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

BRENDA support

Literature summary for 1.5.5.1 extracted from

  • Demmer, J.K.; Pal Chowdhury, N.; Selmer, T.; Ermler, U.; Buckel, W.
    The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile (2017), Nat. Commun., 8, 1577 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.5.5.1

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray structure of the (EtfAB/Bcd)4 complex in the dehydrogenase-conducting D-state, alpha-FAD (bound to domain II of EtfA) and delta-FAD (bound to butyryl-CoA dehydrogenase Bcd) being 8 A apart. A rotation of domain II of nearly 80° is observed, further rotation by 10° brings EtfAB into the bifurcating B-state, alpha-FAD and beta-FAD (bound to EtfB) being 14 A apart Clostridioides difficile

Organism

Organism UniProt Comment Textmining
Clostridioides difficile A0A125V455 subunit alpha, bifunctional electron transferring flavoprotein/butyryl-CoA dehydrogenase
-
Clostridioides difficile DSM 1296 A0A125V455 subunit alpha, bifunctional electron transferring flavoprotein/butyryl-CoA dehydrogenase
-

Synonyms

Synonyms Comment Organism
EtfA2
-
 Clostridioides difficile

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Clostridioides difficile

General Information

General Information Comment Organism
metabolism enzyme catalyzes the reduction of one crotonyl-CoA and two ferredoxins by two NADH within a flavin-based electron-bifurcating process. NADH reduces beta-FAD, which bifurcates. One electron goes to ferredoxin and one to alpha-FAD, which swings over to reduce delta-FAD to the semiquinone. Repetition affords a second reduced ferredoxin and delta-FADH-, which reduces crotonyl-CoA Clostridioides difficile