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

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

EC NUMBER
COMMENTARY
1.2.4.2
-
RECOMMENDED NAME
GeneOntology No.
oxoglutarate dehydrogenase (succinyl-transferring)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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
Gluconacetobacter xylinus
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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
Gluconacetobacter xylinus
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
substrate channeling and catalytic mechanism, active site coupling
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
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
Acinetobacter sp. 4B
-
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
2-oxoglutarate decarboxylation to succinyl-CoA
-
2-oxoglutarate dehydrogenase complex
-
Biosynthesis of secondary metabolites
-
Citrate cycle (TCA cycle)
-
Lysine degradation
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Tryptophan metabolism
-
SYSTEMATIC NAME
IUBMB Comments
2-oxoglutarate:[dihydrolipoyllysine-residue succinyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-succinylating)
Contains thiamine diphosphate. It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, dihydrolipoyllysine-residue succinyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-ketoglutarate dehydrogenase
-
-
-
-
2-ketoglutarate dehydrogenase
-
-
2-OGDH
-
-
-
-
2-oxoglutarate decarboxylase
-
-
2-oxoglutarate decarboxylase
-
part of the 2-oxoglutarate dehydrogenase complex
2-oxoglutarate dehydrogenase
-
-
-
-
2-oxoglutarate dehydrogenase
-
-
2-oxoglutarate dehydrogenase
-
-
2-oxoglutarate dehydrogenase
Corynebacterium glutamicum ATCC13869
-
-
-
2-oxoglutarate dehydrogenase
-
-
2-oxoglutarate dehydrogenase
-
-
2-oxoglutarate dehydrogenase
Q96HY7, Q9ULD0
-
2-oxoglutarate dehydrogenase
-
-
2-oxoglutarate dehydrogenase
-
-
2-oxoglutarate dehydrogenase
-
first and rate-limiting component of the multienzyme 2-oxoglutarate dehydrogenase complex
2-oxoglutarate dehydrogenase
Q87668
-
2-oxoglutarate dehydrogenase complex
-
-
2-oxoglutarate dehydrogenase complex
-
-
2-oxoglutarate dehydrogenase complex
-
-
2-oxoglutarate dehydrogenase complex
-
-
2-oxoglutarate dehydrogenase complex
-
tricarboxylic acid cycle multienzyme
2-oxoglutarate dehydrogenase-like protein
-
brain-specific isozyme
2-oxoglutarate:lipoate oxidoreductase
-
-
-
-
AKGDH
-
-
-
-
alpha-KDE2
-
-
alpha-ketoglutarate dehydrogenase
-
-
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase
-
-
alpha-ketoglutarate dehydrogenase complex
-
-
alpha-ketoglutarate dehydrogenase complex
-
-
alpha-ketoglutarate dehydrogenase complex
-
-
alpha-ketoglutarate dehydrogenase complex
-
-
alpha-ketoglutarate dehydrogenase complex
-
-
alpha-ketoglutarate dehydrogenase complex
-
-
alpha-ketoglutarate dehydrogenase complex
-
-
alpha-ketoglutarate dehydrogenase complex
-
-
alpha-ketoglutarate dehydrogenase complex
-
enzyme in complex with pyruvate dehydrogenase
alpha-ketoglutarate dehydrogenase complex
-
-
alpha-ketoglutarate dehydrogenase complex
-
-
alpha-ketoglutarate dehydrogenase complex
-
-
alpha-ketoglutarate dehydrogenase multienzyme complex
-
-
alpha-ketoglutaric acid dehydrogenase
-
-
-
-
alpha-ketoglutaric dehydrogenase
-
-
-
-
alpha-KGD
-
-
-
-
alpha-KGDH
-
-
alpha-KGDH
-
-
alpha-KGDHC
-
-
alpha-oxoglutarate dehydrogenase
-
-
-
-
dehydrogenase, oxoglutarate
-
-
-
-
DHTKD1
Q96HY7
2-oxoglutarate dehydrogenase-like hypothetical protein
dihydrolipoyl succinyltransferase E2
-
part of the multisubunit alpha-ketoglutarate dehydrogenase complex
E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex
-
-
E1 subunit of the alpha-ketoglutarate dehydrogenase complex
-
-
E1k
-
-
E1k
-
part of the alpha-ketoglutarate dehydrogenase complex
E1o
-
component of the alpha-ketoglutarate dehydrogenase multienzyme complex KGDH consisting of components E1o, EC 1.2.4.2, E2, EC 2.1.3.6, and E3, EC 1.8.1.4
E1o
Q87668
component of the 2-oxoglutarate dehydrogenase multienzyme complex
E1o component
-
-
E1o component 2-oxoglutarate dehydrogenase complex
-
-
E2
-
component of the 2-oxo acid dehydrogenase multienzyme complex
ketoglutaric dehydrogenase
-
-
-
-
KG dehydrogenase
-
-
KGDH
-
KGDH is a multienzyme complex that consists of multiple copies of three subunits: E1 (alpha-ketoacid decarboxylase), E2(dihydrolipoyl transacetylase), and E3 (dihydrolipoamide dehydrogenase)
KGDHC
-
-
KGDHC
-
-
ODH
Corynebacterium glutamicum ATCC 13032, Corynebacterium glutamicum ATCC13869
-
-
-
OGDC
-
-
-
-
OGDC
-
-
OGDH
-
part of the 2-oxoglutarate dehydrogenase complex multienzyme system
OGDHL
Q9ULD0
2-oxoglutarate dehydrogenase-like hypothetical protein
OGDHL
-
brain-specific isozyme
OGHDC-E2
-
component of the 2-oxoglutarate dehydrogenase multienzyme complex
oxoglutarate decarboxylase
-
-
-
-
oxoglutarate dehydrogenase
-
-
-
-
oxoglutarate dehydrogenase
-
-
oxoglutarate dehydrogenase
-
-
-
oxoglutarate dehydrogenase
-
-
PDHC
-
enzyme in complex with alpha-ketoglutarate dehydrogenase
additional information
-
enzyme is part of the alpha-ketoglutarate dehydrogenase complex KGDHC
CAS REGISTRY NUMBER
COMMENTARY
9031-02-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain 4B
-
-
Manually annotated by BRENDA team
Acinetobacter sp. 4B
strain 4B
-
-
Manually annotated by BRENDA team
enzyme E2 is a component of the 2-oxo acid dehydrogenase multienzyme complex, consisting of enzyme components EC 1.2.4.1, EC 1.2.4.2, EC 2.3.1.12, and EC 1.8.1.4
-
-
Manually annotated by BRENDA team
2-oxoglutarate dehydrogenase complex
-
-
Manually annotated by BRENDA team
strain ATCC13869
-
-
Manually annotated by BRENDA team
Corynebacterium glutamicum ATCC13869
strain ATCC13869
-
-
Manually annotated by BRENDA team
enzyme E2 is a component of the 2-oxo acid dehydrogenase multienzyme complex, consisting of enzyme components EC 1.2.4.2, EC 2.3.1.12, and EC 1.8.1.4
-
-
Manually annotated by BRENDA team
enzyme E2 is a component of the 2-oxo acid dehydrogenase multienzyme complex, consisting of enzyme components EC 1.2.4.1, EC 1.2.4.2, EC 2.3.1.12, and EC 1.8.1.4
-
-
Manually annotated by BRENDA team
Gluconacetobacter xylinus
-
-
-
Manually annotated by BRENDA team
enzyme E2 is a component of the 2-oxoglutarate dehydrogenase multienzyme complex
-
-
Manually annotated by BRENDA team
enzyme is part of the alpha-ketoglutarate dehydrogenase complex KGDHC
-
-
Manually annotated by BRENDA team
wild-type mice, and knock-out mice deficient in dihydrolipoyl dehydrogenase
-
-
Manually annotated by BRENDA team
no activity in Mycobacterium tuberculosis
-
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
enzyme E1o is a component of the alpha-ketoglutarate dehydrogenase multienzyme complex KGDH
-
-
Manually annotated by BRENDA team
strain ATCC 13525
-
-
Manually annotated by BRENDA team
enzyme E2 is a component of the 2-oxo acid dehydrogenase multienzyme complex, consisting of enzyme components EC 1.2.4.1, EC 1.2.4.2, EC 2.3.1.12, and EC 1.8.1.4
-
-
Manually annotated by BRENDA team
enzyme is in complex with pyruvate dehydrogenase
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
strain ATCC 14028, gene ogdh, enzyme E1o is a component of the 2-oxoglutarate dehydrogenase multienzyme complex
SwissProt
Manually annotated by BRENDA team
cultivar Desiree
-
-
Manually annotated by BRENDA team
cv. romano
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
the enzyme is bifunctional, both as a metabolic enzyme and as a mitochondrial inheritance factor necessary for the distribution of kinetoplast DNA networks to daughter cells at cytokinesis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + CoA
? + H2O2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + 3-acetylpyridine adenine dinucleotide
succinyl-CoA + CO2 + reduced 3-acetylpyridine adenine dinucleotide
show the reaction diagram
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC13869
-
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 + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
P0AFG3
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
Q87668
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
Q96HY7, Q9ULD0
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
enzyme E2 is a component of the 2-oxoglutarate dehydrogenase multienzyme complex, rate-limiting enzyme in mitochondrial Krebs cycle
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
key step, probably rate-limiting, in the tricarboxylic acid cycle, physiologic function and regulation
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
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 + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
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 + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
reaction significant for energy production, neurotransmitter metabolism, and metabolic interaction between mitochondria and cytoplasm
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
Pigeon
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
Gluconacetobacter xylinus
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
reaction is physiologically irreversible, due to the volatility of CO2
-
-
ir
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
catalyzes a rate limiting step of the TCA cycle
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
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
show the reaction diagram
-
addition of glutamate stimulates the synthesis of the 2-oxoglutarate dehydrogenase complex
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
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
show the reaction diagram
-
enzyme of the TCA cycle
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
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
show the reaction diagram
Acinetobacter sp. 4B
-
-
-
-
?
additional information
?
-
-
-
-
-
-
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
?
-
-
2-oxoglutarate-supported mitochondrial respiration state 3
-
-
-
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
?
-
-
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
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
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
?
-
-
KGDHC is an important component of the tricarboxylic acid cycle
-
-
-
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
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
Q87668
-
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
enzyme E2 is a component of the 2-oxoglutarate dehydrogenase multienzyme complex, rate-limiting enzyme in mitochondrial Krebs cycle
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
key step, probably rate-limiting, in the tricarboxylic acid cycle, physiologic function and regulation
-
-
ir
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
catalyzes a rate limiting step of the TCA cycle
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
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
show the reaction diagram
-
addition of glutamate stimulates the synthesis of the 2-oxoglutarate dehydrogenase complex
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
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
show the reaction diagram
-
enzyme of the TCA cycle
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
show the reaction diagram
-
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
-
-
-
additional information
?
-
-
2-oxoglutarate-supported mitochondrial respiration state 3
-
-
-
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
?
-
-
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
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
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
?
-
-
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
?
-
-
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
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
-
covalently bound to the enzyme
thiamine diphosphate
-
required , 2-oxoglutarate dehydrogenase complex
thiamine diphosphate
-
required , 2-oxoglutarate dehydrogenase complex
thiamine diphosphate
-
required , 2-oxoglutarate dehydrogenase complex
thiamine diphosphate
-
Km: 0.3 mM; required , 2-oxoglutarate dehydrogenase complex
thiamine diphosphate
-
required , 2-oxoglutarate dehydrogenase complex
thiamine diphosphate
Gluconacetobacter xylinus
-
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
-
-
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
-
-
thiamine diphosphate
Q87668
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 diphosphate
-
-
thiamine diphosphate
-
-
thiamine diphosphate
P0AFG3
dependent
thiamine diphosphate
-
thiamine deficiency reduces the activity of the alpha-ketoglutarate dehydrogenase complex
thiamine diphosphate
Q96HY7, Q9ULD0
;
thiamine diphosphate
-
-
thiamine diphosphate
-
-
thiamine diphosphate
-
dependent on
lipoic acid
-
increases KGDHC activity in aged rates
additional information
-
lipoyl moiety, LipS2, is bound in amide linkage to the epsilon amino group of a lysine residue
-
additional information
Gluconacetobacter xylinus
-
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
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ADP
-
activates through allosteric binding
Ca2+
-
3.5 mol of Ca2+-binding sites per mol of 2-oxoglutarate dehydrogenase complex
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+
-
activates
Ca2+
-
0.01 mM, decreases the concentration of 2-oxoglutarate required for half-maximal activity, inhibition at higher concentrations
Ca2+
-
activates
Ca2+
-
no activation
Ca2+
-
Ca2+ and Mg2+ together synergistically reduce the Km-value for 2-oxoglutarate by over 10fold
Ca2+
-
activates the 2-oxoglutarate dehydrogenase complex activity
Ca2+
-
-
Ca2+
-
activates both catalytic function and H2O2 production
Ca2+
-
-
Ca2+
-
-
Ca2+
-
-
Ca2+
-
activation of OGDH, followed by an increase in oxygen consumption under normoxic conditions, during hypoxia accumulation of Ca2+ in mitochondria
Ca2+
-
dependent on, activates through allosteric binding
Ca2+
-
dependent on
Mg2+
-
maximal activation, 75%, with 5 mM
Mg2+
-
required, 2-oxoglutarate dehydrogenase complex
Mg2+
Gluconacetobacter xylinus
-
required, 2-oxoglutarate dehydrogenase complex
Mg2+
-
activates 2-oxoglutarate dehydrogenase complex
Mg2+
-
required, 2-oxoglutarate dehydrogenase complex
Mg2+
-
-
Mn2+
-
activates the 2-oxoglutarate dehydrogenase complex activity
Mn2+
-
-
additional information
-
Ca2+ is no activator
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
((+/-)-2-[4-((3-chloro-5-(trifluoromethyl)-2-pyridyl)oxy)-phenoxy]propionic acid)
-
i.e. haloxyfop, grass-specific herbicide
(R)-2-amino-3-((1,1,2,2-tetrafluoroethyl)thio)propanoic acid
-
inactivates
1,2,3,4-tetrahydroisoquinoline
-
IC50: 18.2
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
-
1-methyl-4-phenylpyridine
-
i.e. MPP+
1-methyl-4-phenylpyridinium
-
IC50: 18.9 mM
1-methyl-4-phenylpyridinium
-
-
1-oxo-3-carboxypropylphosphonic acid methyl ester
-
-
2-oxo-3-methyl-n-valeric acid
-
inhibition of the 2-oxoglutarate dehydrogenase enzyme complex in vivo and in situ, after 40 min 25% inhibition at 10 mM, 46% at 20 mM, after 80 min 58% inhibition at 10 mM, 80% at 20 mM, inhibition does not affect the mitochondrial membrane potential
2-oxo-3-methylpentanoate
-
2-oxoglutarate dehydrogenase complex
2-oxoglutarate
-
2-oxoglutarate dehydrogenase complex
2-oxoglutarate
-
substrate inhibition above 4 mM
2-Oxoisohexanoate
-
2-oxoglutarate dehydrogenase complex
2-oxoisopentanoate
-
2-oxoglutarate dehydrogenase complex
3-nitropropionic acid
-
-
4-hydroxy-2-nonenal
-
-
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
-
0.01 mM produce 70% inhibition
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
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
acetaldehyde
-
2-oxoglutarate dehydrogenase complex
amyloid-beta peptide
-
-
-
arsenite
-
probably bind the dithiol group in the lipoic acid
ATP
-
2-oxoglutarate dehydrogenase complex
ATP
-
inhibits KGDHC in the kidney, in adrenals the effect is rather weak
ATP
-
weakly inhibits in breast muscles
ATP
-
inhibits KGDHC in the heart
Benzene-1,3-dicarboxylate
-
-
Benzene-1,4-dicarboxylate
-
-
Ca2+
-
0.01 mM, decreases the concentration of 2-oxoglutarate required for half-maximal activity, inhibition at higher concentrations
Cd2+
-
probably bind the dithiol group in the lipoic acid
cis-aconitate
-
2-oxoglutarate dehydrogenase complex
cis-aconitate
-
2-oxoglutarate dehydrogenase complex
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
glyoxylate
-
2-oxoglutarate dehydrogenase complex
glyoxylate
-
2-oxoglutarate dehydrogenase complex
H2O2
-
inhibits lysate KGDHC in a concentration- and time-dependent manner, inhibitory effect reversed by addition of dithiothreitol
H2O2
-
ca. 300 times less effective than mono-N-chloramine
H2O2
-
addition outside of cells reduces KGDHC activity in proportion to the increase in reactive oxygen species
H2O2
-
oxidative damage to KGDHC
H2O2
-
1 h treatment with H2O2 decreases KGDHC activity
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
hypochlorous acid
-
myeloperoxidase product, inhibition of the alpha-ketoglutarate dehydrogenase multienzyme complex in vivo
hypochlorous acid
-
concentration-dependent monophasic inhibition
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
Isoquinoline
-
IC50: 6.5 mM
isoquinoline derivative
-
-
-
K+
-
50 mM, 56% inhibition, 2-oxoglutarate dehydrogenase complex
K+
-
50 mM KCl, 63% inhibition of the 2-oxoglutarate dehydrogenase complex
KMV
-
severely inhibits KGDHC activity
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
N-methyl-1,2,3,4-tetrahydroisoquinoline
-
IC50: 2 mM
N-methylisoquinolinium
-
-
N-n-propylisoquinolinium
-
IC50: 3 mM
Na+
-
50 mM, 48% inhibition, 2-oxoglutarate dehydrogenase complex
Na+
-
50 mM NaCl, 34% inhibition of the 2-oxoglutarate dehydrogenase complex
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
NAD+
-
inhibits H2O2 production reaction of the enzyme
NADH
-
2-oxoglutarate dehydrogenase complex
NADH
-
directly inhibits the partial reaction catalyzed by the resolved 2-oxoglutarate dehydrogenase component. Ca2+, ADP or NAD+ decrease NADH inhibition
NADH
-
2-oxoglutarate dehydrogenase complex
NADH
Gluconacetobacter xylinus
-
-
NADH
-
2-oxoglutarate dehydrogenase complex
NADH
-
0.1 mM, 50% inhibition. 0.2 mM AMP completely overcomes the inhibition
NADH
-
allosteric inhibition
NADH
-
allosteric inhibitor, inhibition relieved by micromolar Ca2+ and ADP
NADPH
-
2-oxoglutarate dehydrogenase complex
NEM
Gluconacetobacter xylinus
-
prevents desuccinylation of the 2-oxoglutarate dehydrogenase complex
NH4+
-
50 mM, 70% inhibition, 2-oxoglutarate dehydrogenase complex
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
OdhI
-
unphosphorylated OdhI strongly inhibits ODH activity
-
oxalacetate
-
2-oxoglutarate dehydrogenase complex
oxalacetate
-
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
-
Pyridine-2,4-dicarboxylate
-
-
Pyridine-2,5-dicarboxylate
-
-
pyruvate
-
2-oxoglutarate dehydrogenase complex
reactive oxygen species
-
-
-
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
-
ruthenium red
-
abolishes the Ca-stimulation of OGDH
succinate
-
2-oxoglutarate dehydrogenase complex
succinyl phosphonate
-
-
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 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
succinyl phosphonate triethyl ester
-
specific inhibitor of cellular KGDHC, 44% inhibition at 0.5 mM
succinyl phosphonate triethyl ester
-
-
succinyl-CoA
-
2-oxoglutarate dehydrogenase complex
succinyl-CoA
Gluconacetobacter xylinus
-
-
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
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
tryptamine-4,5-dione
-
strongly inhibits
Valproic acid
-
-
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
Zn2+
-
may play a role in the inhibition of alpha-KGDH during ischemia or reperfusion, is present in elavated concentrations in such cells
mono-N-chloramine
-
inhibits in a time- and concentration-dependent manner; myeloperoxidase product, inhibition of the alpha-ketoglutarate dehydrogenase multienzyme complex in vitro
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
-
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
-
ethyl 4-[ethoxy(hydroxy)phosphoryl]-4-oxobutanoate and triethyl esters of succinyl phosphonate are ineffective
-
additional information
-
the thyil radical of the complex-bound lipoate inactivates E1o in the presence of 2-oxoglutarate, while thioredoxin prevents E1o inactivation
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
AceF
-
acetyltransferase AceF
-
acetyl-CoA
-
activates, 2-oxoglutarate dehydrogenase complex
ADP
-
stimulates 2-oxoglutarate dehydrogenase complex
ADP
-
stimulates 2-oxoglutarate dehydrogenase complex
ADP
-
stimulates
ADP
-
stimulates
ADP
-
activates the enzyme complex for production of reactive oxygen species in absence of NAD+
AMP
-
stimulates 2-oxoglutarate dehydrogenase complex
AMP
Gluconacetobacter xylinus
-
enhances the rate of succinylation of the enzyme complex
AMP
Gluconacetobacter xylinus
-
stimulates 2-oxoglutarate dehydrogenase complex
AMP
-
stimulates 2-oxoglutarate dehydrogenase complex
AMP
-
stimulates 2-oxoglutarate dehydrogenase complex
carbonyl cyanide p-trifluoromethoxyphenylhydrazone
-
activates the enzyme complex for production of reactive oxygen species in absence of NAD+
Cys
-
activates, 2-oxoglutarate dehydrogenase complex
Cys
-
activates, 2-oxoglutarate dehydrogenase complex
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
GMP
-
activates 2-oxoglutarate dehydrogenase complex
GTP
-
activates 2-oxoglutarate dehydrogenase complex
NAD+
-
stimulates
NADH
-
stimulates H2O2 production reaction of the enzyme
NH4+
-
in synaptic mitochondria thioacetamide-induced encephalopathy produces an 84% increase in Vmax and a 35% decrease of KM for 2-oxoglutarate
rotenone
-
stimulates H2O2 production
spermine
-
enhances activity
thiamine
-
can reverse the loss in KGDHC in Alzheimer's disease patients
thiamine diphosphate
-
exogenous
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
Trolox
-
can dramatically increase KGDHC in cultured cells
UDP
-
activates 2-oxoglutarate dehydrogenase complex
UTP
-
activates 2-oxoglutarate dehydrogenase complex
Inorganic phosphate
-
-
-
additional information
-
potassium stabilizes the binding of thiamine diphosphate to E1o
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.013
-
2-oxoglutarate
-
-
0.07
-
2-oxoglutarate
-
in presence of 0.0045 mM Ca2+
0.076
-
2-oxoglutarate
-
2-oxoglutarate dehydrogenase complex
0.08
-
2-oxoglutarate
-
2-oxoglutarate dehydrogenase complex
0.1
-
2-oxoglutarate
-
-
0.116
-
2-oxoglutarate
-
pH 7.0
0.117
-
2-oxoglutarate
-
-
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
0.15
-
2-oxoglutarate
-
-
0.15
-
2-oxoglutarate
-
-
0.27
-
2-oxoglutarate
-
in presence of 0.2 mM AMP
0.4
-
2-oxoglutarate
-
-
0.43
-
2-oxoglutarate
-
in presence of 0.2 M ADP
0.47
-
2-oxoglutarate
-
in presence of 0.0225 mM Ca2+
0.564
-
2-oxoglutarate
-
pH 7.4
0.58
-
2-oxoglutarate
-
in presence of 0.0023 mM Ca2+
0.75
-
2-oxoglutarate
-
in presence of 0.07 mM Ca2+
0.8
-
2-oxoglutarate
-
without Ca2+
0.84
-
2-oxoglutarate
-
in presence of 0.0012 mM Ca2+
1
-
2-oxoglutarate
-
-
2.5
-
2-oxoglutarate
-
in absence of added nucleotide
4
-
2-oxoglutarate
-
-
additional information
-
additional information
-
-
-
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
-
-
additional information
-
additional information
Gluconacetobacter xylinus
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.2
-
acetaldehyde
-
2-oxoglutarate dehydrogenase complex
0.5
-
Benzene-1,3-dicarboxylate
-
-
1.1
-
Benzene-1,4-dicarboxylate
-
-
1.64
-
glyoxylate
-
-
1.7
-
glyoxylate
-
-
3.3
-
glyoxylate
-
2-oxoglutarate dehydrogenase complex
0.018
-
NADH
-
2-oxoglutarate dehydrogenase complex
0.02
-
NADH
Gluconacetobacter xylinus
-
competitive inhibition with respect to NAD+, 2-oxoglutarate dehydrogenase complex
0.0000024
-
OdhI
-
unphosphorylated state
-
0.4
-
Pyridine-2,4-dicarboxylate
-
-
3
-
Pyridine-2,5-dicarboxylate
-
-
0.003
-
succinyl-CoA
Gluconacetobacter xylinus
-
-
0.004
-
succinyl-CoA
-
2-oxoglutarate dehydrogenase complex
0.00037
-
Zn2+
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
18.2
-
1,2,3,4-tetrahydroisoquinoline
-
IC50: 18.2 mM
18.9
-
1-methyl-4-phenylpyridinium
-
IC50: 18.9 mM
6.5
-
Isoquinoline
-
IC50: 6.5 mM
2
-
N-methyl-1,2,3,4-tetrahydroisoquinoline
-
IC50: 2 mM
3
-
N-n-propylisoquinolinium
-
IC50: 3 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.1
-
-
-
0.2
-
-
-
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
-
Gluconacetobacter xylinus
-
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
-
-
activity under different conditions in synaptosomes
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
2-oxoglutarate dehydrogenase reaction
6.6
7.4
-
-
6.7
-
-
oxidation of 2-oxo-4-hydroxyglutarate or 2-oxoglutarate by the 2-oxoglutarate dehydrogenase complex
7.2
7.4
-
-
7.2
-
-
2-oxoglutarate dehydrogenase complex
7.3
7.6
Gluconacetobacter xylinus
-
2-oxoglutarate dehydrogenase complex
7.3
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.4
-
-
in vivo assay at, N2a cells
7.4
-
-
assay at
7.4
-
-
assay at, synaptosomes
7.4
-
-
assay at
7.5
7.7
-
2-oxoglutarate dehydrogenase complex
7.5
-
-
2-oxoglutarate dehydrogenase complex
7.6
-
-
assay at
8
8.5
-
2-oxoglutarate dehydrogenase complex
8
-
-
2-oxoglutarate dehydrogenase complex
8
-
-
oxidation of 2-oxo-4-hydroxyglutarate or 2-oxoglutarate by the 2-oxoglutarate dehydrogenase complex
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.7
6
-
-
6.5
8
-
pH 6.5: about 40% of maximal activity, pH 8.0: about 50% 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
6.5
8.5
-
pH 6.5: about 60% of maximal activity, pH 8.5: about 30% of maximal activity, 2-oxoglutarate dehydrogenase complex
6.6
8.4
Gluconacetobacter xylinus
-
about 50% of maximal activity at pH 6.6 and at pH 8.4, 2-oxoglutarate dehydrogenase complex
7
8.5
-
pH 7.0: about 70% of maximal activity, pH 8.5: about 70% of maximal activity, 2-oxoglutarate dehydrogenase complex
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
35
-
2-oxoglutarate dehydrogenase activity
30
-
-
assay at
30
-
-
assay at
35
-
-
2-oxoglutarate dehydrogenase complex
37
-
-
in vivo assay at, N2a cells
37
-
-
assay at
37
-
-
assay at, synaptosomes
37
-
-
assay at
37
-
-
assay at, H2O2 production
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
45
-
20°C: about 35% of maximal activity, 45°C: about 20% of maximal activity, 2-oxoglutarate dehydrogenase complex
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
postnatal increase of activity
Manually annotated by BRENDA team
-
endothelial cells have about six times higher activity than do brain microglial cells or neurons
Manually annotated by BRENDA team
-
,neurons that appear slectively vulnerable in human temporal cortex in Alzheimer‘s disease are enriched in the 2-oxoglutarate dehydrogenase complex
Manually annotated by BRENDA team
-
diminished activities in regions with severe pathology, as well as in areas of minimal pathology, activity declines with the severity of disease
Manually annotated by BRENDA team
Q96HY7, Q9ULD0
;
Manually annotated by BRENDA team
-
isozyme 2-oxoglutarate dehydrogenase-like protein
Manually annotated by BRENDA team
-
The HEK-293 subline E2k-67 shows about 30% reduced KGDHC activity; control line E2k-100
Manually annotated by BRENDA team
-
postnatal increase of activity
Manually annotated by BRENDA team
-
dystrophic skeletal muscle
Manually annotated by BRENDA team
Pigeon
-
breast muscle
Manually annotated by BRENDA team
-
highest activity found in rapidly growing mycelium, glucose-NH4+ or glucose-peptone medium
Manually annotated by BRENDA team
-
neuroblastoma cells
Manually annotated by BRENDA team
-
cerebellar granule neurons
Manually annotated by BRENDA team
-
hippocampal neuron
Manually annotated by BRENDA team
-
submedial thalamic nucleus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
-
adrenals
Manually annotated by BRENDA team
additional information
-
N2a cells
Manually annotated by BRENDA team
additional information
-
2-oxoglutarate dehydrogenase-like protein is not detected in heart
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme E2 overexpression or disruption of mitochondrial membrane potential causes enzyme E2 release from mitochondria to cytoplasm where it is degraded
Manually annotated by BRENDA team
-
enzyme E1o contains mitochondrial targeting sequence
Manually annotated by BRENDA team
-
alpha-ketoglutarate dehydrogenase is heterogeneously distributed in mitochondria within individual astrocytes originating either from cerebellum or cerebral cortex
Manually annotated by BRENDA team
additional information
-
enzyme complex is expressed during erythrocytic stage of the parasite
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
-
-
SDS-PAGE
117400
-
-
calculated from amino acid sequence
140000
-
-
OdhA, the E1 subunit of ODH
190000
-
-
2-oxoglutarate dehydrogenase component, equilibrium sedimentation
210000
-
P0AFG3
2 * 105000, SDS-PAGE
360000
-
Gluconacetobacter xylinus
-
active 2-oxoglutarate dehydrogenase component, gel filtration
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
-
Gluconacetobacter xylinus
-
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
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 104805, 2-oxoglutarate dehydrogenase subunit, calculation from nucleotide sequence
?
-
x * 103000, 2-oxoglutarate dehydrogenase subunit, SDS-PAGE; x * 105687, 2-oxoglutarate dehydrogenase subunit, calculation from nucleotide sequence
?
-
x * 110000, SDS-PAGE
?
-
x * 52900, 2-oxoglutarate dehydrogenase subunit E1, SDS-PAGE
?
-
x * 105000, SDS-PAGE
?
-
x * 103000, 2-oxoglutarate dehydrogenase subunit, SDS-PAGE
?
-
x * 52000, E2, SDS-PAGE
?
Q87668
x * 110000, about, E1o component, sequence calculation, x * 30000, recombinant N-terminal catalytic domain, SDS-PAGE
tetramer
Gluconacetobacter xylinus
-
4 * 100000, active 2-oxoglutarate dehydrogenase component, SDS-PAGE
homodimer
P0AFG3
x-ray crystallography
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
Gluconacetobacter xylinus
-
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
-
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
additional information
-
in solution at pH 7.0, the 2-oxoglutarate dehydrogenase component exists as a stable dimer
additional information
-
multienzyme complex structure
additional information
Q87668
the catalytic domain of E1o is located at the N-terminus
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
enzyme contains a mitochondrial targeting sequence which is cleaved off in the mitochondria resulting in the mature enzyme
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
additional information
-
resulting in loss of enzyme complex activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sitting drop vapour diffusion method with 12% (w/v) polyethylene glycol 4000, 50 mM sodium citrate (pH 5.6)
P0AFG3
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
60 min, stable, 2-oxoglutarate dehydrogenase complex
21
-
-
60 min, about 65% loss of activity, 2-oxoglutarate dehydrogenase complex
30
-
-
60min, about 80% loss of activity, 2-oxoglutarate dehydrogenase complex
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-oxoglutarate stabilizes against dilution
-
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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80°C, 2-oxoglutarate dehydrogenase complex, 5-15% loss of activity after several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-oxoglutarate dehydrogenase complex
-
2-oxoglutarate dehydrogenase complex
-
2-oxoglutarate dehydrogenase complex from ox heart, by PEG fractionation, ultracentrifugation, and gel filtration
-
partial, 2-oxoglutarate dehydrogenase complex
-
by affinity chromatography, purification of OdhI-T14A leads to specific copurification of OdhA, the E1 subunit of ODH
-
Ni-NTA column chromatography
-
2-oxoglutarate dehydrogenase complex
-
2-oxoglutarate dehydrogenase complex
-
ammonium sulfate precipitation, HiLoad Q-Sepharose column chromatography, and Superdex S200 gel filtration
P0AFG3
2-oxoglutarate dehydrogenase complex
Gluconacetobacter xylinus
-
2-oxoglutarate dehydrogenase complex
-
by gel filtration
-
partial purification
-
partially, isolation of subsarcolemmal mitochondria from heart
-
poly(ethylene glycol) fractionation and Sephacryl HR300 gel filtration
-
2-oxoglutarate dehydrogenase complex
-
2-oxoglutarate dehydrogenase complex
-
enzyme is further purified from commercial pig heart preparation
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-oxoglutarate dehydrogenase component E1o of the 2-oxoglutarate dehydrogenase complex
-
2-oxoglutarate dehydrogenase component E1o, expression in Escherichia coli
-
expressed in Corynebacterium glutamicum
-
expression in Escherichia coli DH5alpha
-
gene odhL encodes the 2-oxoglutarate dehydrogenase component of the multienenzyme complex, expression in Escherichia coli in kgdA mutant of Pseudomonas putida JS347
-
expressed in Escherichia coli BL21(DE3) cells
P0AFG3
expressed in PC-12 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
-
enzyme E1o is located on chromosome 8
-
KGD1 gene encoding the 2-oxoglutarate dehydrogenase component of the 2-oxoglutarate dehydrogenase complex
-
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
Q87668
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
H352C
-
the activity of the mutant is significantly reduced
Q356D
-
the activity of the mutant is slightly reduced
T294A
-
the mutant shows almost no activity
H352C
-
the activity of the mutant is significantly reduced
-
H352C/Q356D
-
the mutations fully prevent succinyltransferase activity
-
Q356D
-
the activity of the mutant is slightly reduced
-
T294A
-
the mutant shows almost no activity
-
H260A
P0AFG3
mutant has a dramatically reduced catalytic rate
H352C/Q356D
-
the mutations fully prevent succinyltransferase activity
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
H298A
P0AFG3
mutant has a dramatically reduced catalytic rate
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
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
-
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
medicine
-
hypochlorous acid and chloramines have the potential to inactivate KGDHC, a major target in neurodegeneration, without significant loss of cellular viability
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
-
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
-
plays a role in neurodegenerative diseases
medicine
-
hypochlorous acid and chloramines have the potential to inactivate KGDHC, a major target in neurodegeneration
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
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
additional information
-
alpha-ketoglutarate-involving reactions belong to the backbone of high-flux reactions, which is rather conserved in evolution
medicine
-
potential of succinyl phosphonate esters for modeling the biochemical and pathophysiological consequences of reduced KGDHC activity in brain diseases
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