the mutant IDH1 molecules in tumor cells form heterodimers with wild-type molecules and, in so doing, dominantly inhibit the activity of wild-type IDH1
R132X
-
naturally occuring mutation of IDH1 in metastatic brain tumors
R172K
-
IDH2 R172 mutation causes production and accumulation of 2-hydroxyglutarate in acute myelogenous leukemia cells
D375N
-
15fold increase in KM-value for NADP+, marked decrease of Vmax-value
H309F
-
site-directed mutagenesis, inactive mutant, poor cofactor binding, altered secondary structure
H309Q
-
site-directed mutagenesis, inactive mutant, poor cofactor binding, altered secondary structure
H315Q
-
site-directed mutagenesis, 40fold increased Km for NADP+ compared to the wild-type enzyme
H319Q
-
site-directed mutagenesis, cofactor binding and kinetics similar to the wild-type enzyme, slightly reduced activity
K212Q
-
site-directed mutagenesis, highly decreased activity in both reaction directions compared to the wild-type enzyme, altered pH-dependency of the activity
K212R
-
site-directed mutagenesis, highly decreased activity in both reaction directions compared to the wild-type enzyme, altered pH-dependency of the activity
K212Y
-
site-directed mutagenesis, highly decreased activity in both reaction directions compared to the wild-type enzyme, altered pH-dependency of the activity
K260Q
-
28fold increase in KM-value for NADP+, marked decrease of Vmax-value
K321Q
-
site-directed mutagenesis, kinetics are similar to the wild-type enzyme
K374Q
-
little change in kinetic parameters
N328D
-
36% decrease in vmax-value compared to wild-type
N328S
-
slight decrease in vmax-value compared to wild-type
N97A
-
site-directed mutagenesis, decreased Vmax compared to the wild-type enzyme, slightly affected Km values, but increased pKa of the ionizable metal-liganded hydroxyl of enzyme-bound isocitrate compared to the wild-type enzyme
N97D
-
site-directed mutagenesis, highly decreased Vmax compared to the wild-type enzyme
R132X
-
mutation of an arginine residue in pig mitochondrial IDH2 equivalent to R132 in human IDH1 causes a dramatic increase in Km for isocitrate by a factor of 165, with minimal effect on Vmax
R314Q
-
site-directed mutagenesis, 10fold increased Km for NADP+ compared to the wild-type enzyme
R323Q
-
site-directed mutagenesis, kinetics are similar to the wild-type enzyme
R83K
-
slight decrease in vmax-value compared to wild-type
R83Q
-
slight decrease in vmax-value compared to wild-type
S95A
-
site-directed mutagenesis, decreased Vmax, and increased Km for isocitrate and Mn2+ compared to the wild-type enzyme
S95D
-
site-directed mutagenesis, highly decreased Vmax compared to the wild-type enzyme
T311A
-
slight decrease in vmax-value compared to wild-type
T311N
-
vmax-value is less than 1% of the value of wild-type
T311S
-
large increase in vmax-value compared to wild-type
T373A
-
reduction of Vmax-value to 1% of wild-type
T373S
-
little change in kinetic parameters
T373V
-
reduction of Vmax-value to 20% of wild-type
T78A
-
site-directed mutagenesis, decreased Vmax, and increased Km for isocitrate and Mn2+ compared to the wild-type enzyme
T78D
-
site-directed mutagenesis, decreased Vmax compared to the wild-type enzyme
Y140E
-
site-directed mutagenesis, highly decreased activity in both reaction directions compared to the wild-type enzyme, unaltered Km for isocitrate and NADP+
Y140F
-
site-directed mutagenesis, highly decreased activity in both reaction directions compared to the wild-type enzyme, unaltered Km for isocitrate and NADP+
Y140K
-
site-directed mutagenesis, highly decreased activity in both reaction directions compared to the wild-type enzyme, unaltered Km for isocitrate and NADP+
Y140T
-
site-directed mutagenesis, highly decreased activity in both reaction directions compared to the wild-type enzyme, unaltered Km for isocitrate and NADP+, highly increased activation by added exogenous acetic acid and phenol compared to the wild-type enzyme
Y316F
-
site-directed mutagenesis, kinetics are similar to the wild-type enzyme
Y316L
-
site-directed mutagenesis, 4fold increased Km for NADP+ compared to the wild-type enzyme
D389N
-
reduction in apparent melting temperature by 21.8C compared to wild-type
F205M
-
reduction in apparent melting temperature by 3.5C compared to wild-type
R186M
-
no change in apparent melting temperature compared to wild-type
R211M
Aeropyrum pernix DSM 11879
-
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
-
additional information
-
introduction of an icdh mutation into the cat2 background, in which increased availability of H2O2 causes perturbed redox homeostasis and induction of stress-related genes. Accumulation of oxidized glutathione and pathogen-related responses are enhanced in double cat2 icdh mutants compared to cat2. Single icdh mutants present constitutive induction of PR genes, enhanced resistance to bacteria in icdh, cat2 and cat2 icdh is quantitatively correlated with PR gene expression. However, the effect of icdh in both Col0 and cat2 backgrounds is not associated with enhanced accumulation of salicylic acid, phenotypes, overview
additional information
Arabidopsis thaliana Columbia ecotype
-
introduction of an icdh mutation into the cat2 background, in which increased availability of H2O2 causes perturbed redox homeostasis and induction of stress-related genes. Accumulation of oxidized glutathione and pathogen-related responses are enhanced in double cat2 icdh mutants compared to cat2. Single icdh mutants present constitutive induction of PR genes, enhanced resistance to bacteria in icdh, cat2 and cat2 icdh is quantitatively correlated with PR gene expression. However, the effect of icdh in both Col0 and cat2 backgrounds is not associated with enhanced accumulation of salicylic acid, phenotypes, overview
-
G123R
-
site-directed mutagenesis, mutation is located in the catalytic domain, the mutant shows reduced activity compared to the wild-type enzyme
additional information
-
1p19q deletion correlates with pure oligodendrogliomas
additional information
-
analysis of IDH1 mutations in chromosome 19, 1p19q, and prognostic impact in glioma patients, overview
additional information
-
mutational analysis of IDH1 codon 132 in 1185 cancer samples, overview