EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.105 | spermine | enhances activity | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.105 | 4-hydroxy-2-nonenal | - |
Homo sapiens | |
1.2.1.105 | H2O2 | - |
Homo sapiens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.2.1.105 | 4 | - |
2-oxoglutarate | - |
Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.2.1.105 | mitochondrion | - |
Homo sapiens | 5739 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.105 | Ca2+ | Ca2+ and Mg2+ together synergistically reduce the Km-value for 2-oxoglutarate by over 10fold | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.105 | 2-oxoglutarate + lipoamide | Saccharomyces cerevisiae | - |
S-succinyldihydrolipoamide + CO2 | - |
? | |
1.2.1.105 | 2-oxoglutarate + lipoamide | Homo sapiens | 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 | S-succinyldihydrolipoamide + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.105 | Homo sapiens | - |
- |
- |
1.2.1.105 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.2.1.105 | 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 | Homo sapiens | |
1.2.1.105 | 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 | Saccharomyces cerevisiae |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.2.1.105 | brain | neurons that appear slectively vulnerable in human temporal cortex in Alzheimer's disease are enriched in the 2-oxoglutarate dehydrogenase complex | Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.105 | 2-oxoglutarate + lipoamide | - |
Saccharomyces cerevisiae | S-succinyldihydrolipoamide + CO2 | - |
? | |
1.2.1.105 | 2-oxoglutarate + lipoamide | reaction is physiologically irreversible, due to the volatility of CO2 | Homo sapiens | S-succinyldihydrolipoamide + CO2 | - |
ir | |
1.2.1.105 | 2-oxoglutarate + lipoamide | 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 | Homo sapiens | S-succinyldihydrolipoamide + CO2 | - |
? |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.105 | thiamine diphosphate | - |
Saccharomyces cerevisiae | |
1.2.1.105 | thiamine diphosphate | thiamine diphosphate is tightly but not covalently bound to the 2-oxoglutarate dehydrogenase component | Homo sapiens |