Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | - |
- |
- |
Corynebacterium glutamicum | Q8NNF6 and Q8NNJ2 and Q8NTE1 | Q8NNF6 i.e. component E1, cf. EC 1.2.42, Q8NNJ2 i.e. component E2, cf. EC 2.3.1.61, Q8NTE1 i.e. component E3, cf. EC 1.8.1.4 | - |
Corynebacterium glutamicum ATCC 13869 | - |
- |
- |
Corynebacterium glutamicum DSM 20300 | Q8NNF6 and Q8NNJ2 and Q8NTE1 | Q8NNF6 i.e. component E1, cf. EC 1.2.42, Q8NNJ2 i.e. component E2, cf. EC 2.3.1.61, Q8NTE1 i.e. component E3, cf. EC 1.8.1.4 | - |
General Information | Comment | Organism |
---|---|---|
physiological function | a hybrid complex consisting of E1p (thiamine diphosphate-dependent pyruvate dehydrogenase, AceE), E2 (dihydrolipoamide acetyltransferase, AceF), E3 (dihydrolipoamide dehydrogenase, Lpd), and E1o (thiamine diphosphate-dependent 2-oxoglutarate dehydrogenase, OdhA) contains six copies of E2 in its core. E2 forms a stable complex with E3 (E2-E3 subcomplex) in vitro, hypothetically comprised of two E2 trimers and four E3 dimers. E1o exists mainly as a hexamer in solution and is ready to form an active ODH complex when mixed with the E2-E3 subcomplex. In vitro, there is E1p- and E1o-dependent inhibition of ODH and PDH, respectively, actively supporting the formation of the hybrid complex, in which both E1p and E1o associate with a single E2-E3 | Corynebacterium glutamicum |
physiological function | in Corynebacterium glutamicum, the PDH-ODH hybrid complex consists of six copies of subunit E2 in its core. E2 forms a stable complex with E3 (E2-E3 subcomplex) in vitro, hypothetically comprised of two E2 trimers and four E3 dimers. E1o exists mainly as a hexamer in solution and is ready to form an active ODH complex when mixed with the E2-E3 subcomplex. Inhibition of ODH and PDH is E1p- and E1o-dependent, respectively, actively supporting the formation Iof the hybrid complex, in which both E1p and E1o associate with a single E2-E3 | Corynebacterium glutamicum |