Information on EC 1.2.4.2 - oxoglutarate dehydrogenase (succinyl-transferring)

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

EC NUMBER
COMMENTARY hide
1.2.4.2
-
RECOMMENDED NAME
GeneOntology No.
oxoglutarate dehydrogenase (succinyl-transferring)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
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reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-oxoglutarate decarboxylation to succinyl-CoA
-
-
2-oxoglutarate dehydrogenase complex
-
-
Biosynthesis of antibiotics
-
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Biosynthesis of secondary metabolites
-
-
Citrate cycle (TCA cycle)
-
-
citric acid cycle
-
-
Lysine degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
TCA cycle III (animals)
-
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Tryptophan metabolism
-
-
vitamin B1 metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
2-oxoglutarate:[dihydrolipoyllysine-residue succinyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-succinylating)
Contains thiamine diphosphate. It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, dihydrolipoyllysine-residue succinyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-02-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 4B
-
-
Manually annotated by BRENDA team
strain 4B
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain ATCC13869
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
no activity in Mycobacterium tuberculosis
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-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
enzyme E1o is a component of the alpha-ketoglutarate dehydrogenase multienzyme complex KGDH
-
-
Manually annotated by BRENDA team
strain ATCC 13525
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-
Manually annotated by BRENDA team
enzyme E2 is a component of the 2-oxo acid dehydrogenase multienzyme complex, consisting of enzyme components EC 1.2.4.1, EC 1.2.4.2, EC 2.3.1.12, and EC 1.8.1.4
-
-
Manually annotated by BRENDA team
strain ATCC 14028, gene ogdh, enzyme E1o is a component of the 2-oxoglutarate dehydrogenase multienzyme complex
SwissProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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RNAi knockdown-inducted bloodstream trypanosomes show pronounced growth reduction and often fail to equally distribute kinetoplast DNA to daughter cells, resulting in accumulation of cells devoid of kinetoplast DNA or containing two kinetoplasts
physiological function
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the enzyme is bifunctional, both as a metabolic enzyme and as a mitochondrial inheritance factor necessary for the distribution of kinetoplast DNA networks to daughter cells at cytokinesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + CoA
? + H2O2
show the reaction diagram
2-oxoglutarate + CoA + 3-acetylpyridine adenine dinucleotide
succinyl-CoA + CO2 + reduced 3-acetylpyridine adenine dinucleotide
show the reaction diagram
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
-
3-acetylpyridine adenine dinucleotide can be used instead of NAD+ to avoid concomitant oxidase activity that would degrade NADH produced by the ODH reaction
lipoic acid
thiamine diphosphate
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADP
-
activates through allosteric binding
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
((+/-)-2-[4-((3-chloro-5-(trifluoromethyl)-2-pyridyl)oxy)-phenoxy]propionic acid)
-
i.e. haloxyfop, grass-specific herbicide
(R)-2-amino-3-((1,1,2,2-tetrafluoroethyl)thio)propanoic acid
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inactivates
1,2,3,4-tetrahydroisoquinoline
-
IC50: 18.2
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
-
1-methyl-4-phenylpyridine
-
i.e. MPP+
1-methyl-4-phenylpyridinium
1-oxo-3-carboxypropylphosphonic acid methyl ester
2-oxo-3-methyl-n-valeric acid
-
inhibition of the 2-oxoglutarate dehydrogenase enzyme complex in vivo and in situ, after 40 min 25% inhibition at 10 mM, 46% at 20 mM, after 80 min 58% inhibition at 10 mM, 80% at 20 mM, inhibition does not affect the mitochondrial membrane potential
2-oxo-3-methylpentanoate
-
2-oxoglutarate dehydrogenase complex
2-oxoglutarate
2-Oxoisohexanoate
-
2-oxoglutarate dehydrogenase complex
2-oxoisopentanoate
-
2-oxoglutarate dehydrogenase complex
3-nitropropionic acid
-
-
3-NP
-
-
4-hydroxy-2-nonenal
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-
4-oxo-4-phosphonobutanoic acid
4-[(2-carboxyethoxy)(hydroxy)phosphoryl]-4-oxobutanoic acid
4-[ethoxy(hydroxy)phosphoryl]-4-oxobutanoic acid
7-(1-hydroxy-2-aminoethyl)-3,4-dihydro-5-hydroxy-2H-1,4-benzothiazine-3-carboxylic acid
-
time-dependent inhibition of the 2-oxoglutarate dehydrogenase complex appears to be related to the oxidation of 7-(1-hydroxy-2-aminoethyl)-3,4-dihydro-5-hydroxy-2H-1,4-benzothiazine-3-carboxylic acid, catalyzed by an unknown component of the inner mitochondrial membrane, to electrophilic intermediates which bind covalently to active site cysteinyl residues of the enzyme complex
7-(2-aminoethyl)-3,4-dihydro-5-hydroxy-2H-1,4-benzothiazine-3-carboxylic acid
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may be an endotoxin that contributes to the alpha-oxoglutarate dehydrogenase and complex I defects in Parkinson‘s disease, the inhibition of the 2-oxoglutarate dehydrogenase complex is dependent on the oxidation of 7-(2-aminoethyl)-3,4-dihydro-5-hydroxy-2H-1,4-benzothiazine-3-carboxylic acid, catalyzed by an unknown constituent of the inner mitochondrial membrane, to an electrophilic o-quinone imine that covalently modifies active site sulfhydryl residues
acetaldehyde
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2-oxoglutarate dehydrogenase complex
amyloid-beta peptide
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-
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arsenite
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probably bind the dithiol group in the lipoic acid
Benzene-1,3-dicarboxylate
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-
Benzene-1,4-dicarboxylate
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-
Ca2+
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0.01 mM, decreases the concentration of 2-oxoglutarate required for half-maximal activity, inhibition at higher concentrations
Cd2+
-
probably bind the dithiol group in the lipoic acid
cis-aconitate
cisplatin
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treatment with 0.05 or 0.1 mM for 3 h, followed by removal of cisplatin from the medium for 24 h, results in a pronounced loss of activity, both in mitochondrial aspartate aminotransferase-transfected cells and control cells, exposure to 0.1 mM results in a significantly greater loss of activity in mitochondrial aspartate aminotransferase-transfected cells than in control cells
ethyl 4-[ethoxy(hydroxy)phosphoryl]-4-oxobutanoate
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only inhibitory after preincubation, release of charged groups by cellular esterases and activation in intact cells
glutathione
-
regulation of enzyme activity by reversible glutathionylation, inactivation with diamide
glyoxylate
hydrogen peroxide
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the E2 subunit of alpha-ketoglutarate dehydrogenase is reversibly glutathionylated and inhibited by 0.025 mM hydrogen peroxide, the enzyme is maximally inhibited (about 45%) 5.0 min after the addition of H2O2
hypochlorous acid
Isoquinoline
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IC50: 6.5 mM
isoquinoline derivative
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-
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mono-N-chloramine
N-methyl-1,2,3,4-tetrahydroisoquinoline
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IC50: 2 mM
N-methylisoquinolinium
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-
N-n-propylisoquinolinium
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IC50: 3 mM
Na2HPO4
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50 mM KCl, 38% inhibition of the 2-oxoglutarate dehydrogenase complex
Na2SO4
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50 mM KCl, 4.5% inhibition of the 2-oxoglutarate dehydrogenase complex
NADPH
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2-oxoglutarate dehydrogenase complex
NEM
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prevents desuccinylation of the 2-oxoglutarate dehydrogenase complex
OdhI
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unphosphorylated OdhI strongly inhibits ODH activity
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oxalacetate
palmitoyl-CoA
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is 10-fold less potent than phytanoyl-CoA, no inhibitory effect up to 0.3 mM
phytanoyl-CoA
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is 10-fold more potent than palmitoyl-CoA, no inhibitory effect up to 0.3 mM
Pyridine-2,4-dicarboxylate
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-
Pyridine-2,5-dicarboxylate
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pyruvate
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2-oxoglutarate dehydrogenase complex
reactive oxygen species
ruthenium red
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abolishes the Ca-stimulation of OGDH
salsolinol
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-
succinate
-
2-oxoglutarate dehydrogenase complex
succinyl phosphonate
succinyl phosphonate carboxy ethyl ester
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potent, slow-binding inhibitor of the 2-oxoglutarate dehydrogenase complex, complete inhibition at 0.1 mM
succinyl phosphonate diethyl ester
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poor inhibitor of the 2-oxoglutarate dehydrogenase complex
succinyl phosphonate phosphono ethyl ester
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poor inhibitor of the 2-oxoglutarate dehydrogenase complex
succinyl phosphonate triethyl ester
succinyl-CoA
triethyl ester of succinyl phosphonate
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only inhibitory after preincubation, release of charged groups by cellular esterases and activation in intact cells
Tris-HCl
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50 mM, 26% inhibition of the 2-oxoglutarate dehydrogenase complex
tryptamine-4,5-dione
Valproic acid
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AceF
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acetyltransferase AceF
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acetyl-CoA
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activates, 2-oxoglutarate dehydrogenase complex
carbonyl cyanide p-trifluoromethoxyphenylhydrazone
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activates the enzyme complex for production of reactive oxygen species in absence of NAD+
ethanol
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a 3fold increase in the protein content of the E1o component 2-oxoglutarate dehydrogenase complex is observed in liver mitochondria of rats exposed to ethanol
glutathione
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regulation of enzyme activity by reversible glutathionylation, modulation of function by redox status
GMP
-
activates 2-oxoglutarate dehydrogenase complex
GTP
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activates 2-oxoglutarate dehydrogenase complex
inorganic phosphate
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NAD+
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stimulates
NH4+
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in synaptic mitochondria thioacetamide-induced encephalopathy produces an 84% increase in Vmax and a 35% decrease of KM for 2-oxoglutarate
phosphate
rotenone
spermine
-
enhances activity
thiamine
-
can reverse the loss in KGDHC in Alzheimer's disease patients
thiamine diphosphate
Trolox
-
can dramatically increase KGDHC in cultured cells
UDP
-
activates 2-oxoglutarate dehydrogenase complex
UTP
-
activates 2-oxoglutarate dehydrogenase complex
additional information
-
potassium stabilizes the binding of thiamine diphosphate to E1o
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013 - 4
2-oxoglutarate
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.2
acetaldehyde
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2-oxoglutarate dehydrogenase complex
0.5
Benzene-1,3-dicarboxylate
-
-
1.1
Benzene-1,4-dicarboxylate
-
-
1.64 - 3.3
glyoxylate
0.018 - 0.02
NADH
0.0000024
OdhI
-
unphosphorylated state
-
0.4
Pyridine-2,4-dicarboxylate
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-
3
Pyridine-2,5-dicarboxylate
-
-
0.003 - 0.004
succinyl-CoA
0.00037
Zn2+
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-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.2
1,2,3,4-tetrahydroisoquinoline
Rattus norvegicus
-
IC50: 18.2 mM
18.9
1-methyl-4-phenylpyridinium
Rattus norvegicus
-
IC50: 18.9 mM
6.5
Isoquinoline
Rattus norvegicus
-
IC50: 6.5 mM
2
N-methyl-1,2,3,4-tetrahydroisoquinoline
Rattus norvegicus
-
IC50: 2 mM
3
N-n-propylisoquinolinium
Rattus norvegicus
-
IC50: 3 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
-
-
0.2
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
2-oxoglutarate dehydrogenase reaction
6.6 - 7.4
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6.7
-
oxidation of 2-oxo-4-hydroxyglutarate or 2-oxoglutarate by the 2-oxoglutarate dehydrogenase complex
7.2 - 7.4
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7.2
-
2-oxoglutarate dehydrogenase complex
7.3 - 7.6
-
2-oxoglutarate dehydrogenase complex
7.3
-
assay at
7.5 - 7.7
-
2-oxoglutarate dehydrogenase complex
7.5
-
2-oxoglutarate dehydrogenase complex
7.6
-
assay at
8
-
2-oxoglutarate dehydrogenase complex
8 - 8.5
-
2-oxoglutarate dehydrogenase complex
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 6
-
-
6.5 - 8.5
6.5 - 8
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pH 6.5: about 40% of maximal activity, pH 8.0: about 50% of maximal activity, 2-oxoglutarate dehydrogenase complex
6.6 - 8.4
-
about 50% of maximal activity at pH 6.6 and at pH 8.4, 2-oxoglutarate dehydrogenase complex
7 - 8.5
-
pH 7.0: about 70% of maximal activity, pH 8.5: about 70% of maximal activity, 2-oxoglutarate dehydrogenase complex
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 35
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2-oxoglutarate dehydrogenase activity
35
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2-oxoglutarate dehydrogenase complex
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 45
-
20°C: about 35% of maximal activity, 45°C: about 20% of maximal activity, 2-oxoglutarate dehydrogenase complex
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
The HEK-293 subline E2k-67 shows about 30% reduced KGDHC activity; control line E2k-100
Manually annotated by BRENDA team
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highest activity found in rapidly growing mycelium, glucose-NH4+ or glucose-peptone medium
Manually annotated by BRENDA team
-
neuroblastoma cells
Manually annotated by BRENDA team
-
submedial thalamic nucleus
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
enzyme complex is expressed during erythrocytic stage of the parasite
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
SDS-PAGE
117400
-
calculated from amino acid sequence
140000
-
OdhA, the E1 subunit of ODH
190000
-
2-oxoglutarate dehydrogenase component, equilibrium sedimentation
210000
2 * 105000, SDS-PAGE
360000
-
active 2-oxoglutarate dehydrogenase component, gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
tetramer
-
4 * 100000, active 2-oxoglutarate dehydrogenase component, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
additional information
-
resulting in loss of enzyme complex activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method with 12% (w/v) polyethylene glycol 4000, 50 mM sodium citrate (pH 5.6)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
60 min, stable, 2-oxoglutarate dehydrogenase complex
21
-
60 min, about 65% loss of activity, 2-oxoglutarate dehydrogenase complex
30
-
60min, about 80% loss of activity, 2-oxoglutarate dehydrogenase complex
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate dehydrogenase complex is stabilized by glycerol, Mg2+ and thiamine diphosphate
-
2-oxoglutarate stabilizes against dilution
-
successive freeze-thawing cycles of the 2-oxoglutarate dehydrogenase complex leads to complete inactivation
-
vigorous sonication of the 2-oxoglutarate dehydrogenase complex lead to complete inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 2-oxoglutarate dehydrogenase complex, 5-15% loss of activity after several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate dehydrogenase complex
2-oxoglutarate dehydrogenase complex from ox heart, by PEG fractionation, ultracentrifugation, and gel filtration
-
ammonium sulfate precipitation, HiLoad Q-Sepharose column chromatography, and Superdex S200 gel filtration
by affinity chromatography, purification of OdhI-T14A leads to specific copurification of OdhA, the E1 subunit of ODH
-
by gel filtration
-
enzyme is further purified from commercial pig heart preparation
-
Ni-NTA column chromatography
-
partial purification
-
partial, 2-oxoglutarate dehydrogenase complex
-
partially, isolation of subsarcolemmal mitochondria from heart
-
poly(ethylene glycol) fractionation and Sephacryl HR300 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate dehydrogenase component E1o of the 2-oxoglutarate dehydrogenase complex
-
2-oxoglutarate dehydrogenase component E1o, expression in Escherichia coli
-
enzyme E1o is located on chromosome 8
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expressed in Corynebacterium glutamicum
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expressed in Escherichia coli BL21(DE3) cells
expressed in PC-12 cells
-
expression in Escherichia coli DH5alpha
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FLAG-tagged enzyme expression in siah2-/- cells and siah2+/+ cells in mitochondria and, by disruption of the mitochondrial targeting sequence, in cytoplasm, in the cytoplasm the enzyme is rapidly proteasome-dependently degraded, overvexpression of hemagglutinin-labeled enzyme E2 in 293T cells
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gene odhL encodes the 2-oxoglutarate dehydrogenase component of the multienenzyme complex, expression in Escherichia coli in kgdA mutant of Pseudomonas putida JS347
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gene ogdh, library screening, complementation of an enzyme-deficient Escherichia coli mutant strain JRG72, DNA and amino acid sequence determination and analysis, functional expression of full-length enzyme and N-terminal catalytic domain in Escherichia coli strain JM109
KGD1 gene encoding the 2-oxoglutarate dehydrogenase component of the 2-oxoglutarate dehydrogenase complex
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H352C
-
the activity of the mutant is significantly reduced
H352C/Q356D
-
the mutations fully prevent succinyltransferase activity
Q356D
-
the activity of the mutant is slightly reduced
T294A
-
the mutant shows almost no activity
H352C
-
the activity of the mutant is significantly reduced
-
H352C/Q356D
-
the mutations fully prevent succinyltransferase activity
-
Q356D
-
the activity of the mutant is slightly reduced
-
T294A
-
the mutant shows almost no activity
-
H260A
mutant has a dramatically reduced catalytic rate
H298A
mutant has a dramatically reduced catalytic rate
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
-
ODH is essential for glutamine utilization, regulatory mechanisms of reduced ODH activity that is essential for the industrial production of 1.5 million tons per year of glutamate with Corynebacterium glutamicum
medicine
additional information
Show AA Sequence (3852 entries)
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