Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ADP | stimulates | Homo sapiens | |
ADP | stimulates | Saccharomyces cerevisiae | |
NAD+ | stimulates | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine | - |
Homo sapiens | |
1-methyl-4-phenylpyridinium | - |
Homo sapiens | |
ATP | - |
Homo sapiens | |
Ca2+ | 0.01 mM, decreases the concentration of 2-oxoglutarate required for half-maximal activity, inhibition at higher concentrations | Homo sapiens | |
NADH | - |
Homo sapiens | |
NH4+ | - |
Homo sapiens | |
Valproic acid | - |
Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Homo sapiens | 5739 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | 0.01 mM, decreases the concentration of 2-oxoglutarate required for half-maximal activity, inhibition at higher concentrations | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxoglutarate + lipoamide | Saccharomyces cerevisiae | - |
S-succinyldihydrolipoamide + CO2 | - |
? | |
2-oxoglutarate + lipoamide | Homo sapiens | 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 | S-succinyldihydrolipoamide + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | |
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 |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | endothelial cells have about six times higher activity than do brain microglial cells or neurons | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxoglutarate + lipoamide | - |
Homo sapiens | S-succinyldihydrolipoamide + CO2 | - |
? | |
2-oxoglutarate + lipoamide | - |
Saccharomyces cerevisiae | S-succinyldihydrolipoamide + CO2 | - |
? | |
2-oxoglutarate + lipoamide | 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 | Homo sapiens | S-succinyldihydrolipoamide + CO2 | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | EC 1.8.1.4, dihydrolipoyl dehydrogenase component of the 2-oxoglutarate dehydrogenase complex is a flavin protein | Homo sapiens | |
additional information | EC 2.3.1.61, dihydrolipoamide succinyltransferase component of the 2-oxoglutarate dehydrogenase enzyme complex contains a lipoate moiety that is covalently bound to Lys110 through an epsilon-amide linkage. The thiamine diphosphate reaction adduct then reductively acylates the lipoyl moiety of EC 2.3.1.61 | Homo sapiens | |
thiamine diphosphate | - |
Saccharomyces cerevisiae | |
thiamine diphosphate | 2-oxoglotarate dehydrogenase component of the 2-oxoglutarate dehydrogenase complex is dependent on thiamine diphosphate. Thiamine diphosphate attacks the alpha-carbon of 2-oxoglutarate and decarboxylates the substrate. The thiamine diphosphate reaction adduct then reductively acylates the lipoyl moiety of EC 2.3.1.61 | Homo sapiens | |
thiamine diphosphate | required, 2-oxoglutarate dehydrogenase component | Homo sapiens |