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Information on EC 1.2.4.2 - oxoglutarate dehydrogenase (succinyl-transferring) and Organism(s) Rattus norvegicus
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1.2.4.2 oxoglutarate dehydrogenase (succinyl-transferring)IUBMB Comments
Contains thiamine diphosphate. It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex, EC 1.2.1.105, 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.
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Word Map
- 1.2.4.2
- succinate
-
tricarboxylic
- malate
- isocitrate
- tca
- thiamin
- citrate
- dehydrogenases
-
krebs
- dihydrolipoamide
-
citric
- neurodegenerative
-
lipoylation
- alzheimer
-
lipoic
- lipoamide
- aconitase
-
branched-chain
- transketolase
-
succinylation
-
intramitochondrial
- succinyl-coa
- oxaloacetate
- hexokinase
- acidosis
- glyoxylate
- glutamicum
- fumarase
- encephalopathy
-
antimitochondrial
- glutaminase
-
pigeon
- alpha-ketoacids
-
aciduria
-
thiamine-dependent
-
thiamine-deficient
-
ca2+-sensitive
- 2-oxo-acid
-
anaplerotic
- 6-phosphofructokinase
- wernicke
-
ketoacids
- dihydrolipoate
- thiokinase
-
1.2.4.1
-
diphosphate-dependent
-
nadh-linked
-
malate-aspartate
- pdc-e2
- industry
- synthesis
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
alpha-ketoglutarate dehydrogenase, 2-oxoglutarate dehydrogenase, kgdhc, alpha-ketoglutarate dehydrogenase complex, 2-oxoglutarate dehydrogenase complex, oxoglutarate dehydrogenase, kgdh, dhtkd1, ogdhl, ogdhc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-ketoglutarate dehydrogenase
2-OGDH
-
-
-
-
2-oxoglutarate dehydrogenase
2-oxoglutarate:lipoate oxidoreductase
-
-
-
-
AKGDH
-
-
-
-
alpha-ketoglutarate dehydrogenase
alpha-ketoglutaric acid dehydrogenase
-
-
-
-
alpha-ketoglutaric dehydrogenase
-
-
-
-
alpha-KGD
-
-
-
-
alpha-oxoglutarate dehydrogenase
-
-
-
-
dehydrogenase, oxoglutarate
-
-
-
-
E1o
ketoglutaric dehydrogenase
-
-
-
-
OGDC
-
-
-
-
OGDH
oxoglutarate decarboxylase
-
-
-
-
oxoglutarate dehydrogenase
2-ketoglutarate dehydrogenase
-
-
-
-
2-oxoglutarate dehydrogenase
-
-
-
-
2-oxoglutarate dehydrogenase
-
first and rate-limiting component of the multienzyme 2-oxoglutarate dehydrogenase complex
alpha-ketoglutarate dehydrogenase
-
-
-
-
oxoglutarate dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-
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, EC 1.2.1.105, 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
9031-02-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoadipate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine + CO2
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
?
additional information
?
-
-
enzyme complex produces H2O2 in vivo, which is inhibited by NAD+ with the isolated enzyme complex and in mitochondria, physiological effects and regulation, overview
-
-
?
additional information
?
-
-
the E1o component of the2-oxoglutarate dehydrogenase complex catalyses the initial, substrate-specific and irreversible stage of the overall reaction, and has the lowest catalytic activity (turnover number) among the components and as such limits the rate of the overall process
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
?
additional information
?
-
-
enzyme complex produces H2O2 in vivo, which is inhibited by NAD+ with the isolated enzyme complex and in mitochondria, physiological effects and regulation, overview
-
-
?
additional information
?
-
-
the E1o component of the2-oxoglutarate dehydrogenase complex catalyses the initial, substrate-specific and irreversible stage of the overall reaction, and has the lowest catalytic activity (turnover number) among the components and as such limits the rate of the overall process
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
-
activation of OGDH, followed by an increase in oxygen consumption under normoxic conditions, during hypoxia accumulation of Ca2+ in mitochondria
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutathione
-
regulation of enzyme activity by reversible glutathionylation, inactivation with diamide
succinyl phosphonate
-
OGDHC inhibitor competitive to 2-oxoglutarate, 0.005 mM succinyl phosphonate protects OGDHC from catalysis-induced inactivation
additional information
-
treatment of mitochondria with H2O2 or tert-butylhydroperoxide leads to decreased enzyme activity due to alterations in the glutathione status, reversible inhibition in case of H2O2, irrevrsible in case of tert-butylhydroperoxide, no direct interaction and no inhibition of isolated enzyme, inhibitory mechanism, enzyme reactivation by DTT, glutathione, and the glutaredoxin system, but not by thioredoxin system
-
additional information
-
the thyil radical of the complex-bound lipoate inactivates E1o in the presence of 2-oxoglutarate, while thioredoxin prevents E1o inactivation
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
carbonyl cyanide p-trifluoromethoxyphenylhydrazone
-
activates the enzyme complex for production of reactive oxygen species in absence of NAD+
ethanol
-
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
-
regulation of enzyme activity by reversible glutathionylation, modulation of function by redox status
additional information
-
potassium stabilizes the binding of thiamine diphosphate to E1o
-
ADP
-
activates the enzyme complex for production of reactive oxygen species in absence of NAD+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
2-oxoadipate
preparation from liver, low affinity state, pH 7, temperature not specified in the publication
0.27
2-oxoadipate
preparation from liver, pH 7, temperature not specified in the publication
0.45
2-oxoadipate
preparation from heart, pH 7, temperature not specified in the publication
0.45
2-oxoadipate
preparation from liver, low affinity state, pH 7, temperature not specified in the publication
0.55
2-oxoadipate
preparation from heart, pH 7, temperature not specified in the publication
0.27
2-oxoglutarate
enzyme from liver, at pH 7.0, temperature not specified in the publication
0.45
2-oxoglutarate
enzyme from heart, at pH 7.0, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00005
adipoyl phosphonate
and 0.50, preparation from liver, pH 7, temperature not specified in the publication
-
0.049
adipoyl phosphonate
preparation from heart, pH 7, temperature not specified in the publication
-
0.05
adipoyl phosphonate
and 0.000050, preparation from liver, pH 7, temperature not specified in the publication
-
0.405
adipoyl phosphonate
enzyme from liver, at pH 7.0, temperature not specified in the publication
-
0.405
adipoyl phosphonate
preparation from liver, pH 7, temperature not specified in the publication
-
2.487
adipoyl phosphonate
enzyme from heart, at pH 7.0, temperature not specified in the publication
-
2.487
adipoyl phosphonate
preparation from heart, pH 7, temperature not specified in the publication
-
0.0014
glutaryl phosphonate
and 0.0024, preparation from liver, pH 7, temperature not specified in the publication
-
0.0024
glutaryl phosphonate
and 0.0014, preparation from liver, pH 7, temperature not specified in the publication
-
0.0038
glutaryl phosphonate
preparation from heart, pH 7, temperature not specified in the publication
-
0.0073
glutaryl phosphonate
enzyme from liver, at pH 7.0, temperature not specified in the publication
-
0.039
glutaryl phosphonate
enzyme from heart, at pH 7.0, temperature not specified in the publication
-
0.039
glutaryl phosphonate
preparation from heart, pH 7, temperature not specified in the publication
-
0.073
glutaryl phosphonate
preparation from liver, pH 7, temperature not specified in the publication
-
0.0038
succinyl phosphonate
and 0.128, preparation from liver, pH 7, temperature not specified in the publication
0.0096
succinyl phosphonate
enzyme from liver, at pH 7.0, temperature not specified in the publication
0.0096
succinyl phosphonate
preparation from liver, pH 7, temperature not specified in the publication
0.0102
succinyl phosphonate
preparation from heart, pH 7, temperature not specified in the publication
0.02
succinyl phosphonate
enzyme from heart, at pH 7.0, temperature not specified in the publication
0.02
succinyl phosphonate
preparation from heart, pH 7, temperature not specified in the publication
0.128
succinyl phosphonate
and 0.0038, preparation from liver, pH 7, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
2-oxoglutarate dehydrogenase-like protein is not detected in heart
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
isoenzymes 2-oxoglutarate dehydrogenase (OGDH) and 2-oxoadipate dehydrogenase (OADH) show a 100fold difference in their ratio in the heart and liver, but similar Michaelis saturations by 2-oxoglutarate are inherent in the enzyme preparations from these tissues. In the heart, OADH/OGDH ratio is about 0.01, and OADH possesses low-affinity sites to 2-oxoadipate. In liver preparation, OADH/OGDH ratio is about 1.6, and OADH a biphasic saturation with 2-oxoadipate
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ODO1_RAT
1023
0
116296
Swiss-Prot
Mitochondrion (Reliability: 2)
OGDHL_RAT
1010
0
114637
Swiss-Prot
Mitochondrion (Reliability: 1)
A0A8I6AF05_RAT
1019
0
115865
TrEMBL
Mitochondrion (Reliability: 2)
A0A8I6A1Y1_RAT
1034
0
117595
TrEMBL
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nichols, B.J.; Rigoulet, M.; Denton, R.M.
Comparison of the effects of Ca2+, adenine nucleotides and pH on the kinetic properties of mitochondrial NAD+-isocitrate dehydrogenase and oxoglutarate dehydrogenase from the yeast Saccharomyces cerevisiae and rat heart
Biochem. J.
303
461-465
1994
Saccharomyces cerevisiae, Rattus norvegicus
Nulton-Persson, A.C.; Starke, D.W.; Mieyal, J.J.; Szweda, L.I.
Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status
Biochemistry
42
4235-4242
2003
Rattus norvegicus
Starkov, A.A.; Fiskum, G.; Chinopoulos, C.; Lorenzo, B.J.; Browne, S.E.; Patel, M.S.; Beal, M.F.
Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species
J. Neurosci.
24
7779-7788
2004
Mus musculus, Rattus norvegicus
Solien, J.; Haynes, V.; Giulivi, C.
Differential requirements of calcium for oxoglutarate dehydrogenase and mitochondrial nitric-oxide synthase under hypoxia: Impact on the regulation of mitochondrial oxygen consumption
Comp. Biochem. Physiol. A
142A
111-117
2005
Rattus norvegicus
-
Bunik, V.I.; Fernie, A.R.
Metabolic control exerted by the 2-oxoglutarate dehydrogenase reaction: a cross-kingdom comparison of the crossroad between energy production and nitrogen assimilation
Biochem. J.
422
405-421
2009
Rattus norvegicus
Bunik, V.; Kaehne, T.; Degtyarev, D.; Shcherbakova, T.; Reiser, G.
Novel isoenzyme of 2-oxoglutarate dehydrogenase is identified in brain, but not in heart
FEBS J.
275
4990-5006
2008
Rattus norvegicus
Graf, A.; Kabysheva, M.; Klimuk, E.; Trofimova, L.; Dunaeva, T.; Z1/4ndorf, G.; Kahlert, S.; Reiser, G.; Storozhevykh, T.; Pinelis, V.; Sokolova, N.; Bunik, V.
Role of 2-oxoglutarate dehydrogenase in brain pathologies involving glutamate neurotoxicity
J. Mol. Catal. B
61
80-87
2009
Rattus norvegicus
-
Zakharchenko, M.; Zakharchenko, A.; Khunderyakova, N.; Tutukina, M.; Simonova, M.; Vasilieva, A.; Romanova, O.; Fedotcheva, N.; Litvinova, E.; Maevsky, E.; Zinchenko, V.; Berezhnov, A.; Morgunov, I.; Gulayev, A.; Kondrashova, M.
Burst of succinate dehydrogenase and alpha-ketoglutarate dehydrogenase activity in concert with the expression of genes coding for respiratory chain proteins underlies short-term beneficial physiological stress in mitochondria
Int. J. Biochem. Cell Biol.
45
190-200
2013
Rattus norvegicus
Choi, S.; Pfleger, J.; Jeon, Y.H.; Yang, Z.; He, M.; Shin, H.; Sayed, D.; Astrof, S.; Abdellatif, M.
Oxoglutarate dehydrogenase and acetyl-CoA acyltransferase 2 selectively associate with H2A.Z-occupied promoters and are required for histone modifications
Biochim. Biophys. Acta Gene Regul. Mech.
1862
194436
2019
Homo sapiens, Mus musculus, Rattus norvegicus
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