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2-ketoglutarate dehydrogenase
2-oxoglutarate decarboxylase
2-oxoglutarate dehydrogenase
2-oxoglutarate dehydrogenase complex
2-oxoglutarate dehydrogenase complex E1 component
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2-oxoglutarate dehydrogenase-like protein
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brain-specific isozyme
2-oxoglutarate:lipoate oxidoreductase
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alpha-ketoglutarate dehydrogenase
alpha-ketoglutarate dehydrogenase complex
alpha-ketoglutarate dehydrogenase multienzyme complex
alpha-ketoglutaric acid dehydrogenase
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alpha-ketoglutaric dehydrogenase
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alpha-oxoglutarate dehydrogenase
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dehydrogenase, oxoglutarate
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DHTKD1
2-oxoglutarate dehydrogenase-like hypothetical protein
dihydrolipoyl succinyltransferase E2
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part of the multisubunit alpha-ketoglutarate dehydrogenase complex
E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex
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E1 subunit of the alpha-ketoglutarate dehydrogenase complex
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E1o component 2-oxoglutarate dehydrogenase complex
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ketoglutaric dehydrogenase
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OGHDC-E2
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component of the 2-oxoglutarate dehydrogenase multienzyme complex
oxoglutarate decarboxylase
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oxoglutarate dehydrogenase
PDHC
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enzyme in complex with alpha-ketoglutarate dehydrogenase
additional information
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enzyme is part of the alpha-ketoglutarate dehydrogenase complex KGDHC
2-ketoglutarate dehydrogenase
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2-ketoglutarate dehydrogenase
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2-oxoglutarate decarboxylase
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2-oxoglutarate decarboxylase
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part of the 2-oxoglutarate dehydrogenase complex
2-oxoglutarate dehydrogenase
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2-oxoglutarate dehydrogenase
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2-oxoglutarate dehydrogenase
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2-oxoglutarate dehydrogenase
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2-oxoglutarate dehydrogenase
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2-oxoglutarate dehydrogenase
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2-oxoglutarate dehydrogenase
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2-oxoglutarate dehydrogenase
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2-oxoglutarate dehydrogenase
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2-oxoglutarate dehydrogenase
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first and rate-limiting component of the multienzyme 2-oxoglutarate dehydrogenase complex
2-oxoglutarate dehydrogenase
O87668
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2-oxoglutarate dehydrogenase
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2-oxoglutarate dehydrogenase complex
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2-oxoglutarate dehydrogenase complex
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2-oxoglutarate dehydrogenase complex
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2-oxoglutarate dehydrogenase complex
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2-oxoglutarate dehydrogenase complex
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tricarboxylic acid cycle multienzyme
alpha-ketoglutarate dehydrogenase
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alpha-ketoglutarate dehydrogenase
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alpha-ketoglutarate dehydrogenase
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alpha-ketoglutarate dehydrogenase
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alpha-ketoglutarate dehydrogenase
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alpha-ketoglutarate dehydrogenase
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alpha-ketoglutarate dehydrogenase
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alpha-ketoglutarate dehydrogenase
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alpha-ketoglutarate dehydrogenase
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alpha-ketoglutarate dehydrogenase
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alpha-ketoglutarate dehydrogenase complex
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alpha-ketoglutarate dehydrogenase complex
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alpha-ketoglutarate dehydrogenase complex
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alpha-ketoglutarate dehydrogenase complex
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alpha-ketoglutarate dehydrogenase complex
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alpha-ketoglutarate dehydrogenase complex
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alpha-ketoglutarate dehydrogenase complex
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alpha-ketoglutarate dehydrogenase complex
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alpha-ketoglutarate dehydrogenase complex
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enzyme in complex with pyruvate dehydrogenase
alpha-ketoglutarate dehydrogenase complex
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alpha-ketoglutarate dehydrogenase complex
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alpha-ketoglutarate dehydrogenase complex
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alpha-ketoglutarate dehydrogenase multienzyme complex
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alpha-ketoglutarate dehydrogenase multienzyme complex
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alpha-KGDH
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E1k
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E1k
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part of the alpha-ketoglutarate dehydrogenase complex
E1o
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E1o
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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
O87668
component of the 2-oxoglutarate dehydrogenase multienzyme complex
E2
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component of the 2-oxo acid dehydrogenase multienzyme complex
E2
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component of the 2-oxo acid dehydrogenase multienzyme complex
E2
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component of the 2-oxo acid dehydrogenase multienzyme complex
E2
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component of the 2-oxo acid dehydrogenase multienzyme complex
KGDH
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KGDH
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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
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ODH
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OdhA
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OGDC
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OGDH
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OGDH
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part of the 2-oxoglutarate dehydrogenase complex multienzyme system
OGDHL
2-oxoglutarate dehydrogenase-like hypothetical protein
OGDHL
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brain-specific isozyme
oxoglutarate dehydrogenase
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oxoglutarate dehydrogenase
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oxoglutarate dehydrogenase
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oxoglutarate dehydrogenase
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); mechanism of the enzyme complex is bi bi uni uni ping pong; the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
kinetics of succinylation and desuccinylation; the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
mechanism of the reaction catalyzed by the 2-oxoglutarate dehydrogenase complex; the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxoglutarate dehydrogenase complex consists of 3 enzymes: E1 (alpha-ketoglutarate dehydrogenase, EC 1.2.4.2), E2 (dihydrolipoyl transsuccinylase, EC 2.3.1.61), E3 (dihydrolipoyl dehydrogenase, EC 1.8.1.4); the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
Pigeon
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
substrate channeling and catalytic mechanism, active site coupling
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
substrate channeling and catalytic mechanism, active site coupling
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
substrate channeling and catalytic mechanism, active site coupling
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
substrate channeling and catalytic mechanism, active site coupling
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
the enzyme complex catalyzes the reaction : 2-oxoglutarate + CoA + NAD+--> succinyl-CoA + CO2 + NADH, the following partial reactions are catalyzed: 1. HOOC(CH2)2COCOOH + (thiamine diphosphate)-E1--> (HOOC(CH2)2 CHOH-thiamine-diphosphate)-E1 + CO2, 2. (HOOC(CH2)2CH OH-thiamine-diphosphate)-E1 + (LipS2)-E2--> (HOOC(CH)2 CO-(SLipSH))-E2 + (thiamine-diphosphate)-E1, 3. (HOOC(CH2)2CO-(SLipSH))-E2 + HSCoA--> (Lip(SH)2)-E2 + HOOC(CH2)2CO-SCoA, 4. (Lip(SH)2)-E2 + E3-FAD--> (LipS2)-E2 + reduced E3-FAD, 5. reduced E3-FAD + NAD+--> E3-FAD + NADH
-
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
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2-oxoglutarate + CoA
? + H2O2
2-oxoglutarate + CoA + 3-acetylpyridine adenine dinucleotide
succinyl-CoA + CO2 + reduced 3-acetylpyridine adenine dinucleotide
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
additional information
?
-
2-oxoglutarate + CoA
? + H2O2
-
-
-
-
?
2-oxoglutarate + CoA
? + H2O2
-
-
-
-
?
2-oxoglutarate + CoA + 3-acetylpyridine adenine dinucleotide
succinyl-CoA + CO2 + reduced 3-acetylpyridine adenine dinucleotide
-
3-acetylpyridine adenine dinucleotide is used instead of NAD+ to avoid concomitant oxidase activity that would degrade NADH produced by the ODH reaction
-
-
?
2-oxoglutarate + CoA + 3-acetylpyridine adenine dinucleotide
succinyl-CoA + CO2 + reduced 3-acetylpyridine adenine dinucleotide
-
3-acetylpyridine adenine dinucleotide is used instead of NAD+ to avoid concomitant oxidase activity that would degrade NADH produced by the ODH reaction
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
addition of glutamate stimulates the synthesis of the 2-oxoglutarate dehydrogenase complex
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
reaction is physiologically irreversible, due to the volatility of CO2
-
-
ir
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
the 2-oxoglutarate dehydrogenase complex catalyzes a critical step in the Krebs tricarboxylic acid cycle, which is also a step in the metabolism of the potentially excitotoxic neurotransmitter glutamate. Deficiencies of the 2-oxoglutarate dehydrogenase complex are likely to impair energy metabolism and therfore brain function, and lead to manifestations of brain disease. Neurons that are enriched in the 2-oxoglutarate dehydrogenase complex may be selectively vulnerable in Alzheimer‘s disease. Variations in 2-oxoglutarate dehydrogenase complex that are not deleterious during reproductive life become deleterious with aging, perhaps by predisposing this mitochondrial metabolon to oxidative damage
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
reductions in enzyme activity occurs in a number of neurodegenerative disorders including Alzheimer‘s disease. The reduction in 2-oxoglutarate dehydrogenase complex activity can be linked to several aspects of brain dysfunction and neuropathology in a number of neurodegenerative diseases
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
Pigeon
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
catalyzes a rate limiting step of the TCA cycle
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
transcription of the 2-oxoglutarate dehydrogenase component of the 2-oxoglutarate dehydrogenase complex is regulated by glucose and activated by the products of HAP2 and HAP3
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
348910, 348914, 349001, 349005, 349014, 349020, 349021, 349023, 349026, 349027, 349028, 349033 -
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
enzyme of the TCA cycle
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
the enzyme contains a covalently attached lipoyl group, which is reductively acylated by enzyme complex component E1, EC 1.2.4.1, the enzyme component E2 catalyzes the subsequent acyl transfer to CoA
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
the enzyme contains a covalently attached lipoyl group, which is reductively acylated by enzyme component E1, the enzyme component E2 catalyzes the subsequent acyl transfer to CoA
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
reaction significant for energy production, neurotransmitter metabolism, and metabolic interaction between mitochondria and cytoplasm
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
the enzyme contains a covalently attached lipoyl group, which is reductively acylated by enzyme complex component E1, EC 1.2.4.1, the enzyme component E2 catalyzes the subsequent acyl transfer to CoA
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
enzyme E2 is a component of the 2-oxoglutarate dehydrogenase multienzyme complex, rate-limiting enzyme in mitochondrial Krebs cycle
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
key step, probably rate-limiting, in the tricarboxylic acid cycle, physiologic function and regulation
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
the enzyme contains a covalently attached lipoyl group, which is reductively acylated by enzyme complex component E1, EC 1.2.4.1, the enzyme component E2 catalyzes the subsequent acyl transfer to CoA
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
O87668
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
additional information
?
-
-
enzyme complex is also active with 2-oxoadipate
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
enzyme also catalyzes the production of H2O2 in vivo, in vitro, and in situ from 2-oxoglutarate with CoA in absence of NAD+, which inhibits this reaction, enzyme is a atrget for reactive oxygen species and also contributes to generation of oxidative stress in mitochondria when NADH oxidation is impaired, overview
-
-
-
additional information
?
-
-
OdhA can utilize free dihydrodilipoamide to perform the E2 reaction specifically with succinyl-CoA. OdhA specifically catalyzes the E1 and E2 reaction to convert 2-oxoglutarate to succinyl-CoA but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA
-
-
-
additional information
?
-
-
OdhA can utilize free dihydrodilipoamide to perform the E2 reaction specifically with succinyl-CoA. OdhA specifically catalyzes the E1 and E2 reaction to convert 2-oxoglutarate to succinyl-CoA but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
the enzyme complex also catalyzes CoASH-dependent oxidation of 2-oxo-4-hydroxyglutarate to malate
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
enzyme activity is reduced in patients with Parkinson's disease due to elevated levels of monoamine oxidase B, physiological effects and regulation, overview
-
-
-
additional information
?
-
-
loss of enzyme activity contributes to the major loss of cerebral energy metabolism leading to a number of neurodegenerative disorders and Alzheimer's disease, myeloperoxidase activity is involved
-
-
-
additional information
?
-
-
reduced enzyme activity in vivo does not lead to the Ca2+ abnormalities observed in patients suffering brain disorders and abnormal mitochondrial function, or Alzheimer's disease, but the release of cytochrome c together with reduced enzyme activity activates other pathways including cell death cascades, enzyme inhibition alters Ca2+ homeostasis and increases cytosolic accumulation of cytochrome c
-
-
-
additional information
?
-
-
the enzyme is targeted for ubiquitination-dependent degradation in mitochondria by binding of Siah2, the RING finger ubiquitin-protein isopeptide ligase 2, encoded by gene siah2
-
-
-
additional information
?
-
-
enzyme complex produces H2O2 in vivo, which is inhibited by NAD+ with the isolated enzyme complex and in mitochondria, physiological effects and regulation, overview
-
-
-
additional information
?
-
-
KGDHC is an important component of the tricarboxylic acid cycle
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
2-oxoglutarate-supported mitochondrial respiration state 3
-
-
-
additional information
?
-
-
enzyme complex produces H2O2 in vivo, which is inhibited by NAD+ with the isolated enzyme complex and in mitochondria, physiological effects and regulation, overview
-
-
-
additional information
?
-
-
KGDHC contributes to neuronal reactive oxygen species increase in situ
-
-
-
additional information
?
-
-
the E1o component of the2-oxoglutarate dehydrogenase complex catalyses the initial, substrate-specific and irreversible stage of the overall reaction, and has the lowest catalytic activity (turnover number) among the components and as such limits the rate of the overall process
-
-
-
additional information
?
-
-
the KGDH enzyme has also a function as a poly(ADP-ribose) polymerase-like enzyme, which may play a role in regulating intramitochondrial NAD+ and poly(ADP-ribose) homeostasis
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
enzyme complex is also active with 2-oxoadipate
-
-
-
additional information
?
-
-
enzyme complex is also active with 2-oxoadipate
-
-
-
additional information
?
-
-
the enzyme complex also catalyzes CoASH-dependent oxidation of 2-oxo-4-hydroxyglutarate to malate
-
-
-
additional information
?
-
-
enzyme also catalyzes the production of H2O2 from 2-oxoglutarate with CoA in absence of NAD+, which inhibits this reaction, enzyme is a atrget for reactive oxygen species and also contributes to generation of oxidative stress in mitochondria when NADH oxidation is impaired, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
additional information
?
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
addition of glutamate stimulates the synthesis of the 2-oxoglutarate dehydrogenase complex
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
the 2-oxoglutarate dehydrogenase complex catalyzes a critical step in the Krebs tricarboxylic acid cycle, which is also a step in the metabolism of the potentially excitotoxic neurotransmitter glutamate. Deficiencies of the 2-oxoglutarate dehydrogenase complex are likely to impair energy metabolism and therfore brain function, and lead to manifestations of brain disease. Neurons that are enriched in the 2-oxoglutarate dehydrogenase complex may be selectively vulnerable in Alzheimer‘s disease. Variations in 2-oxoglutarate dehydrogenase complex that are not deleterious during reproductive life become deleterious with aging, perhaps by predisposing this mitochondrial metabolon to oxidative damage
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
reductions in enzyme activity occurs in a number of neurodegenerative disorders including Alzheimer‘s disease. The reduction in 2-oxoglutarate dehydrogenase complex activity can be linked to several aspects of brain dysfunction and neuropathology in a number of neurodegenerative diseases
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
catalyzes a rate limiting step of the TCA cycle
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
transcription of the 2-oxoglutarate dehydrogenase component of the 2-oxoglutarate dehydrogenase complex is regulated by glucose and activated by the products of HAP2 and HAP3
-
-
-
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
enzyme of the TCA cycle
-
-
-
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
enzyme E2 is a component of the 2-oxoglutarate dehydrogenase multienzyme complex, rate-limiting enzyme in mitochondrial Krebs cycle
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
key step, probably rate-limiting, in the tricarboxylic acid cycle, physiologic function and regulation
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
O87668
-
-
-
ir
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
-
-
-
ir
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
enzyme also catalyzes the production of H2O2 in vivo, in vitro, and in situ from 2-oxoglutarate with CoA in absence of NAD+, which inhibits this reaction, enzyme is a atrget for reactive oxygen species and also contributes to generation of oxidative stress in mitochondria when NADH oxidation is impaired, overview
-
-
-
additional information
?
-
-
OdhA can utilize free dihydrodilipoamide to perform the E2 reaction specifically with succinyl-CoA. OdhA specifically catalyzes the E1 and E2 reaction to convert 2-oxoglutarate to succinyl-CoA but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA
-
-
-
additional information
?
-
-
OdhA can utilize free dihydrodilipoamide to perform the E2 reaction specifically with succinyl-CoA. OdhA specifically catalyzes the E1 and E2 reaction to convert 2-oxoglutarate to succinyl-CoA but fully relies on the lipoyl residues provided by AceF involved in the reactions to convert pyruvate to acetyl-CoA
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
enzyme activity is reduced in patients with Parkinson's disease due to elevated levels of monoamine oxidase B, physiological effects and regulation, overview
-
-
-
additional information
?
-
-
loss of enzyme activity contributes to the major loss of cerebral energy metabolism leading to a number of neurodegenerative disorders and Alzheimer's disease, myeloperoxidase activity is involved
-
-
-
additional information
?
-
-
reduced enzyme activity in vivo does not lead to the Ca2+ abnormalities observed in patients suffering brain disorders and abnormal mitochondrial function, or Alzheimer's disease, but the release of cytochrome c together with reduced enzyme activity activates other pathways including cell death cascades, enzyme inhibition alters Ca2+ homeostasis and increases cytosolic accumulation of cytochrome c
-
-
-
additional information
?
-
-
the enzyme is targeted for ubiquitination-dependent degradation in mitochondria by binding of Siah2, the RING finger ubiquitin-protein isopeptide ligase 2, encoded by gene siah2
-
-
-
additional information
?
-
-
enzyme complex produces H2O2 in vivo, which is inhibited by NAD+ with the isolated enzyme complex and in mitochondria, physiological effects and regulation, overview
-
-
-
additional information
?
-
-
substrate channeling in the 2-oxo acid dehydrogenase multienzyme complex, mechanism, overview
-
-
-
additional information
?
-
-
2-oxoglutarate-supported mitochondrial respiration state 3
-
-
-
additional information
?
-
-
enzyme complex produces H2O2 in vivo, which is inhibited by NAD+ with the isolated enzyme complex and in mitochondria, physiological effects and regulation, overview
-
-
-
additional information
?
-
-
KGDHC contributes to neuronal reactive oxygen species increase in situ
-
-
-
additional information
?
-
-
the E1o component of the2-oxoglutarate dehydrogenase complex catalyses the initial, substrate-specific and irreversible stage of the overall reaction, and has the lowest catalytic activity (turnover number) among the components and as such limits the rate of the overall process
-
-
-
additional information
?
-
-
the KGDH enzyme has also a function as a poly(ADP-ribose) polymerase-like enzyme, which may play a role in regulating intramitochondrial NAD+ and poly(ADP-ribose) homeostasis
-
-
-
additional information
?
-
-
enzyme also catalyzes the production of H2O2 from 2-oxoglutarate with CoA in absence of NAD+, which inhibits this reaction, enzyme is a atrget for reactive oxygen species and also contributes to generation of oxidative stress in mitochondria when NADH oxidation is impaired, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
((+/-)-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
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-Oxoisohexanoate
-
2-oxoglutarate dehydrogenase complex
2-oxoisopentanoate
-
2-oxoglutarate dehydrogenase complex
3-nitropropionic acid
-
-
4-oxo-4-phosphonobutanoic acid
4-[(2-carboxyethoxy)(hydroxy)phosphoryl]-4-oxobutanoic acid
4-[ethoxy(hydroxy)phosphoryl]-4-oxobutanoic acid
7-(1-hydroxy-2-aminoethyl)-3,4-dihydro-5-hydroxy-2H-1,4-benzothiazine-3-carboxylic acid
-
time-dependent inhibition of the 2-oxoglutarate dehydrogenase complex appears to be related to the oxidation of 7-(1-hydroxy-2-aminoethyl)-3,4-dihydro-5-hydroxy-2H-1,4-benzothiazine-3-carboxylic acid, catalyzed by an unknown component of the inner mitochondrial membrane, to electrophilic intermediates which bind covalently to active site cysteinyl residues of the enzyme complex
7-(2-aminoethyl)-3,4-dihydro-5-hydroxy-2H-1,4-benzothiazine-3-carboxylic acid
-
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
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
cisplatin
-
treatment with 0.05 or 0.1 mM for 3 h, followed by removal of cisplatin from the medium for 24 h, results in a pronounced loss of activity, both in mitochondrial aspartate aminotransferase-transfected cells and control cells, exposure to 0.1 mM results in a significantly greater loss of activity in mitochondrial aspartate aminotransferase-transfected cells than in control cells
ethyl 4-[ethoxy(hydroxy)phosphoryl]-4-oxobutanoate
-
only inhibitory after preincubation, release of charged groups by cellular esterases and activation in intact cells
glutathione
-
regulation of enzyme activity by reversible glutathionylation, inactivation with diamide
hydrogen peroxide
-
the E2 subunit of alpha-ketoglutarate dehydrogenase is reversibly glutathionylated and inhibited by 0.025 mM hydrogen peroxide, the enzyme is maximally inhibited (about 45%) 5.0 min after the addition of H2O2
Isoquinoline
-
IC50: 6.5 mM
isoquinoline derivative
-
-
-
N-methyl-1,2,3,4-tetrahydroisoquinoline
-
IC50: 2 mM
N-methylisoquinolinium
-
-
N-n-propylisoquinolinium
-
IC50: 3 mM
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
NADPH
-
2-oxoglutarate dehydrogenase complex
NEM
-
prevents desuccinylation of the 2-oxoglutarate dehydrogenase complex
OdhI
-
unphosphorylated OdhI strongly inhibits ODH activity
-
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
-
ruthenium red
-
abolishes the Ca-stimulation of OGDH
succinate
-
2-oxoglutarate dehydrogenase complex
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
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
1-methyl-4-phenylpyridinium
-
-
1-methyl-4-phenylpyridinium
-
IC50: 18.9 mM
1-oxo-3-carboxypropylphosphonic acid methyl ester
-
-
1-oxo-3-carboxypropylphosphonic acid methyl ester
Pigeon
-
-
2-oxoglutarate
-
substrate inhibition above 4 mM
2-oxoglutarate
-
2-oxoglutarate dehydrogenase complex
4-oxo-4-phosphonobutanoic acid
-
0.01 mM completely inhibits even in the presence of a 200fold higher concentration of its substrate 2-oxoglutarate
4-oxo-4-phosphonobutanoic acid
-
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
ATP
-
inhibits KGDHC in the kidney, in adrenals the effect is rather weak
ATP
-
weakly inhibits in breast muscles
ATP
-
2-oxoglutarate dehydrogenase complex
ATP
-
inhibits KGDHC in the heart
cis-aconitate
-
2-oxoglutarate dehydrogenase complex
cis-aconitate
-
2-oxoglutarate dehydrogenase complex
glyoxylate
-
2-oxoglutarate dehydrogenase complex
glyoxylate
-
2-oxoglutarate dehydrogenase complex
glyoxylate
-
2-oxoglutarate dehydrogenase complex
H2O2
-
-
H2O2
-
addition outside of cells reduces KGDHC activity in proportion to the increase in reactive oxygen species
H2O2
-
1 h treatment with H2O2 decreases KGDHC activity
H2O2
-
inhibits lysate KGDHC in a concentration- and time-dependent manner, inhibitory effect reversed by addition of dithiothreitol
H2O2
-
oxidative damage to KGDHC
H2O2
-
ca. 300 times less effective than mono-N-chloramine
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
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
mono-N-chloramine
-
inhibits in a time- and concentration-dependent manner; myeloperoxidase product, inhibition of the alpha-ketoglutarate dehydrogenase multienzyme complex in vitro
Na+
-
50 mM, 48% inhibition, 2-oxoglutarate dehydrogenase complex
Na+
-
50 mM NaCl, 34% inhibition of the 2-oxoglutarate dehydrogenase complex
NAD+
-
inhibits H2O2 production reaction of the enzyme
NAD+
-
inhibits H2O2 production reaction of the enzyme
NADH
-
2-oxoglutarate dehydrogenase complex
NADH
-
0.1 mM, 50% inhibition. 0.2 mM AMP completely overcomes the inhibition
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
-
allosteric inhibition
NADH
-
allosteric inhibitor, inhibition relieved by micromolar Ca2+ and ADP
NADH
-
2-oxoglutarate dehydrogenase complex
NADH
-
allosteric inhibition
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
oxalacetate
-
2-oxoglutarate dehydrogenase complex
oxalacetate
-
2-oxoglutarate dehydrogenase complex
reactive oxygen species
-
-
-
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
-
succinyl phosphonate
-
-
succinyl phosphonate
Pigeon
-
-
succinyl phosphonate
-
OGDHC inhibitor competitive to 2-oxoglutarate, 0.005 mM succinyl phosphonate protects OGDHC from catalysis-induced inactivation
succinyl phosphonate
-
specific inhibitor of cellular KGDHC, 20% inhibition at 0.2 mM
succinyl phosphonate
-
potent, slow-binding inhibitor of the 2-oxoglutarate dehydrogenase complex, complete inhibition at 0.1 mM
succinyl phosphonate triethyl ester
-
specific inhibitor of cellular KGDHC, 44% inhibition at 0.5 mM
succinyl phosphonate triethyl ester
-
-
succinyl-CoA
-
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
Zn2+
-
may play a role in the inhibition of alpha-KGDH during ischemia or reperfusion, is present in elavated concentrations in such cells
Zn2+
-
inhibition of the 2-oxoglutarate dehydrogenase complex requires enzyme cycling and is reversed by EDTA. Reversibility is inversely related to the duration of exposure and the concentration of Zn2+. Physiological free Zn2+ may modulate hepatic mitochondrial respiration by reversible inhibition of the 2-oxoglutarate dehydrogenase complex
additional information
-
ethyl 4-[ethoxy(hydroxy)phosphoryl]-4-oxobutanoate and triethyl esters of succinyl phosphonate are ineffective
-
additional information
-
inhibition of the alpha-ketoglutarate dehydrogenase complex alters mitochondrial function and cellular calcium regulation
-
additional information
-
enzyme activity is reduced by 40% in PC12 cells treated with doxycyclin, which is reversible by deprenyl, monoamine oxidase-B-mediated enzyme inhibition, Ca2+ levels influence the NADH/NAD+ pool, which influences the enzyme
-
additional information
-
the enzyme is targeted for ubiquitination-dependent degradation in mitochondria by binding of Siah2, the RING finger ubiquitin-protein isopeptide ligase 2, encoded by gene siah2
-
additional information
-
KGDH is sharply decreased in cells challenged with menadione, treatment of cellular extracts from the menadione-exposed cells with 5 mM dithiothreitol partially restores the activity of KGDH, KGDH levels are diminished when ammonium is utilized as the nitrogen source
-
additional information
-
treatment of mitochondria with H2O2 or tert-butylhydroperoxide leads to decreased enzyme activity due to alterations in the glutathione status, reversible inhibition in case of H2O2, irrevrsible in case of tert-butylhydroperoxide, no direct interaction and no inhibition of isolated enzyme, inhibitory mechanism, enzyme reactivation by DTT, glutathione, and the glutaredoxin system, but not by thioredoxin system
-
additional information
-
the thyil radical of the complex-bound lipoate inactivates E1o in the presence of 2-oxoglutarate, while thioredoxin prevents E1o inactivation
-
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Yeaman, S.J.
The mammalian 2-oxoacid dehydrogenases: a complex family
Trends Biochem. Sci.
11
293-296
1986
Sus scrofa
-
brenda
Reed, L.J.; Cox, D.J.
Multienzyme complexes
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
1
213-240
1970
Bos taurus, Escherichia coli, Sus scrofa
-
brenda
Guest, J.R.; Darlison, M.G.; Spencer, M.E.; Stephens, P.E.
Cloning and sequence analysis of the pyruvate and 2-oxoglutarate dehydrogenase complex genes of Escherichia coli
Biochem. Soc. Trans.
12
220-223
1984
Escherichia coli
brenda
Schulze, E.; Westphal, A.H.; Hanemaaijer, R.; de Kok A.
The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component
Eur. J. Biochem.
187
229-234
1990
Azotobacter vinelandii
brenda
Carlsson, P.; Hederstedt, L.
Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively
J. Bacteriol.
171
3667-3672
1989
Bacillus subtilis
brenda
Repetto, B.; Tzagoloff, A.
Structure and regulation of KGD1, the structural gene for yeast alpha-ketoglutarate dehydrogenase
Mol. Cell. Biol.
9
2695-2705
1989
Saccharomyces cerevisiae
brenda
Karam, G.A.; Bishop, S.H.
alpha-Ketoglutarate dehydrogenase from cauliflower mitochondria: preparation and reactivity with substrates
Phytochemistry
28
3291-3293
1989
Brassica oleracea
-
brenda
Rutter, G.A.; Denton, R.M.
The binding of Ca2+ ions to pig heart NAD+-isocitrate dehydrogenase and the 2-oxoglutarate dehydrogenase complex
Biochem. J.
263
453-462
1989
Sus scrofa
brenda
Heckert, L.L.; Butler, M.H.; Reimers, J.M.; Albe, K.R.; Wright, B.E.
Purification and characterization of the 2-oxoglutarate dehydrogenase complex from Dictyostelium discoideum
J. Gen. Microbiol.
135
155-161
1989
Dictyostelium discoideum
brenda
Bessam, H.; Mareck, A.M.; Foucher, B.
Neurospora crassa alpha-ketoglutarate dehydrogenase complex: description, resolution of components and catalytic properties
Biochim. Biophys. Acta
990
66-72
1989
Neurospora crassa
brenda
Reed, L.J.; Mukherjee, B.B.
alpha-Ketoglutarate dehydrogenase complex from Escherichia coli
Methods Enzymol.
13
55-61
1969
Escherichia coli
-
brenda
Sanadi, D.R.
alpha-Ketoglutarate dehydrogenase from pig heart
Methods Enzymol.
13
52-55
1969
Sus scrofa
-
brenda
Murphy, A.N.; Kelleher, J.K.; Fiskum, G.
Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma mitochondria
Biochem. Biophys. Res. Commun.
157
1218-1255
1988
Rattus norvegicus
brenda
Iwata, H.; Tonomura, H.; Matsuda, T.
Transketolase and 2-oxoglutarate dehydrogenase activities in the brain and liver of the developing rat
Experientia
44
780-781
1988
Rattus norvegicus
brenda
Cho, H.Y.; Widholm, J.M.; Slife, F.W.
Haloxyfop inhibition of the pyruvate and the alpha-ketoglutarate dehydrogenase complexes of corn (Zea mays L.) and soybean (Glycine max [L.] Merr.)
Plant Physiol.
87
334-340
1988
Glycine max, Zea mays
brenda
Dry, I.B.; Wiskich, J.T.
2-Oxoglutarate dehydrogenase and pyruvate dehydrogenase activities in plant mitochondria: interaction via a common coenzyme a pool
Arch. Biochem. Biophys.
257
92-99
1987
Brassica rapa, Pisum sativum
brenda
Burke, L.A.; Heffron, J.J.A.
Isocitrate and oxoglutarate dehydrogenase activities of murine dystrophic skeletal muscle
Biochem. Soc. Trans.
15
233-234
1987
Mus musculus
-
brenda
De Marcucci, O.G.L.; Hunter, A.; Lindsay, J.G.
Precursor forms of the constituent polypeptides of pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes from ox heart
Biochem. Soc. Trans.
14
870
1986
Bos taurus
-
brenda
Hunter, A.; Lindsay, J.G.
Immunological and biosynthetic studies on the mammalian 2-oxoglutarate dehydrogenase multienzyme complex
Eur. J. Biochem.
155
103-109
1986
Bos taurus
brenda
Majamaa, K.; Turpeenniemi-Hujanen, T.M.; Latipää, P.; Gunzler, V.; Hanauske-Abel, H.M.; Hassinen, I.E.; Kivirikko, K.I.
Differences between collagen hydroxylases and 2-oxoglutarate dehydrogenase in their inhibition by structural analogues of 2-oxoglutarate
Biochem. J.
229
127-133
1985
Sus scrofa
brenda
Meixner-Monori, B.; Kubicek, C.P.; Habison, A.; Kubicek-Pranz, E.M.; Roehr, M.
Presence and regulation of the alpha-ketoglutarate dehydrogenase multienzyme complex
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