HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.2.4.2 - oxoglutarate dehydrogenase (succinyl-transferring)
for references in articles please use BRENDA:EC1.2.4.2
Word Map on EC 1.2.4.2
- 1.2.4.2
- succinate
-
tricarboxylic
- malate
- isocitrate
- thiamin
- citrate
- lactate
- dihydrolipoamide
- dysfunction
-
krebs
-
citric
- aconitase
-
lipoic
-
lipoylation
- lipoamide
- alzheimer
-
branched-chain
- neurodegenerative
- succinyl-coa
-
decarboxylation
- transketolase
-
intramitochondrial
- hexokinase
- acidosis
-
succinylation
- oxaloacetate
- glyoxylate
- glutaminase
- fumarase
- pigeon
- tpp
-
alpha-ketoacids
-
antimitochondrial
-
thiamine-dependent
-
diphosphate-dependent
- oxythiamine
- medicine
- 2-oxo-acid
- pdc-e2
- thiokinase
- pyrithiamine
- wernicke
-
anaplerotic
-
thiamine-deficient
-
ketoacids
- 6-phosphofructokinase
-
ca2+-sensitive
-
nadh-dehydrogenase
-
ammoniagenesis
- dihydrolipoate
-
1.2.4.1
- industry
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.2.4.2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
oxoglutarate dehydrogenase (succinyl-transferring)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); 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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); 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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); 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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); 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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); 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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); 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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); 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
-
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
-
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
-
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
-
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
-
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
-
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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); 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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); mechanism of the enzyme complex is bi bi uni uni ping pong; 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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); 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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
kinetics of succinylation and desuccinylation; 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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
mechanism of the reaction catalyzed by the 2-oxoglutarate dehydrogenase complex; 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
-
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
-
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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); 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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
Pigeon
-
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
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
substrate channeling and catalytic mechanism, active site coupling
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
substrate channeling and catalytic mechanism, active site coupling
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
substrate channeling and catalytic mechanism, active site coupling
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
substrate channeling and catalytic mechanism, active site coupling
-
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
-
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9031-02-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme E1o is a component of the alpha-ketoglutarate dehydrogenase multienzyme complex KGDH
-
-
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
-
-
strain ATCC 14028, gene ogdh, enzyme E1o is a component of the 2-oxoglutarate dehydrogenase multienzyme complex
SwissProt
-
348910, 348914, 349001, 349005, 349014, 349020, 349021, 349023, 349026, 349027, 349028, 349033, 656591, 656595, 672202, 672280, 676088, 676319, 740480
-
-
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
-
-
-
-
-
enzyme E2 is a component of the 2-oxo acid dehydrogenase multienzyme complex, consisting of enzyme components EC 1.2.4.2, EC 2.3.1.12, and EC 1.8.1.4
-
-
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
-
-
-
-
-
enzyme E2 is a component of the 2-oxoglutarate dehydrogenase multienzyme complex
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
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
physiological function
-
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
physiological function
-
the enzyme is a potent source of reactive oxygen species in liver and cardiac tissue
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-oxoglutarate + CoA + 3-acetylpyridine adenine dinucleotide
succinyl-CoA + CO2 + reduced 3-acetylpyridine adenine dinucleotide
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate + CoA + 3-acetylpyridine adenine dinucleotide
succinyl-CoA + CO2 + reduced 3-acetylpyridine adenine dinucleotide
-
3-acetylpyridine adenine dinucleotide is used instead of NAD+ to avoid concomitant oxidase activity that would degrade NADH produced by the ODH reaction
-
-
?
2-oxoglutarate + CoA + 3-acetylpyridine adenine dinucleotide
succinyl-CoA + CO2 + reduced 3-acetylpyridine adenine dinucleotide
-
3-acetylpyridine adenine dinucleotide is used instead of NAD+ to avoid concomitant oxidase activity that would degrade NADH produced by the ODH reaction
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
addition of glutamate stimulates the synthesis of the 2-oxoglutarate dehydrogenase complex
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
reaction is physiologically irreversible, due to the volatility of CO2
-
-
ir
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
the 2-oxoglutarate dehydrogenase complex catalyzes a critical step in the Krebs tricarboxylic acid cycle, which is also a step in the metabolism of the potentially excitotoxic neurotransmitter glutamate. Deficiencies of the 2-oxoglutarate dehydrogenase complex are likely to impair energy metabolism and therfore brain function, and lead to manifestations of brain disease. Neurons that are enriched in the 2-oxoglutarate dehydrogenase complex may be selectively vulnerable in Alzheimer‘s disease. Variations in 2-oxoglutarate dehydrogenase complex that are not deleterious during reproductive life become deleterious with aging, perhaps by predisposing this mitochondrial metabolon to oxidative damage
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
reductions in enzyme activity occurs in a number of neurodegenerative disorders including Alzheimer‘s disease. The reduction in 2-oxoglutarate dehydrogenase complex activity can be linked to several aspects of brain dysfunction and neuropathology in a number of neurodegenerative diseases
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
catalyzes a rate limiting step of the TCA cycle
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
transcription of the 2-oxoglutarate dehydrogenase component of the 2-oxoglutarate dehydrogenase complex is regulated by glucose and activated by the products of HAP2 and HAP3
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
enzyme of the TCA cycle
-
-
-
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
-
the enzyme contains a covalently attached lipoyl group, which is reductively acylated by enzyme complex component E1, EC 1.2.4.1, the enzyme component E2 catalyzes the subsequent acyl transfer to CoA
-
-
ir
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
the enzyme contains a covalently attached lipoyl group, which is reductively acylated by enzyme component E1, the enzyme component E2 catalyzes the subsequent acyl transfer to CoA
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
reaction significant for energy production, neurotransmitter metabolism, and metabolic interaction between mitochondria and cytoplasm
-
-
?
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
-
the enzyme contains a covalently attached lipoyl group, which is reductively acylated by enzyme complex component E1, EC 1.2.4.1, the enzyme component E2 catalyzes the subsequent acyl transfer to CoA
-
-
ir
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
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
enzyme E2 is a component of the 2-oxoglutarate dehydrogenase multienzyme complex, rate-limiting enzyme in mitochondrial Krebs cycle
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
key step, probably rate-limiting, in the tricarboxylic acid cycle, physiologic function and regulation
-
-
ir
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
-
-
-
-
ir
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
-
the enzyme contains a covalently attached lipoyl group, which is reductively acylated by enzyme complex component E1, EC 1.2.4.1, the enzyme component E2 catalyzes the subsequent acyl transfer to CoA
-
-
ir
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
-
-
-
ir
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
additional information
?
-
-
enzyme complex is also active with 2-oxoadipate
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
enzyme also catalyzes the production of H2O2 in vivo, in vitro, and in situ from 2-oxoglutarate with CoA in absence of NAD+, which inhibits this reaction, enzyme is a atrget for reactive oxygen species and also contributes to generation of oxidative stress in mitochondria when NADH oxidation is impaired, overview
-
-
-
additional information
?
-
-
OdhA can utilize free dihydrodilipoamide to perform the E2 reaction specifically with succinyl-CoA. OdhA specifically catalyzes the E1 and E2 reaction to convert 2-oxoglutarate to succinyl-CoA but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA
-
-
-
additional information
?
-
-
OdhA can utilize free dihydrodilipoamide to perform the E2 reaction specifically with succinyl-CoA. OdhA specifically catalyzes the E1 and E2 reaction to convert 2-oxoglutarate to succinyl-CoA but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA
-
-
-
additional information
?
-
-
the enzyme complex also catalyzes CoASH-dependent oxidation of 2-oxo-4-hydroxyglutarate to malate
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
enzyme activity is reduced in patients with Parkinson's disease due to elevated levels of monoamine oxidase B, physiological effects and regulation, overview
-
-
-
additional information
?
-
-
loss of enzyme activity contributes to the major loss of cerebral energy metabolism leading to a number of neurodegenerative disorders and Alzheimer's disease, myeloperoxidase activity is involved
-
-
-
additional information
?
-
-
reduced enzyme activity in vivo does not lead to the Ca2+ abnormalities observed in patients suffering brain disorders and abnormal mitochondrial function, or Alzheimer's disease, but the release of cytochrome c together with reduced enzyme activity activates other pathways including cell death cascades, enzyme inhibition alters Ca2+ homeostasis and increases cytosolic accumulation of cytochrome c
-
-
-
additional information
?
-
-
the enzyme is targeted for ubiquitination-dependent degradation in mitochondria by binding of Siah2, the RING finger ubiquitin-protein isopeptide ligase 2, encoded by gene siah2
-
-
-
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
?
-
-
KGDHC is an important component of the tricarboxylic acid cycle
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
2-oxoglutarate-supported mitochondrial respiration state 3
-
-
-
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
?
-
-
KGDHC contributes to neuronal reactive oxygen species increase in situ
-
-
-
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
-
-
-
additional information
?
-
-
the KGDH enzyme has also a function as a poly(ADP-ribose) polymerase-like enzyme, which may play a role in regulating intramitochondrial NAD+ and poly(ADP-ribose) homeostasis
-
-
-
additional information
?
-
-
enzyme complex is also active with 2-oxoadipate
-
-
-
additional information
?
-
-
enzyme complex is also active with 2-oxoadipate
-
-
-
additional information
?
-
-
the enzyme complex also catalyzes CoASH-dependent oxidation of 2-oxo-4-hydroxyglutarate to malate
-
-
-
additional information
?
-
-
enzyme also catalyzes the production of H2O2 from 2-oxoglutarate with CoA in absence of NAD+, which inhibits this reaction, enzyme is a atrget for reactive oxygen species and also contributes to generation of oxidative stress in mitochondria when NADH oxidation is impaired, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + lipoamide
S-succinyldihydrolipoamide + CO2
-
addition of glutamate stimulates the synthesis of the 2-oxoglutarate dehydrogenase complex
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
the 2-oxoglutarate dehydrogenase complex catalyzes a critical step in the Krebs tricarboxylic acid cycle, which is also a step in the metabolism of the potentially excitotoxic neurotransmitter glutamate. Deficiencies of the 2-oxoglutarate dehydrogenase complex are likely to impair energy metabolism and therfore brain function, and lead to manifestations of brain disease. Neurons that are enriched in the 2-oxoglutarate dehydrogenase complex may be selectively vulnerable in Alzheimer‘s disease. Variations in 2-oxoglutarate dehydrogenase complex that are not deleterious during reproductive life become deleterious with aging, perhaps by predisposing this mitochondrial metabolon to oxidative damage
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
reductions in enzyme activity occurs in a number of neurodegenerative disorders including Alzheimer‘s disease. The reduction in 2-oxoglutarate dehydrogenase complex activity can be linked to several aspects of brain dysfunction and neuropathology in a number of neurodegenerative diseases
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
catalyzes a rate limiting step of the TCA cycle
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
transcription of the 2-oxoglutarate dehydrogenase component of the 2-oxoglutarate dehydrogenase complex is regulated by glucose and activated by the products of HAP2 and HAP3
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
enzyme of the TCA cycle
-
-
-
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
-
-
-
-
ir
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
-
-
-
-
?
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
-
-
-
-
ir
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
-
enzyme E2 is a component of the 2-oxoglutarate dehydrogenase multienzyme complex, rate-limiting enzyme in mitochondrial Krebs cycle
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
key step, probably rate-limiting, in the tricarboxylic acid cycle, physiologic function and regulation
-
-
ir
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
-
-
-
-
ir
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
-
-
-
-
?
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
O87668
-
-
-
ir
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
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
enzyme also catalyzes the production of H2O2 in vivo, in vitro, and in situ from 2-oxoglutarate with CoA in absence of NAD+, which inhibits this reaction, enzyme is a atrget for reactive oxygen species and also contributes to generation of oxidative stress in mitochondria when NADH oxidation is impaired, overview
-
-
-
additional information
?
-
-
OdhA can utilize free dihydrodilipoamide to perform the E2 reaction specifically with succinyl-CoA. OdhA specifically catalyzes the E1 and E2 reaction to convert 2-oxoglutarate to succinyl-CoA but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA
-
-
-
additional information
?
-
-
OdhA can utilize free dihydrodilipoamide to perform the E2 reaction specifically with succinyl-CoA. OdhA specifically catalyzes the E1 and E2 reaction to convert 2-oxoglutarate to succinyl-CoA but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
enzyme activity is reduced in patients with Parkinson's disease due to elevated levels of monoamine oxidase B, physiological effects and regulation, overview
-
-
-
additional information
?
-
-
loss of enzyme activity contributes to the major loss of cerebral energy metabolism leading to a number of neurodegenerative disorders and Alzheimer's disease, myeloperoxidase activity is involved
-
-
-
additional information
?
-
-
reduced enzyme activity in vivo does not lead to the Ca2+ abnormalities observed in patients suffering brain disorders and abnormal mitochondrial function, or Alzheimer's disease, but the release of cytochrome c together with reduced enzyme activity activates other pathways including cell death cascades, enzyme inhibition alters Ca2+ homeostasis and increases cytosolic accumulation of cytochrome c
-
-
-
additional information
?
-
-
the enzyme is targeted for ubiquitination-dependent degradation in mitochondria by binding of Siah2, the RING finger ubiquitin-protein isopeptide ligase 2, encoded by gene siah2
-
-
-
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
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
2-oxoglutarate-supported mitochondrial respiration state 3
-
-
-
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
?
-
-
KGDHC contributes to neuronal reactive oxygen species increase in situ
-
-
-
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
-
-
-
additional information
?
-
-
the KGDH enzyme has also a function as a poly(ADP-ribose) polymerase-like enzyme, which may play a role in regulating intramitochondrial NAD+ and poly(ADP-ribose) homeostasis
-
-
-
additional information
?
-
-
enzyme also catalyzes the production of H2O2 from 2-oxoglutarate with CoA in absence of NAD+, which inhibits this reaction, enzyme is a atrget for reactive oxygen species and also contributes to generation of oxidative stress in mitochondria when NADH oxidation is impaired, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
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
-
leads to a stabilization of cognitive functions in Alzheimer's disease patients
thiamine diphosphate
-
Km: 0.3 mM; required , 2-oxoglutarate dehydrogenase complex
thiamine diphosphate
-
required , 2-oxoglutarate dehydrogenase complex
thiamine diphosphate
-
2-oxoglutarate dehydrogenase complex contains thiamine diphosphate
thiamine diphosphate
-
required , 2-oxoglutarate dehydrogenase complex
thiamine diphosphate
-
2-oxoglotarate dehydrogenase component of the 2-oxoglutarate dehydrogenase complex is dependent on thiamine diphosphate. Thiamine diphosphate attacks the alpha-carbon of 2-oxoglutarate and decarboxylates the substrate. The thiamine diphosphate reaction adduct then reductively acylates the lipoyl moiety of EC 2.3.1.61; required, 2-oxoglutarate dehydrogenase component
thiamine diphosphate
-
thiamine diphosphate is tightly but not covalently bound to the 2-oxoglutarate dehydrogenase component
thiamine diphosphate
-
formation of a precatalytic complex SE between the substrate and the 2-oxoglutarate dehydrogenase component before the catalytic complex ES, in which the substrate is added to the thiamin diphosphate cofactor
thiamine diphosphate
prosthetic group
thiamine diphosphate
-
activates the 2-oxoglutarate dehydrogenase complex activity, involved in conformational changes
thiamine diphosphate
-
thiamine deficiency results in decreased enzyme complex activity and selective neuronal loss
thiamine diphosphate
-
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine diphosphate
-
-
additional information
-
lipoyl moiety, LipS2, is bound in amide linkage to the epsilon amino group of a lysine residue
-
additional information
-
the complex contains 12.1 mol FAD per mol of enzyme complex; the complex contains 12 lipoyl groups
-
additional information
-
2-oxoglutarate dehydrogenase complex contains FAD; 2-oxoglutarate dehydrogenase complex contains protein-bound lipoic acid
-
additional information
-
EC 1.8.1.4, dihydrolipoyl dehydrogenase component of the 2-oxoglutarate dehydrogenase complex is a flavin protein; EC 2.3.1.61, dihydrolipoamide succinyltransferase component of the 2-oxoglutarate dehydrogenase enzyme complex contains a lipoate moiety that is covalently bound to Lys110 through an epsilon-amide linkage. The thiamine diphosphate reaction adduct then reductively acylates the lipoyl moiety of EC 2.3.1.61
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
additional information
Ca2+
-
0.01 mM, decreases the concentration of 2-oxoglutarate required for half-maximal activity, inhibition at higher concentrations
Ca2+
-
Ca2+ and Mg2+ together synergistically reduce the Km-value for 2-oxoglutarate by over 10fold
Ca2+
-
diminishes the Km value of the 2-oxoglutarate dehydrogenase complex for 2-oxoglutarate in the physiological range, maximal activation, 35%, with 0.004 mM Ca2+
Ca2+
-
activation of OGDH, followed by an increase in oxygen consumption under normoxic conditions, during hypoxia accumulation of Ca2+ in mitochondria
Ca2+
-
3.5 mol of Ca2+-binding sites per mol of 2-oxoglutarate dehydrogenase complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
((+/-)-2-[4-((3-chloro-5-(trifluoromethyl)-2-pyridyl)oxy)-phenoxy]propionic acid)
-
i.e. haloxyfop, grass-specific herbicide
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
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
-
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
Ca2+
-
0.01 mM, decreases the concentration of 2-oxoglutarate required for half-maximal activity, inhibition at higher concentrations
cisplatin
-
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
-
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
hydrogen peroxide
-
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
Na2HPO4
-
50 mM KCl, 38% inhibition of the 2-oxoglutarate dehydrogenase complex
Na2SO4
-
50 mM KCl, 4.5% inhibition of the 2-oxoglutarate dehydrogenase complex
NEM
-
prevents desuccinylation of the 2-oxoglutarate dehydrogenase complex
palmitoyl-CoA
-
is 10-fold less potent than phytanoyl-CoA, no inhibitory effect up to 0.3 mM
phytanoyl-CoA
-
is 10-fold more potent than palmitoyl-CoA, no inhibitory effect up to 0.3 mM
succinyl phosphonate carboxy ethyl ester
-
potent, slow-binding inhibitor of the 2-oxoglutarate dehydrogenase complex, complete inhibition at 0.1 mM
succinyl phosphonate diethyl ester
-
poor inhibitor of the 2-oxoglutarate dehydrogenase complex
succinyl phosphonate phosphono ethyl ester
-
poor inhibitor of the 2-oxoglutarate dehydrogenase complex
triethyl ester of succinyl phosphonate
-
only inhibitory after preincubation, release of charged groups by cellular esterases and activation in intact cells
Tris-HCl
-
50 mM, 26% inhibition of the 2-oxoglutarate dehydrogenase complex
4-oxo-4-phosphonobutanoic acid
-
0.01 mM completely inhibits even in the presence of a 200fold higher concentration of its substrate 2-oxoglutarate
4-oxo-4-phosphonobutanoic acid
-
affects (1-13C)glucose and (U-13C)glutamate metabolism, phosphonoethyl and carboxy ethyl ester reduce the concentration of aspartate, alanine and gamma-aminobutyric acid, phosphonoethyl ester reduces gluthatione content, carboxy ethyl ester reduces the intracellular concentration of valine and leucine
4-[(2-carboxyethoxy)(hydroxy)phosphoryl]-4-oxobutanoic acid
-
0.01 mM completely inhibits even in the presence of a 200fold higher concentration of its substrate 2-oxoglutarate
4-[(2-carboxyethoxy)(hydroxy)phosphoryl]-4-oxobutanoic acid
-
0.01 mM produce 70% inhibition
4-[ethoxy(hydroxy)phosphoryl]-4-oxobutanoic acid
-
0.01 mM completely inhibits even in the presence of a 200fold higher concentration of its substrate 2-oxoglutarate
4-[ethoxy(hydroxy)phosphoryl]-4-oxobutanoic acid
-
0.01 mM produce 70% inhibition
H2O2
-
addition outside of cells reduces KGDHC activity in proportion to the increase in reactive oxygen species
H2O2
-
inhibits lysate KGDHC in a concentration- and time-dependent manner, inhibitory effect reversed by addition of dithiothreitol
hypochlorous acid
-
myeloperoxidase product, inhibition of the alpha-ketoglutarate dehydrogenase multienzyme complex in vivo
hypochlorous acid
-
inhibits at concentrations ca. 50 times less than the effective mono-N-chloramine concentrations; myeloperoxidase product, inhibition of the alpha-ketoglutarate dehydrogenase multienzyme complex in vitro
K+
-
50 mM KCl, 63% inhibition of the 2-oxoglutarate dehydrogenase complex
KMV
-
inhibits KGDHC in PC-12 cells and does not alter mitochondrial membrane potential, but is associated with the release of cytochrome-c from mitochondria into the cytosol, reduction in basal cytosolic Ca2+, and diminishing endoplasmic reticulum calcium stores
mono-N-chloramine
-
myeloperoxidase product, inhibition of the alpha-ketoglutarate dehydrogenase multienzyme complex in vivo
mono-N-chloramine
-
inhibits both lysate and in situ KGDHC activities in a concentration-dependent manner in three distinct phases
mono-N-chloramine
-
inhibits in a time- and concentration-dependent manner; myeloperoxidase product, inhibition of the alpha-ketoglutarate dehydrogenase multienzyme complex in vitro
Na+
-
50 mM NaCl, 34% inhibition of the 2-oxoglutarate dehydrogenase complex
NADH
-
0.1 mM, 50% inhibition. 0.2 mM AMP completely overcomes the inhibition
NADH
-
directly inhibits the partial reaction catalyzed by the resolved 2-oxoglutarate dehydrogenase component. Ca2+, ADP or NAD+ decrease NADH inhibition
NH4+
-
50 mM NH4Cl, 21% inhibition of the 2-oxoglutarate dehydrogenase complex
NH4+
-
3 mM NH4Cl, enzyme activity in nonsynaptic mitochondria: 21% decrease of Vmax, 35% decrease of Km for 2-oxoglutarate. In synaptic mitochondria thioacetamide-induced encephalopathy produces an 84% increase in Vmax and a 35% decrease of KM for 2-oxoglutarate
reactive oxygen species
-
alpha-KGDH can generate reactive oxygen species during its catalytic function, which is regulated by the NADH/NAD+ ratio, formation by alpha-KGDH is attributed to the E3 subunit
-
reactive oxygen species
-
aconitase in the Krebs cycle is more vulnerable than alpha-KGDH to reactive oxygen species, alpha-KGDH can generate reactive oxygen species during its catalytic function, which is regulated by the NADH/NAD+ ratio, as long as alpha-KGDH is functional NADH generation in the Krebs cycle is maintained
-
succinyl phosphonate
-
OGDHC inhibitor competitive to 2-oxoglutarate, 0.005 mM succinyl phosphonate protects OGDHC from catalysis-induced inactivation
succinyl phosphonate
-
specific inhibitor of cellular KGDHC, 20% inhibition at 0.2 mM
succinyl phosphonate
-
potent, slow-binding inhibitor of the 2-oxoglutarate dehydrogenase complex, complete inhibition at 0.1 mM
succinyl phosphonate triethyl ester
-
specific inhibitor of cellular KGDHC, 44% inhibition at 0.5 mM
tryptamine-4,5-dione
-
rapid inhibition, 87.7% reduced activity at 0.1 mM, inhibition is blocked by reduced glutathione or cysteine at large molar excess, ascorbate protects partially, inhibition is not affected by catalase and superoxide dismutase
Zn2+
-
may play a role in the inhibition of alpha-KGDH during ischemia or reperfusion, is present in elavated concentrations in such cells
Zn2+
-
inhibition of the 2-oxoglutarate dehydrogenase complex requires enzyme cycling and is reversed by EDTA. Reversibility is inversely related to the duration of exposure and the concentration of Zn2+. Physiological free Zn2+ may modulate hepatic mitochondrial respiration by reversible inhibition of the 2-oxoglutarate dehydrogenase complex
additional information
-
ethyl 4-[ethoxy(hydroxy)phosphoryl]-4-oxobutanoate and triethyl esters of succinyl phosphonate are ineffective
-
additional information
-
inhibition of the alpha-ketoglutarate dehydrogenase complex alters mitochondrial function and cellular calcium regulation
-
additional information
-
enzyme activity is reduced by 40% in PC12 cells treated with doxycyclin, which is reversible by deprenyl, monoamine oxidase-B-mediated enzyme inhibition, Ca2+ levels influence the NADH/NAD+ pool, which influences the enzyme
-
additional information
-
the enzyme is targeted for ubiquitination-dependent degradation in mitochondria by binding of Siah2, the RING finger ubiquitin-protein isopeptide ligase 2, encoded by gene siah2
-
additional information
-
KGDH is sharply decreased in cells challenged with menadione, treatment of cellular extracts from the menadione-exposed cells with 5 mM dithiothreitol partially restores the activity of KGDH, KGDH levels are diminished when ammonium is utilized as the nitrogen source
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
NH4+
-
in synaptic mitochondria thioacetamide-induced encephalopathy produces an 84% increase in Vmax and a 35% decrease of KM for 2-oxoglutarate
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+
thiamine diphosphate
-
KGDHC is saturated with endogenous tightly bound thiamine diphosphate, but the addition of exogenous thiamine diphosphate to the reaction medium leads to a marked increase in KGDHC affinity to 2-oxoglutarate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
2-oxoglutarate
-
in 50 mM TES (pH 7.7), 10 mM MgCl2, 3 mM L-cysteine, 2 mM NAD+, 0.9 mM thiamine diphosphate, 0.05 mM chlorpromazine, and 1.5 mM 2-oxoglutarate, temperature not specified in the publication
additional information
additional information
-
two substrate-binding modes are revealed at different degrees of saturation of the enzyme with 2-oxoglutarate. At low substrate concentrations, 0.001-0.01 mM, the binding mainly depends on the interaction of the enzyme with the substrate carbonyl groups. At 0.1-1 mM the relative contribution of the 2-oxo group in the binding increases
-
additional information
additional information
-
kinetic study, reaction of 2-oxoglutarate dehydrogenase complex
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
NADH
-
competitive inhibition with respect to NAD+, 2-oxoglutarate dehydrogenase complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
specific activity of the 2-oxoglutarate dehydrogenase complex
additional information
-
specific activity of the 2-oxoglutarate dehydrogenase complex
additional information
-
specific activity of the 2-oxoglutarate dehydrogenase complex
additional information
-
specific activity of the 2-oxoglutarate dehydrogenase complex
additional information
-
specific activity of the 2-oxoglutarate dehydrogenase complex
additional information
-
specific activity of the 2-oxoglutarate dehydrogenase complex
additional information
-
specific activity of the 2-oxoglutarate dehydrogenase complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7
-
oxidation of 2-oxo-4-hydroxyglutarate or 2-oxoglutarate by the 2-oxoglutarate dehydrogenase complex
7.4
8
-
oxidation of 2-oxo-4-hydroxyglutarate or 2-oxoglutarate by the 2-oxoglutarate dehydrogenase complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
6.5 - 8
-
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
6.5 - 8.5
-
pH 6.5: about 60% of maximal activity, pH 8.5: about 30% of maximal activity, 2-oxoglutarate dehydrogenase complex
6.5 - 8.5
-
pH 6.5: about 25% of maximal activity, pH 8.5: about 30% of maximal activity, 2-oxoglutarate dehydrogenase complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 45
-
20°C: about 35% of maximal activity, 45°C: about 20% of maximal activity, 2-oxoglutarate dehydrogenase complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
The HEK-293 subline E2k-67 shows about 30% reduced KGDHC activity; control line E2k-100
-
highest activity found in rapidly growing mycelium, glucose-NH4+ or glucose-peptone medium
additional information
-
endothelial cells have about six times higher activity than do brain microglial cells or neurons
-
,neurons that appear slectively vulnerable in human temporal cortex in Alzheimer‘s disease are enriched in the 2-oxoglutarate dehydrogenase complex
-
diminished activities in regions with severe pathology, as well as in areas of minimal pathology, activity declines with the severity of disease
-
-
348910, 348914, 349005, 349014, 349020, 349021, 349023, 349026, 349027, 349028, 349033, 656591, 656595, 672280, 676088, 676319, 740480
additional information
-
tenfold increase in 2-oxoglutarate dehydrogenase complex activity between the amoeba stage and the aggregation stage, 2fold increase between the aggregation stage and the sorocarp stage
additional information
-
2-oxoglutarate dehydrogenase-like protein is not detected in heart
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
enzyme complex is expressed during erythrocytic stage of the parasite
-
-
enzyme E2 overexpression or disruption of mitochondrial membrane potential causes enzyme E2 release from mitochondria to cytoplasm where it is degraded
-
alpha-ketoglutarate dehydrogenase is heterogeneously distributed in mitochondria within individual astrocytes originating either from cerebellum or cerebral cortex
-
enzyme E1o contains mitochondrial targeting sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Mus musculus;
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
A0R2B1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
A0R2B1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
A0R2B1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
A0R2B1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
A0R2B1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
A0R2B1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
x * 110000, about, E1o component, sequence calculation, x * 30000, recombinant N-terminal catalytic domain, SDS-PAGE
100000
-
4 * 100000, active 2-oxoglutarate dehydrogenase component, SDS-PAGE
103000
-
x * 103000, 2-oxoglutarate dehydrogenase subunit, SDS-PAGE
104805
-
x * 104805, 2-oxoglutarate dehydrogenase subunit, calculation from nucleotide sequence
105687
-
x * 105687, 2-oxoglutarate dehydrogenase subunit, calculation from nucleotide sequence
110000
360000
-
active 2-oxoglutarate dehydrogenase component, gel filtration
additional information
110000
x * 110000, about, E1o component, sequence calculation, x * 30000, recombinant N-terminal catalytic domain, SDS-PAGE
additional information
-
2400000 Da is the MW of the 2-oxoglutarate dehydrogenase complex
additional information
-
7000000 Da is the MW of the 2-oxoglutarate dehydrogenase complex, gel filtration
additional information
-
2600000 Da is the MW of the 2-oxoglutarate dehydrogenase complex, calculation from sedimentation and diffusion data
additional information
-
2700000 is the MW of the 2-oxoglutarate dehydrogenase complex, gel filtration; 2800000 Da is the MW of the 2-oxoglutarate dehydrogenase complex, calculation from sedimentation and diffusion data
additional information
-
2470000 Da is the MW of the 2-oxoglutarate dehydrogenase complex, sucrose density gradient centrifugation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
-
4 * 100000, active 2-oxoglutarate dehydrogenase component, SDS-PAGE
additional information
?
-
x * 103000, 2-oxoglutarate dehydrogenase subunit, SDS-PAGE; x * 105687, 2-oxoglutarate dehydrogenase subunit, calculation from nucleotide sequence
?
-
x * 104805, 2-oxoglutarate dehydrogenase subunit, calculation from nucleotide sequence
?
x * 110000, about, E1o component, sequence calculation, x * 30000, recombinant N-terminal catalytic domain, SDS-PAGE
additional information
-
in solution at pH 7.0, the 2-oxoglutarate dehydrogenase component exists as a stable dimer
additional information
-
the complex constists of 12 chains of E1, EC 1.2.4.2, 12 chains of E2, EC 2.3.1.61 and 12 chains of E3, EC 1.8.1.4
additional information
the catalytic domain of E1o is located at the N-terminus
additional information
-
structure of the 2-oxoglutarate dehydrogenase complex: E1 (EC 1.2.4.2): 12 subunits per complex (each with 113000 Da), E2 (EC 2.3.1.61): 24 subunits per complex (each with 48000 Da), E3 (EC 1.8.1.4): 12 subunits per complex (each with 55000 Da)
additional information
-
biochemical and microsopic data indicate that the complex is a mosaic comprising 1 molecule of lipoate succinyltransferase, 6 molecules of 2-oxoglutarate dehydrogenase and 6 molecules of lipoamide dehydrogenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
the precursor of 2-oxoglutarate dehydrogenase component of the complex has a MW of 98000 Da, compared to 96000 Da of the mature form
proteolytic modification
-
the initial cytoplasmic translation product of the 2-oxoglutarate dehydrogenase component of the complex is 1500-3000 Da greater than in the mature enzyme
proteolytic modification
-
enzyme contains a mitochondrial targeting sequence which is cleaved off in the mitochondria resulting in the mature enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method with 12% (w/v) polyethylene glycol 4000, 50 mM sodium citrate (pH 5.6)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21
-
60 min, about 65% loss of activity, 2-oxoglutarate dehydrogenase complex
30
-
60min, about 80% loss of activity, 2-oxoglutarate dehydrogenase complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate dehydrogenase complex is stabilized by glycerol, Mg2+ and thiamine diphosphate
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 2-oxoglutarate dehydrogenase complex, 5-15% loss of activity after several months
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
expressed in Escherichia coli BL21(DE3) cells
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
-
gene odhL encodes the 2-oxoglutarate dehydrogenase component of the multienenzyme complex, expression in Escherichia coli in kgdA mutant of Pseudomonas putida JS347
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H352C/Q356D
-
the mutations fully prevent succinyltransferase activity
H352C/Q356D
-
the mutations fully prevent succinyltransferase activity
-
additional information
additional information
-
mutant deltapknG has a defect in glutamine utilization, which is abolished by additional deletion of odhI, mutant deltaodhI transformed with plasmid OdhI-T14A has a defect in glutamine utilization
additional information
-
siah2 is the RING finger ubiquitin-protein isopeptide ligase 2, 2-oxoglutarate dehydrogenase component E2 expression and activity are elevated in siah2-/- cells deficient in siah2 expression compared to siah2+/+ cells
additional information
-
patients bearing the APP670/671 mutation show declined KGDHC activity
additional information
-
knock-out mice, deficient in dihydrolipoyl dehydrogenase, show reduced 2-oxoglutarate dehydrogenase activity and reduced H2O2 production
additional information
-
thiamine diphosphate deficiency diminishes KGDHC activity, knockouts of eNOS or ICAM-1 diminish oxidative stress and reduce neuronal death in thiamine-deficient mice, knockouts of E3 have diminished KGDHC in brain and liver
additional information
-
heterozygous knockout mice deficient in the E3 subunit produce significantly less H2O2 than mitochondria form their littermate wild-type mice
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
medicine
-
hypochlorous acid and chloramines have the potential to inactivate KGDHC, a major target in neurodegeneration, without significant loss of cellular viability
medicine
-
hypochlorous acid and chloramines have the potential to inactivate KGDHC, a major target in neurodegeneration
medicine
-
succinyl phosphonate and its esters may be useful in studying the effects of reduced KGDHC activity on neuronal and brain function
medicine
-
succinyl phosphonate and its esters may be useful in studying the effects of reduced KGDHC activity on neuronal and brain function
medicine
-
susceptibility of KGDHC to inactivation in kidney cells exposed to cisplatin metabolites my be due to the proximity of mitochondrial aspartate aminotransferase to KGDHC in mitochondria, mitochondrial aspartate aminotransferase may catalyze a beta-lyase reaction with the cisplatin-cysteine S-conjugate, converting cisplatin to a toxicant
medicine
-
key regulatory branch points of mitochondrial metabolism are targets of a cellular derivative of phytanic acid, decreased activity of the complexes may contribute to neurological symptoms upon accumulation of phytanic acid in Refsum disease
medicine
-
potential of succinyl phosphonate esters for modeling the biochemical and pathophysiological consequences of reduced KGDHC activity in brain diseases
medicine
-
KGDHC is diminished in brains from patients with Alzheimers's disease, Parkinson's disease, Huntington's disease, Wernicke-Korskoff disease, and progressive supranuclear palsy, not diminished in brains of patients that died with schizophrenia, reduced KDGDHC may be a better indicator of the primary reactive oxygen species action than commonly used measures of oxidative stress
medicine
-
loss of KGDHC activity resulting from the lack of thiamine diphosphate coenzyme may lead to oxidative stress and to neuronal death both directly and by predisposing to other insults
medicine
-
altered in the post-mortem substantia nigra samples from patients suffering from Parkinson's disease, decreased activity in the brain of Alzheimer's disease patients, involving regions affected by the disease as well as regions that remain normal, reduced activity or increased vulnerability to oxidative stress in fibroblasts from patients with presenlilin-1 mutation
additional information
-
alpha-ketoglutarate-involving reactions belong to the backbone of high-flux reactions, which is rather conserved in evolution
additional information
-
in post-mortem mice brain samples the activity is quickly lost, whereas the activity of another TPP-dependent enzyme, PDH, remains unalterd for at least 24 h
Show AA Sequence (5049 entries)
Longer loading times are possible. Please use the Sequence Search for a specific query.
Longer loading times are possible. Please use the Sequence Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.