1.1.1.42: isocitrate dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about isocitrate dehydrogenase (NADP+), go to the full flat file.
Word Map on EC 1.1.1.42
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1.1.1.42
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glioma
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glioblastoma
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astrocytomas
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dehydrogenases
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malate
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leukemia
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myeloid
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glucose-6-phosphate
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resect
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oncometabolite
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oligodendrogliomas
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d-2-hydroxyglutarate
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anaplastic
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malic
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idh1-mutant
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tricarboxylic
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hypermethylation
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multiforme
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high-grade
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progression-free
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temozolomide
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2-oxoglutarate
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radiotherapy
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codeletion
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neomorphic
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alpha-ketoglutarate
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6-phosphogluconate
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nadph-generating
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cholangiocarcinomas
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o6-methylguanine-dna
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gliomagenesis
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aconitase
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oligodendroglial
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lgg
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chondrosarcoma
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lower-grade
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oligoastrocytomas
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medicine
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nadp-malic
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supratentorial
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biotechnology
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nadph-producing
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analysis
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diagnostics
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nadp-me
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radiomics
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pilocytic
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karnofsky
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proneural
- 1.1.1.42
- glioma
- glioblastoma
- astrocytomas
- dehydrogenases
- malate
- leukemia
- myeloid
- glucose-6-phosphate
-
resect
-
oncometabolite
- oligodendrogliomas
- d-2-hydroxyglutarate
-
anaplastic
-
malic
-
idh1-mutant
-
tricarboxylic
-
hypermethylation
- multiforme
-
high-grade
-
progression-free
- temozolomide
- 2-oxoglutarate
-
radiotherapy
-
codeletion
-
neomorphic
- alpha-ketoglutarate
- 6-phosphogluconate
-
nadph-generating
- cholangiocarcinomas
-
o6-methylguanine-dna
-
gliomagenesis
- aconitase
-
oligodendroglial
- lgg
- chondrosarcoma
-
lower-grade
- oligoastrocytomas
- medicine
-
nadp-malic
-
supratentorial
- biotechnology
-
nadph-producing
- analysis
- diagnostics
- nadp-me
-
radiomics
-
pilocytic
-
karnofsky
-
proneural
Reaction
Synonyms
AbIDH1, AfIDH, CgIDH, cICDH, CtIDP1, CtIDP2, cytosolic isocitrate dehydrogenase 1, cytosolic NADP(+)-dependent isocitrate dehydrogenase, cytosolic NADP+-dependent isocitrate dehydrogenase, cytosolic NADP-dependent isocitrate dehydrogenase, cytosolic NADPH-dependent isocitrate dehydrogenase, DpIDH, EcIDH, HICDH, ICD, ICD1, ICD2, icdA, ICDH, ICDH-1, IDH, IDH-90, IDH-I, IDH-IIa, IDH-IIb, IDH1, IDH2, IDH3, IDHP, IDP, IDP1, IDP2, IDP3, IDPA, IDPc, IDPm, isocitrate dehydrogenase, isocitrate dehydrogenase (NADP), isocitrate dehydrogenase (NADP-dependent), isocitrate dehydrogenase (nicotinamide adenine dinucleotide phosphate), isocitrate dehydrogenase 1, isocitrate dehydrogenase 2, isocitrate dehydrogenase-1, isocytrate deyhdrogenase, mICDH, mitochondrial NADP+-dependent isocitrate dehydrogenase, NAD+-dependent isocitrate dehydrogenase, NADP isocitric dehydrogenase, NADP+ dependent isocitrate dehydrogenase, NADP+-dependent Ds-threo-isocitrate dehydrogenase, NADP+-dependent Ds-threo-isocitrate:NADP+ oxidoreductase, NADP+-dependent ICDH, NADP+-dependent IDH, NADP+-dependent isocitrate dehydrogenase, NADP+-ICDH, NADP+-IDH, NADP+-isocitrate dehydrogenase, NADP+-linked isocitrate dehydrogenase, NADP+-specific ICDH, NADP+-specific IDH, NADP+-specific isocitrate dehydrogenase, NADP-dependent IDH, NADP-dependent isocitrate dehydrogenase, NADP-dependent isocitric dehydrogenase, NADP-ICDH, NADP-IDH, NADP-IDH Idp1p, NADP-isocitrate dehydrogenase, NADP-linked isocitrate dehydrogenase, NADP-specific isocitrate dehydrogenase, NADPH-dependent isocitrate dehydrogenase, NADPH-IDH, oxalosuccinate decarboxylase, oxalsuccinic decarboxylase, perICDH, PS-NADP-IDH, TaIDH, TM1148, YlIDP
ECTree
1.1.1.42 isocitrate dehydrogenase (NADP+)Advanced search results
results (
results (Engineering
Engineering on EC 1.1.1.42 - isocitrate dehydrogenase (NADP+)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
S113A
S113D
S113E
S113G
S113T
S113Y
R211M
C363S
the mutation does not perturb the enzymatic characteristics of the enzyme. However, the mutant is less affected by nitrosoglutathione treatment than the wild type enzyme
D253A/S257K/K260Q/R314D/H315I/T327A
site-directed mutagenesis, the mutant shows a witch in cofactor specificity from NADP+ to NAD+
D253A/S257K/K260Q/R314D/H315I/T327A
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site-directed mutagenesis, the mutant shows a witch in cofactor specificity from NADP+ to NAD+
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A325P/G326S
50% inactivation after 10 min at 91.3°C as compared to 87.5°C for wild-type enzyme
A336F
50% inactivation after 10 min at 74°C as compared to 87.5°C or wild-type enzyme
I321L
50% inactivation after 10 min at 88.9°C as compared to 87.5°C for wild-type enzyme
Y309I/I310L
50% inactivation after 10 min at 88.4°C as compared to 87.5°C for wild-type enzyme
Y309I/I310L/I321L/A325P/G326S
50% inactivation after 10 min at 90°C as compared to 87.5°C for wild-type enzyme
A741S
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the mutant exhibits higher specific activity and thermostability than the wild type enzyme
E596L
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the mutant exhibits higher specific activity and thermostability than the wild type enzyme
R153C
the mutation dramatically reduces the catalytic efficiency of the enzyme for isocitrate oxidation, which drops to 1.5% of the wild type enzyme. The mutant acquires a neomorphic ability of producing 2-hydroxyglutarate from 2-oxoglutarate
R153H
the mutation dramatically reduces the catalytic efficiency of the enzyme for isocitrate oxidation, which drops to 0.6% of the wild type enzyme. The mutant acquires a neomorphic ability of producing 2-hydroxyglutarate from 2-oxoglutarate
R291S/K343D/Y344I/V350A/Y390P
Q8X277
switch in coenzyme specificity from NADP+ to NAD+
A134D
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
C269S
C379S
D273L
the mutant exhibits an about 170fold decrease in catalytic efficiency, driven by a 5.4fold decrease in kcat and 31fold increase in Km as compared to the wild type enzyme
D273N
the mutant has a more than 500fold decrease in kcat/Km, driven primarily through more than 300fold increase in Km as compared to the wild type enzyme
D273S
the mutant exhibits adecrease in catalytic efficiency, driven by a 2.5fold decrease in kcat and 200fold increase in Km as compared to the wild type enzyme
G123R
site-directed mutagenesis, mutation is located in the catalytic domain, the mutant shows reduced activity compared to the wild-type enzyme
H133Q
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
K217M
the mutant shows reduced catalytic efficiency as compared to the wild type enzym
K217Q
the mutant shows reduced catalytic efficiency as compared to the wild type enzym
K413Q
the acetylation surrogate mutant of isoform IDH2 exhibits lower oxidative reaction rates than wild type. 2-Hydroxyglutarate production by the mutant is largely diminished at the enzymatic and cellular level
R100Q
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R132A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R132C
R132G
R132H
R132K
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R132L
R132N
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R132Q
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R132S
R132W
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R132X
R172K
IDH2 R172 mutation causes production and accumulation of 2-hydroxyglutarate in acute myelogenous leukemia cells
R172X
naturally occuring mutations of IDH2 in metastatic brain tumors
H590L/R601D
the mutant with strongly decreased activity wit NADP+ compared to the wild type enzyme displays a 0.183fold preference for NAD+ over NADP+
H590L/R601D/R650S
the mutant with severely decreased activity with NADP+ compared to the wild type enzyme displays a 5.93fold preference for NAD+ over NADP+
H590L/R601D
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the mutant with strongly decreased activity wit NADP+ compared to the wild type enzyme displays a 0.183fold preference for NAD+ over NADP+
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H590L/R601D/R650S
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the mutant with severely decreased activity with NADP+ compared to the wild type enzyme displays a 5.93fold preference for NAD+ over NADP+
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C245S
the activities of the mutant in the presence of Cd2+ are decreased as that of wild type enzyme
C379S
the activity of the mutant in the absence of Cd2+ is similar to that of the wild type enzyme, but the decrease of activity in the presence of Cd2+ is much reduced
L594E
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the mutant is more thermolabile than wild type enzyme and has a lower specific activity at temperatures over 45°C
H309F
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site-directed mutagenesis, inactive mutant, poor cofactor binding, altered secondary structure
H309Q
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site-directed mutagenesis, inactive mutant, poor cofactor binding, altered secondary structure
H315Q
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site-directed mutagenesis, 40fold increased Km for NADP+ compared to the wild-type enzyme
H319Q
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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
N97A
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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
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site-directed mutagenesis, highly decreased Vmax compared to the wild-type enzyme
R132X
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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
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site-directed mutagenesis, 10fold increased Km for NADP+ compared to the wild-type enzyme
S95A
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site-directed mutagenesis, decreased Vmax, and increased Km for isocitrate and Mn2+ compared to the wild-type enzyme
S95D
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site-directed mutagenesis, highly decreased Vmax compared to the wild-type enzyme
T78A
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site-directed mutagenesis, decreased Vmax, and increased Km for isocitrate and Mn2+ 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
Y316L
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site-directed mutagenesis, 4fold increased Km for NADP+ compared to the wild-type enzyme
D389N
reduction in apparent melting temperature by 21.8°C compared to wild-type
F205M
reduction in apparent melting temperature by 3.5°C compared to wild-type
R186M
no change in apparent melting temperature compared to wild-type
H590L/R601L
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the mutations greatly reduce the affinity for NADP+, but fail to improve the ability to use NAD+ so the mutant has similar affinities to NADP+ and NAD+
K589T/H590L/R601L
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the mutations greatly reduce the affinity for NADP+, but fail to improve the ability to use NAD+ so the mutant has similar affinities to NADP+ and NAD+
R322D
site-directed mutagenesis, the mutant shows an 41fold higher Km for NADP+ than the wild-type enzyme, and it shows NAD+-dependent activity in contrast to the wild-type enzyme
R322D
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site-directed mutagenesis, the mutant shows an 41fold higher Km for NADP+ than the wild-type enzyme, and it shows NAD+-dependent activity in contrast to the wild-type enzyme
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additional information
S113A
mutant enzyme with remarkably reduced enzymatic activity
S113D
the phosphorylation-mimicking mutant lacks almost all enzymatic activity
S113E
the phosphorylation-mimicking mutant lacks almost all enzymatic activity
S113G
mutant enzyme with remarkably reduced enzymatic activity
S113T
mutant enzyme with remarkably reduced enzymatic activity
S113Y
mutant enzyme with remarkably reduced enzymatic activity
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
R211M
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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
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C269S
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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
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site-directed mutagenesis, is not sensitive to inhibition by Cd2+ in contrast to the wild-type enzyme
C379S
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glutathionylation of the C379S mutant is similar to that of wild type enzyme
C379S
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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
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naturally occuring mutation C394T, genotyping in glioma samples, overview
R132C
naturally occuring mutation of IDH1 in melanoma metastasis of the lung
R132C
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naturally occuring mutation of IDH1, results in 60fold increased Km for isocitrate compared to the wild-type IDH1
R132C
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R132G
IDH1 R132 mutations cause production and accumulation of 2-hydroxyglutarate in acute myelogenous leukemia cells
R132G
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naturally occuring mutation C394G, genotyping in glioma samples, overview
R132G
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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 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
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naturally occuring mutation G395A, genotyping in glioma samples, overview
R132H
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naturally occuring mutation in myelodysplastic syndrome preceding acute myeloid leukemia. R132H alteration can be detected by immunohistochemistry using R132H mutation-specific antibodies, overview
R132H
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naturally occuring mutation of IDH1, results in 94fold increased Km for isocitrate compared to the wild-type IDH1
R132H
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
R132H
the mutant catalyzes the conversion of 2-oxoglutarate plus NADPH to D-2-hydroxyglutarate
R132L
-
naturally occuring mutation G395T, genotyping in glioma samples, overview
R132S
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naturally occuring mutation C394A, genotyping in glioma samples, overview
R132S
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naturally occuring mutation of IDH1, results in 70fold increased Km for isocitrate compared to the wild-type IDH1
R132X
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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
additional information
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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
identification of naturally occurring peroxisomal NADP-ICDH (picdh) Arabidopsis mutant lines, designated as picdh-1 (SALK_072422) and picdh-2 (SALK_039193C) carrying a T-DNA insertion in exons 9 and in the 5'UTR, respectively. The mutation results in a lack of the peroxisomal NADP-ICDH in both picdh-1 and picdh-2 plants. There are no significant differences in phenotype between the wild-type (Wt) and the two mutant (picdh-1 and picdh-2) lines. Intrinsic photosynthetic performance is not altered in the different plants with similar maximum C assimilation capacities, light use efficiency, and respiration rates in darkness due to similar growth rates. No differences are found in growth rates, stomatal densities, or leaf mass-area ratios
additional information
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identification of naturally occurring peroxisomal NADP-ICDH (picdh) Arabidopsis mutant lines, designated as picdh-1 (SALK_072422) and picdh-2 (SALK_039193C) carrying a T-DNA insertion in exons 9 and in the 5'UTR, respectively. The mutation results in a lack of the peroxisomal NADP-ICDH in both picdh-1 and picdh-2 plants. There are no significant differences in phenotype between the wild-type (Wt) and the two mutant (picdh-1 and picdh-2) lines. Intrinsic photosynthetic performance is not altered in the different plants with similar maximum C assimilation capacities, light use efficiency, and respiration rates in darkness due to similar growth rates. No differences are found in growth rates, stomatal densities, or leaf mass-area ratios
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additional information
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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
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additional information
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construction of an NADP+-ICDH gene (icdA)-overexpressing strain (OPI-1) using Aspergillus niger strain WU-2223L. The amount of citric acid produced by Aspergillus niger can be altered with the NADP+-ICDH activity. Time-dependent transcriptional changes in the genes encoding NADP+-ICDH, NAD+-ICDH, and ICL are analyzed by RT-PCR. The glyoxylate cycle is poorly activated or slightly repressed in the icdA-overexpressing Aspergillus niger clone
additional information
the coenzyme specificity of BlIDH can be completely reversed from NADP+ to NAD+ by a factor of 2387 by replacing six residues. The loss in NADP+-dependent activity might result from the removal of favorable interactions between Arg314 or His315 and the 2'-phosphate group
additional information
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the coenzyme specificity of BlIDH can be completely reversed from NADP+ to NAD+ by a factor of 2387 by replacing six residues. The loss in NADP+-dependent activity might result from the removal of favorable interactions between Arg314 or His315 and the 2'-phosphate group
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additional information
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analysis of IDH1 mutations in chromosome 19, 1p19q, and prognostic impact in glioma patients, overview
additional information
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mutational analysis of IDH1 codon 132 in 1185 cancer samples, overview
additional information
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siRNA-mediated knockdown of IDPm suppresses hypoxia-induced stimulation of HIF-1alpha protein expression in PC-3 human prostate cancer cells. Treatment with the 26S proteasome inhibitor MG132 fails to abrogate the suppression of HIF-1alpha accumulation induced by IDPm knockdown, whereas HIF-1alpha levels are reduced by cycloheximide treatment in both control and IDPm siRNA-transfected cells
additional information
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transfection of HEK-293 cells with an IDPc small interfering RNA significantly decreases the activity of IDPc and enhances cellular susceptibility to cadmium-induced apoptosis as indicated by the morphological evidence of apoptosis, DNA fragmentation and condensation, cellular redox status, mitochondria redox status and function, and the modulation of apoptotic marker proteins, overview. DNA fragmentation is enhanced in IDPc siRNA-transfected HEK293 cells compared to control cells upon exposure to cadmium
additional information
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two independent short hairpin RNAs decrease IDH1 mRNA by more than 75% and reduce cellular 2-oxoglutarate levels by up to 50%
additional information
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construction of transgenic mice by infection of fertilized eggs, enzyme overexpressing transgenic mice show increased triglyceride and cholesterol levels and develop fatty liver, hyperlipidemia, and obesity
additional information
Idh2 gene deletion, generation of Idh2-/- mice, phenotype,overview
additional information
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Idh2 gene deletion, generation of Idh2-/- mice, phenotype,overview
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additional information
knockdown of IDPm by siRNA in H9c2 cells, the suppression of IDPm expression by siRNA induces apoptosis and hypertrophy of cultured cardiomyocytes through the disruption of cellular redox balance, phenotype, overview
additional information
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construction of IDP1, IDP2, and IDP3 disruption mutants, and of double and triple disruption mutants in haploid strain MMY011. Complementation study in disruption mutants expressing the full-length IDPA enzyme from Aspergillus nidulans, which behaves similar to the yeast IDP2 harboring a type I peroxisomal targeting sequence, PTS1, and occurs in cytosol and peroxisomes, subcellular localization study, overview. Expression of IDPA lacking the mitochondrial targeting sequence and containing a different PTS1 results in the same expression level and subcellular orientation
additional information
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construction of IDP1, IDP2, and IDP3 disruption mutants, and of double and triple disruption mutants in haploid strain MMY011. Complementation study in disruption mutants expressing the full-length IDPA enzyme from Aspergillus nidulans, which behaves similar to the yeast IDP2 harboring a type I peroxisomal targeting sequence, PTS1, and occurs in cytosol and peroxisomes, subcellular localization study, overview. Expression of IDPA lacking the mitochondrial targeting sequence and containing a different PTS1 results in the same expression level and subcellular orientation
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additional information
engineering the 2-oxoglutarate overproduction from raw glycerol by overexpression of the genes encoding NADP+-dependent isocitrate dehydrogenase and pyruvate carboxylase in Yarrowia lipolytica. Overexpression of NADP+-dependent isocitrate dehydrogenase IDP1 or simultaneous overexpression of IDP1 and pyruvate carboxylase gene PYC1 strongly increase the amount of secreted 2-oxoglutarate
additional information
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engineering the 2-oxoglutarate overproduction from raw glycerol by overexpression of the genes encoding NADP+-dependent isocitrate dehydrogenase and pyruvate carboxylase in Yarrowia lipolytica. Overexpression of NADP+-dependent isocitrate dehydrogenase IDP1 or simultaneous overexpression of IDP1 and pyruvate carboxylase gene PYC1 strongly increase the amount of secreted 2-oxoglutarate
additional information
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engineering the 2-oxoglutarate overproduction from raw glycerol by overexpression of the genes encoding NADP+-dependent isocitrate dehydrogenase and pyruvate carboxylase in Yarrowia lipolytica. Overexpression of NADP+-dependent isocitrate dehydrogenase IDP1 or simultaneous overexpression of IDP1 and pyruvate carboxylase gene PYC1 strongly increase the amount of secreted 2-oxoglutarate
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