Literature summary extracted from
Parker, M.G.; Weitzman, P.D.J.
The purification and regulatory properties of alpha-oxoglutarate dehydrogenase from Acinetobacter lwoffi (1973), Biochem. J., 135, 215-223.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.2.1.105 |
ADP |
stimulates 2-oxoglutarate dehydrogenase complex |
Acinetobacter lwoffii |
|
1.2.1.105 |
AMP |
stimulates 2-oxoglutarate dehydrogenase complex |
Acinetobacter lwoffii |
|
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.2.1.105 |
NADH |
2-oxoglutarate dehydrogenase complex |
Acinetobacter lwoffii |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.2.1.105 |
Acinetobacter lwoffii |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.2.1.105 |
2-oxoglutarate dehydrogenase complex |
Acinetobacter lwoffii |
Reaction
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 |
Acinetobacter lwoffii |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.2.1.105 |
2-oxoglutarate + lipoamide |
- |
Acinetobacter lwoffii |
S-succinyldihydrolipoamide + CO2 |
- |
? |
|