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2-oxoglutarate + CoA + NAD+ = succinyl-CoA + CO2 + NADH
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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)
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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)
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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)
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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)
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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)
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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)
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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)
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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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348910, 348914, 349001, 349005, 349014, 349020, 349021, 349023, 349026, 349027, 349028, 349033
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
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
Pigeon
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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
kinetics of succinylation and desuccinylation
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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
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
mechanism of the enzyme complex is bi bi uni uni ping pong
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
substrate channeling and catalytic mechanism, active site coupling
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
substrate channeling and catalytic mechanism, active site coupling
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
substrate channeling and catalytic mechanism, active site coupling
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2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
substrate channeling and catalytic mechanism, active site coupling
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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
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2-oxoadipate + CoA + NAD+
glutaryl-CoA + CO2 + NADH
2-oxoadipate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine + CO2
2-oxoglutarate + CoA + 3-acetylpyridine adenine dinucleotide
succinyl-CoA + CO2 + reduced 3-acetylpyridine adenine dinucleotide
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH + H+
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?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
2-oxovalerate + CoA + NAD+
? + CO2 + NADH
unnatural substrate, very poor substrate of wild-type
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-
?
additional information
?
-
2-oxoadipate + CoA + NAD+
glutaryl-CoA + CO2 + NADH
-
-
-
?
2-oxoadipate + CoA + NAD+
glutaryl-CoA + CO2 + NADH
-
-
-
?
2-oxoadipate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine + CO2
-
-
-
?
2-oxoadipate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
[dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine + CO2
-
-
-
?
2-oxoglutarate + CoA + 3-acetylpyridine adenine dinucleotide
succinyl-CoA + CO2 + reduced 3-acetylpyridine adenine dinucleotide
-
3-acetylpyridine adenine dinucleotide is used instead of NAD+ to avoid concomitant oxidase activity that would degrade NADH produced by the ODH reaction
-
-
?
2-oxoglutarate + CoA + 3-acetylpyridine adenine dinucleotide
succinyl-CoA + CO2 + reduced 3-acetylpyridine adenine dinucleotide
-
3-acetylpyridine adenine dinucleotide is used instead of NAD+ to avoid concomitant oxidase activity that would degrade NADH produced by the ODH reaction
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
-
-
-
-
?
2-oxoglutarate + CoA + NAD+
succinyl-CoA + CO2 + NADH
-
-
-
-
?
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
-
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 Alzheimers 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 Alzheimers 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
Pigeon
-
-
-
-
?
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
-
-
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 + lipoamide
S-succinyldihydrolipoamide + CO2
-
-
-
-
?
2-oxoglutarate + lipoamide
S-succinyldihydrolipoamide + CO2
-
addition of glutamate stimulates the synthesis of the 2-oxoglutarate dehydrogenase complex
-
-
?
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
-
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
-
-
-
?
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
-
-
-
-
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
-
-
-
-
?
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
?
-
-
-
-
-
?
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
?
-
-
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
?
-
-
KGDHC contributes to neuronal reactive oxygen species increase in situ
-
-
?
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
-
-
?
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((+/-)-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 Parkinsons 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
ADP
-
the Sa0.5 for ADP in the absence of Ca2+ decreases as ionic strength increases. In the presence of calcium and 0.2 M ionic strength, ADP has no effect on 2-oxoglutarate dehydrogenase complex activity
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
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
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
-
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
ATP
-
the magnitude of inhibition by ATP is not influenced by changes in ionic strength in the absence of calcium. In the presence of Ca2+, increases in ionic strength lower the inhibitory effects of ATP. The S0.5 for ATP in both presence and absence of Ca2+ is not affected by changes in ionic strength in the range of 0.1-0.2 M
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
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
-
allosteric inhibition
NADH
-
2-oxoglutarate dehydrogenase complex
NH4+
-
50 mM, 70% inhibition, 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
NH4+
-
50 mM NH4Cl, 21% inhibition of the 2-oxoglutarate dehydrogenase complex
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
-
synthetic analog of 2-oxoglutarate
succinyl phosphonate
Pigeon
-
-
succinyl phosphonate
-
specific inhibitor of cellular KGDHC, 20% inhibition at 0.2 mM
succinyl phosphonate
-
synthetic analog of 2-oxoglutarate
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
-
-
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
-
desuccinylation of the enzyme by SIRT5 inhibits the activity of the enzyme complex
-
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0.107 - 0.52
2-oxoadipate
0.0025 - 10.1
2-oxoglutarate
0.0063 - 0.0163
2-oxovalerate
additional information
additional information
-
0.107
2-oxoadipate
component E1, pH 7.5, 37°C
0.52
2-oxoadipate
recombinant enzyme complex, pH 7.5, 37°C
0.0025
2-oxoglutarate
mutant H298T, pH not specified in the publication, temperature not specified in the publication
0.00261
2-oxoglutarate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.00273
2-oxoglutarate
mutant H260E/H298N, pH not specified in the publication, temperature not specified in the publication
0.00341
2-oxoglutarate
mutant H298L, pH not specified in the publication, temperature not specified in the publication
0.017
2-oxoglutarate
component E1, pH 7.5, 37°C
0.06
2-oxoglutarate
-
overall activity of the complex, presence of Ca2+, absence of NADH, 30°C, pH not specified in the publication
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
0.08
2-oxoglutarate
-
activity of component E1, presence of Ca2+, absence of NADH, 30°C, pH not specified in the publication
0.11
2-oxoglutarate
-
overall activity of the complex, presence of Ca2+, presence of NADH, 30°C, pH not specified in the publication
0.13
2-oxoglutarate
-
activity of component E1, absence of Ca2+, absence of NADH, 30°C, pH not specified in the publication
0.15
2-oxoglutarate
activity of component E1, presence of Ca2+, absence of NADH, 30°C, pH not specified in the publication
0.15
2-oxoglutarate
recombinant enzyme complex, pH 7.5, 37°C
0.16
2-oxoglutarate
-
S0.5 value, 0.20 M ionic strength, pH 7.8, 30°C
0.165
2-oxoglutarate
mutant H298V, pH not specified in the publication, temperature not specified in the publication
0.2
2-oxoglutarate
activity of component E1, presence of Ca2+, presence of NADH, 30°C, pH not specified in the publication
0.21
2-oxoglutarate
-
activity of component E1, presence of Ca2+, presence of NADH, 30°C, pH not specified in the publication
0.251
2-oxoglutarate
-
S0.5 value, pH 7.5, temperature not specified in the publication
0.27
2-oxoglutarate
-
in presence of 0.2 mM AMP
0.27
2-oxoglutarate
-
S0.5 value, 0.15 M ionic strength, pH 7.8, 30°C
0.28
2-oxoglutarate
activity of component E1, absence of Ca2+, absence of NADH, 30°C, pH not specified in the publication
0.29
2-oxoglutarate
-
overall reaction, enzyme from euthermic animals, 22°C, pH 7.8
0.29
2-oxoglutarate
-
overall reaction, enzyme from hibernating animals, 37°C, pH 7.8
0.32
2-oxoglutarate
-
overall reaction, enzyme from euthermic animals, 37°C, pH 7.8
0.38
2-oxoglutarate
-
pH 7.4, 30°C
0.38
2-oxoglutarate
-
overall reaction, enzyme from hibernating animals, 22°C, pH 7.8
0.383
2-oxoglutarate
mutant H260E, pH not specified in the publication, temperature not specified in the publication
0.4
2-oxoglutarate
-
overall reaction, enzyme from hibernating animals, 5°C, pH 7.8
0.43
2-oxoglutarate
-
in presence of 0.2 M ADP
0.43
2-oxoglutarate
-
S0.5 value, 0.10 M ionic strength, pH 7.8, 30°C
0.45
2-oxoglutarate
-
overall reaction, enzyme from euthermic animals, 5°C, pH 7.8
0.47
2-oxoglutarate
-
in presence of 0.0225 mM Ca2+
0.58
2-oxoglutarate
-
in presence of 0.0023 mM Ca2+
0.65
2-oxoglutarate
-
S0.5 value, 0.05 M ionic strength, pH 7.8, 30°C
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+
1.28
2-oxoglutarate
-
overall activity of the complex, absence of Ca2+, absence of NADH, 30°C, pH not specified in the publication
1.48
2-oxoglutarate
-
activity of component E1, absence of Ca2+, presence of NADH, 30°C, pH not specified in the publication
1.57
2-oxoglutarate
activity of component E1, absence of Ca2+, presence of NADH, 30°C, pH not specified in the publication
2.5
2-oxoglutarate
-
in absence of added nucleotide
10.1
2-oxoglutarate
-
overall activity of the complex, absence of Ca2+, presence of NADH, 30°C, pH not specified in the publication
0.0063
2-oxovalerate
mutant H298L, pH not specified in the publication, temperature not specified in the publication
0.00702
2-oxovalerate
mutant H298D, pH not specified in the publication, temperature not specified in the publication
0.00896
2-oxovalerate
mutant H298V, pH not specified in the publication, temperature not specified in the publication
0.0153
2-oxovalerate
mutant H298T, pH not specified in the publication, temperature not specified in the publication
0.0163
2-oxovalerate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0032
CoA
-
S0.5 value, 0.15 M ionic strength, pH 7.8, 30°C
0.0035
CoA
-
S0.5 value, 0.10 M ionic strength, pH 7.8, 30°C
0.0042
CoA
-
S0.5 value, 0.05 M ionic strength, pH 7.8, 30°C
0.0042
CoA
-
S0.5 value, 0.20 M ionic strength, pH 7.8, 30°C
0.0198
CoA
-
S0.5 value, pH 7.5, temperature not specified in the publication
0.023
CoA
-
overall reaction, enzyme from euthermic animals, 22°C, pH 7.8
0.026
CoA
-
overall reaction, enzyme from euthermic animals, 37°C, pH 7.8
0.028
CoA
-
overall reaction, enzyme from euthermic animals, 5°C, pH 7.8
0.065
CoA
-
overall reaction, enzyme from hibernating animals, 37°C, pH 7.8
0.067
CoA
-
overall reaction, enzyme from hibernating animals, 5°C, pH 7.8
0.075
CoA
-
overall reaction, enzyme from hibernating animals, 22°C, pH 7.8
0.0249
NAD+
-
S0.5 value, Hill coefficient 0.4, pH 7.5, temperature not specified in the publication
0.031
NAD+
-
S0.5 value, 0.05 M ionic strength, pH 7.8, 30°C
0.038
NAD+
-
S0.5 value, 0.10 M ionic strength, pH 7.8, 30°C
0.05
NAD+
-
S0.5 value, 0.15 M ionic strength, pH 7.8, 30°C
0.06
NAD+
-
S0.5 value, 0.20 M ionic strength, pH 7.8, 30°C
0.09
NAD+
-
overall reaction, enzyme from hibernating animals, 5°C, pH 7.8
0.11
NAD+
-
overall reaction, enzyme from euthermic animals, 5°C, pH 7.8
0.17
NAD+
-
overall reaction, enzyme from hibernating animals, 37°C, pH 7.8
0.19
NAD+
-
overall reaction, enzyme from euthermic animals, 22°C, pH 7.8
0.25
NAD+
-
overall reaction, enzyme from euthermic animals, 37°C, pH 7.8
0.3
NAD+
-
overall reaction, enzyme from hibernating animals, 22°C, pH 7.8
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
-
additional information
additional information
-
the Hill coefficient for 2-oxoglutarate and NAD at 0.2 M ionic strength is 1.0, whereas at 0.05 M ionic strength it is 0.85 and 1.2 for 2-oxoglutarate and NAD, respectively, pH 7.8, 30°C
-
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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
Rutter, G.A.; Denton, R.M.
The binding of Ca2+ ions to pig heart NAD+-isocitrate dehydrogenase and the 2-oxoglutarate dehydrogenase complex
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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
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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
Majamaa, K.; Turpeenniemi-Hujanen, T.M.; Latip, 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 in the filamentous fungus Aspergillus niger
J. Bacteriol.
161
265-271
1985
Aspergillus niger
brenda
Lawlis, V.B.; Roche, T.E.
Inhibition of bovine kidney alpha-ketoglutarate dehydrogenase complex by reduced nicotinamide adenine dinucleotide in the presence or absence of calcium ion and effect of adenosine 5'-diphosphate on reduced nicotinamide adenine dinucleotide inhibition
Biochemistry
20
2319-2324
1981
Bos taurus
-
brenda
Shiio, I.; Ujigawa-Takeda, U.
Presence and regulation of alphe-ketoglutarate dehydrogenase complex in a glutamate-producing bacterium Brevibacterium flavum
Agric. Biol. Chem.
44
1897-1904
1980
[Brevibacterium] flavum
-
brenda
De Kok, A.; Kornfeld, S.; Benziman, M.; Milner, Y.
Subunit composition and partial reactions of the 2-oxoglutarate dehydrogenase complex of Acetobacter xylinum
Eur. J. Biochem.
106
49-58
1980
Komagataeibacter xylinus
brenda
Gupta, S.C.; Dekker, E.E.
Evidence for the identity and some comparative properties of alpha-ketoglutarate and 2-keto-4-hydroxyglutarate dehydrogenase activity
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255
1107-1112
1980
Escherichia coli, Sus scrofa
brenda
Gupta, S.C.; Dekker, E.E.
Oxidation of 2-keto-4-hydroxyglutarate by pig heart and Escherichia coli alpha-ketoglutarate dehydrogenase complex
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192
324-326
1979
Escherichia coli, Sus scrofa
brenda
Waskiewicz, D.E.; Hammes, G.G.
Elementary steps in the reaction mechanism of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: kinetics of succinylation and desuccinylation
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23
3136-3143
1984
Escherichia coli
brenda
McMinn, C.L.; Ottaway, J.H.
Studies on the mechanism and kinetics of the 2-oxoglutarate dehydrogenase system from pig heart
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161
569-581
1977
Komagataeibacter xylinus, Sus scrofa
brenda
Kornfeld, S.; Benziman, M.; Milner, Y.
alpha-Ketoglutarate dehydrogenase complex of Acetobacter xylinum. Purification and regulatory properties
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252
2940-2947
1977
Komagataeibacter xylinus
brenda
Parker, M.G.; Weitzman, P.D.J.
The purification and regulatory properties of alpha-oxoglutarate dehydrogenase from Acinetobacter lwoffi
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135
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1973
Acinetobacter lwoffii
brenda
Hirashima, M.; Hayakawa, T.; Koike, M.
Mammalian alpha-keto acid dehydrogenase complexes. II. An improved procedure for the preparation of 2-oxoglutarate dehydrogenase complex from pig heart muscle
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242
902-907
1967
Sus scrofa
brenda
Kanzaki, T.; Hayakawa, T.; Hamada, M.; Fukuyoshi, Y.; Koike, M.
Mammalian alpha-keto acid dehydrogenase complexes. IV. Substrate specificities and kinetic properties of the pig heart pyruvate and 2-oxoglutarate dehydrogenase complexes
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244
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1969
Sus scrofa
brenda
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Mammalian alpha-keto acid dehydrogenase complexes. VII. Resolution and reconstitution of the pig heart 2-oxoglutarate dehydrogenase complex
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247
4043-4049
1972
Sus scrofa
brenda
Pettit, F.H.; Hamilton, L.; Munk, P.; Namihira, G.; Eley, M.H.; Willms, C.R.; Reed, L.J.
alpha-Keto acid dehydrogenase complexes. XIX. Subunit structure of the Escherichia coli alpha-ketoglutarate dehydrogenase complex
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248
5282-5290
1973
Escherichia coli
brenda
Hirabayashi, T.; Harada, T.
Inhibition of the alpha-ketoglutarate dehydrogenase complex from baker's yeast by acetaldehyde and glyoxylate
Agric. Biol. Chem.
36
1249-1251
1972
Saccharomyces cerevisiae
-
brenda
Weitzman, P.D.J.
Regulation of alpha-ketoglutarate dehydrogenase activity in Acinetobacter
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22
323-326
1972
Acinetobacter sp., Acinetobacter sp. 4B
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Hirabayashi, T.; Harada, T.
Isolation and properties of alpha-ketoglutarate dehydrogenase complex from bakers yeast (Saccharomyces cerevisiae)
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45
1369-1375
1971
Saccharomyces cerevisiae
brenda
Brown, A.M.; Kristal, B.S.; Effron, M.S.; Shestopalov, A.I.; Ullucci, P.A.; Sheu, K.F.; Blass, J.P.; Cooper, A.J.
Zn2+ inhibits alpha-ketoglutarate-stimulated mitochondrial respiration and the isolated alpha-ketoglutarate dehydrogenase complex
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275
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2000
Sus scrofa
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Shen, X.M.; Li, H.; Dryhurst, G.
Oxidative metabolites of 5-S-cysteinyldopamine inhibit the alpha-ketoglutarate dehydrogenase complex: possible relevance to the pathogenesis of Parkinson's disease
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107
959-978
2000
Rattus norvegicus
brenda
Xin, W.; Shen, X.M.; Li, H.; Dryhurst, G.
Oxidative metabolites of 5-S-cysteinylnorepinephrine are irreversible inhibitors of mitochondrial complex I and the alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase complexes: possible implications for neurodegenerative brain disorders
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13
749-760
2000
Rattus norvegicus
brenda
McNaught, K.S.; Altomare, C.; Cellamare, S.; Carotti, A.; Thull, U.; Carrupt, P.A.; Testa, B.; Jenner, P.; Marsden, C.D.
Inhibition of alpha-ketoglutarate dehydrogenase by isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)
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6
1105-1108
1995
Rattus norvegicus
brenda
Faff-Michalak, L.; Albrecht, J.
The two catalytic components of the 2-oxoglutarate dehydrogenase complex in rat cerebral synaptic and nonsynaptic mitochondria: Comparison of the response to in vitro treatment with ammonia, hyperammonemia, and hepatic encephalopathy
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18
119-123
1993
Rattus norvegicus
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Gibson, G.E.; Park, L.C.H.; Sheu, K.F.R.; Blass, J.P.; Calingasan, N.Y.
The alpha-ketoglutarate dehydrogenase complex in neurodegeneration
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36
97-112
2000
Saccharomyces cerevisiae, Homo sapiens
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Aevarsson, A.; Chuang, J.L.; Wynn, R.M.; Turley, S.; Chuang, D.T.; Hol, W.G.J.
Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease
Structure
8
277-291
2000
Solanum tuberosum
brenda
Sheu, K.F.R.; Blass, J.P.
The alpha-ketoglutarate dehydrogenase complex
Ann. N. Y. Acad. Sci.
893
61-78
1999
Saccharomyces cerevisiae, Homo sapiens
brenda
Biryukov, A.I.; Bunik, V.I.; Zhukov, Y.N.; Khurs, E.N.; Khomutov, R.M.
Succinyl phosphonate inhibits alpha-ketoglutarate oxidative decarboxylation, catalyzed by alpha-ketoglutarate dehydrogenase complexes from E. coli and pigeon breast muscle
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382
167-170
1996
Escherichia coli, Pigeon
brenda
Bunik, V.; Westphal, A.H.; de Kok, A.
Kinetic properties of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii evidence for the formation of a precatalytic complex with 2-oxoglutarate
Eur. J. Biochem.
267
3583-3591
2000
Azotobacter vinelandii
brenda
Perham, R.N.; Jones, D.D.; Chauhan, H.J.; Howard, M.J.
Substrate channeling in 2-oxo acid dehydrogenase multienzyme complexes
Biochem. Soc. Trans.
30
47-51
2002
Azotobacter vinelandii, Geobacillus stearothermophilus, Escherichia coli, Pseudomonas putida
brenda
Huang, H.M.; Zhang, H.; Xu, H.; Gibson, G.E.
Inhibition of the alpha-ketoglutarate dehydrogenase complex alters mitochondrial function and cellular calcium regulation
Biochim. Biophys. Acta
1637
119-126
2003
Homo sapiens
brenda
Jiang, X.R.; Dryhurst, G.
Inhibition of the alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase complexes by a putative aberrant metabolite of serotonin, tryptamine-4,5-dione
Chem. Res. Toxicol.
15
1242-1247
2002
Rattus norvegicus
brenda
Kumar, M.J.; Nicholls, D.G.; Andersen, J.K.
Oxidative alpha-ketoglutarate dehydrogenase inhibition via subtle elevations in monoamine oxidase B levels results in loss of spare respiratory capacity: implications for Parkinson's disease
J. Biol. Chem.
278
46432-46439
2003
Homo sapiens
brenda
Habelhah, H.; Laine, A.; Erdjument-Bromage, H.; Tempst, P.; Gershwin, M.E.; Bowtell, D.D.; Ronai, Z.
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Homo sapiens
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Bos taurus
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Homo sapiens, Mus musculus, Sus scrofa
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Bunik, V.I.; Denton, T.T.; Xu, H.; Thompson, C.M.; Cooper, A.J.; Gibson, G.E.
Phosphonate analogues of alpha-ketoglutarate inhibit the activity of the alpha-ketoglutarate dehydrogenase complex isolated from brain and in cultured cells
Biochemistry
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2005
Bos taurus, Homo sapiens
brenda
Zhang, L.; Cooper, A.J.; Krasnikov, B.F.; Xu, H.; Bubber, P.; Pinto, J.T.; Gibson, G.E.; Hanigan, M.H.
Cisplatin-induced toxicity is associated with platinum deposition in mouse kidney mitochondria in vivo and with selective inactivation of the alpha-ketoglutarate dehydrogenase complex in LLC-PK1 cells
Biochemistry
45
8959-8971
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Sus scrofa
brenda
Strumilo, S.
Short-term regulation of the alpha-ketoglutarate dehydrogenase complex by energy-linked and some other effectors
Biochemistry
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2005
Bison bison, Bos taurus, Columba livia, Escherichia coli, Homo sapiens, Rattus norvegicus, Solanum tuberosum, Sus scrofa
brenda
Bunik, V.I.; Raddatz, G.; Wanders, R.J.; Reiser, G.
Brain pyruvate and 2-oxoglutarate dehydrogenase complexes are mitochondrial targets of the CoA ester of the Refsum disease marker phytanic acid
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Rattus norvegicus
brenda
Waagepetersen, H.S.; Hansen, G.H.; Fenger, K.; Lindsay, J.G.; Gibson, G.; Schousboe, A.
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Mus musculus
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Santos, S.S.; Gibson, G.E.; Cooper, A.J.; Denton, T.T.; Thompson, C.M.; Bunik, V.I.; Alves, P.M.; Sonnewald, U.
Inhibitors of the alpha-ketoglutarate dehydrogenase complex alter [1-13C]glucose and [U-13C]glutamate metabolism in cerebellar granule neurons
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Mus musculus
brenda
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Bos taurus, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus, Sus scrofa
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Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
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Applegate, M.A.; Humphries, K.M.; Szweda, L.I.
Reversible inhibition of alpha-ketoglutarate dehydrogenase by hydrogen peroxide: glutathionylation and protection of lipoic acid
Biochemistry
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2008
Rattus norvegicus
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Shi, Q.; Xu, H.; Kleinman, W.A.; Gibson, G.E.
Novel functions of the alpha-ketoglutarate dehydrogenase complex may mediate diverse oxidant-induced changes in mitochondrial enzymes associated with Alzheimers disease
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Homo sapiens
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Hasegawa, T.; Hashimoto, K.; Kawasaki, H.; Nakamatsu, T.
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Geobacillus stearothermophilus, Homo sapiens (Q96HY7), Homo sapiens (Q9ULD0)
brenda
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Homo sapiens
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Intra-mitochondrial poly(ADP-ribosyl)ation: potential role for alpha-ketoglutarate dehydrogenase
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Rattus norvegicus
brenda
Zuendorf, G.; Kahlert, S.; Bunik, V.I.; Reiser, G.
alpha-Ketoglutarate dehydrogenase contributes to production of reactive oxygen species in glutamate-stimulated hippocampal neurons in situ
Neuroscience
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Rattus norvegicus
brenda
Araujo, W.L.; Nunes-Nesi, A.; Trenkamp, S.; Bunik, V.I.; Fernie, A.R.
Inhibition of 2-oxoglutarate dehydrogenase in potato tuber suggests the enzyme is limiting for respiration and confirms its importance in nitrogen assimilation,
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Solanum tuberosum
brenda
Sykes, S.E.; Hajduk, S.L.
Dual functions of alpha-ketoglutarate dehydrogenase E2 in the Krebs cycle and mitochondrial DNA inheritance in Trypanosoma brucei
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2013
Trypanosoma brucei
brenda
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Arabidopsis thaliana, Rattus norvegicus
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Plant mitochondrial 2-oxoglutarate dehydrogenase complex purification and characterization in potato
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Solanum tuberosum (P81895 and P81896 and P80503)
brenda
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Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli
Biochemistry
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Escherichia coli (P0AFG6)
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Escherichia coli (P0AFG3)
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Homo sapiens (A0A024R713 and A0A024R6C9)
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Neurospora crassa
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Sus scrofa
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Homo sapiens (A0A024R713 and A0A024R6C9 and Q02218), Homo sapiens (Q02218)
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Homo sapiens
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Knapp, J.E.; Mitchell, D.T.; Yazdi, M.A.; Ernst, S.R.; Reed, L.J.; Hackert, M.L.
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Escherichia coli (P0AFG6)
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Kinugawa, H.; Kondo, N.; Komine-Abe, A.; Tomita, T.; Nishiyama, M.; Kosono, S.
In vitro reconstitution and characterization of pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase hybrid complex from Corynebacterium glutamicum
MicrobiologyOpen
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Corynebacterium glutamicum (Q8NRC3 and Q8NNJ2 and Q8NTE1), Corynebacterium glutamicum DSM 20300 (Q8NRC3 and Q8NNJ2 and Q8NTE1)
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Bailey, P.S.J.; Ortmann, B.M.; Martinelli, A.W.; Houghton, J.W.; Costa, A.S.H.; Burr, S.P.; Antrobus, R.; Frezza, C.; Nathan, J.A.
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Homo sapiens (Q02218 and P36957 and P09622)
brenda
Condori-Apfata, J.A.; Batista-Silva, W.; Medeiros, D.B.; Vargas, J.R.; Valente, L.M.L.; Heyneke, E.; Perez-Diaz, J.L.; Fernie, A.R.; Araujo, W.L.; Nunes-Nesi, A.
The Arabidopsis E1 subunit of the 2-oxoglutarate dehydrogenase complex modulates plant growth and seed production
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Arabidopsis thaliana (F4IWV2), Arabidopsis thaliana (Q9FLH2)
brenda
Murphy, G.; Jensen, G.
Electron cryotomography of the E. coli pyruvate and 2-oxoglutarate dehydrogenase complexes
Structure
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1765-1773
2005
Escherichia coli
brenda
Tsepkova, P.M.; Artiukhov, A.V.; Boyko, A.I.; Aleshin, V.A.; Mkrtchyan, G.V.; Zvyagintseva, M.A.; Ryabov, S.I.; Ksenofontov, A.L.; Baratova, L.A.; Graf, A.V.; Bunik, V.I.
Thiamine induces long-term changes in amino acid profiles and activities of 2-oxoglutarate and 2-oxoadipate dehydrogenases in rat brain
Biochemistry
82
723-736
2017
Rattus norvegicus
brenda
Green, S.R.; Storey, K.B.
Regulation of the alpha-ketoglutarate dehydrogenasecomplex during hibernation in a small mammal, the Richardsons ground squirrel (Urocitellus richardsonii)
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Urocitellus richardsonii
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Lu, X.; Yang, P.; Zhao, X.; Jiang, M.; Hu, S.; Ouyang, Y.; Zeng, L.; Wu, J.
OGDH mediates the inhibition of SIRT5 on cell proliferation and migration of gastric cancer
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Homo sapiens
brenda
Nemeria, N.S.; Gerfen, G.; Nareddy, P.R.; Yang, L.; Zhang, X.; Szostak, M.; Jordan, F.
The mitochondrial 2-oxoadipate and 2-oxoglutarate dehydrogenase complexes share their E2 and E3 components for their function and both generate reactive oxygen species
Free Radic. Biol. Med.
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136-145
2018
Homo sapiens (Q96HY7 and Q02218)
brenda
Baldi, N.; Dykstra, J.C.; Luttik, M.A.H.; Pabst, M.; Wu, L.; Benjamin, K.R.; Vente, A.; Pronk, J.T.; Mans, R.
Functional expression of a bacterial alpha-ketoglutarate dehydrogenase in the cytosol of Saccharomyces cerevisiae
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190-197
2019
Escherichia coli (P0AFG3 and P0AFG6 and P0A9P0)
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