Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.1.104 extracted from

  • Kinugawa, H.; Kondo, N.; Komine-Abe, A.; Tomita, T.; Nishiyama, M.; Kosono, S.
    In vitro reconstitution and characterization of pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase hybrid complex from Corynebacterium glutamicum (2020), MicrobiologyOpen, 9, e1113 .
    View publication on PubMed

Organism

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

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