EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.105 | Ca2+ | activates | Sus scrofa | |
1.2.1.105 | Mg2+ | activates 2-oxoglutarate dehydrogenase complex | Sus scrofa |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.2.1.105 | additional information | - |
2700000 is the MW of the 2-oxoglutarate dehydrogenase complex, gel filtration | Sus scrofa |
1.2.1.105 | additional information | - |
2800000 Da is the MW of the 2-oxoglutarate dehydrogenase complex, calculation from sedimentation and diffusion data | Sus scrofa |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.105 | Sus scrofa | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.2.1.105 | 2-oxoglutarate dehydrogenase complex | Sus scrofa |
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 | Sus scrofa |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.2.1.105 | heart | - |
Sus scrofa | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.105 | 2-oxoglutarate + lipoamide | - |
Sus scrofa | S-succinyldihydrolipoamide + CO2 | - |
? | |
1.2.1.105 | additional information | enzyme complex is also active with 2-oxoadipate | Sus scrofa | ? | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.2.1.105 | 30 | 35 | 2-oxoglutarate dehydrogenase activity | Sus scrofa |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.2.1.105 | 6.5 | - |
2-oxoglutarate dehydrogenase reaction | Sus scrofa |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.105 | additional information | 2-oxoglutarate dehydrogenase complex contains protein-bound lipoic acid | Sus scrofa | |
1.2.1.105 | additional information | 2-oxoglutarate dehydrogenase complex contains FAD | Sus scrofa | |
1.2.1.105 | thiamine diphosphate | 2-oxoglutarate dehydrogenase complex contains thiamine diphosphate | Sus scrofa |