| Title : FrsA functions as a cofactor-independent decarboxylase to control metabolic flux - Lee_2011_Nat.Chem.Biol_7_434 |
| Author(s) : Lee KJ , Jeong CS , An YJ , Lee HJ , Park SJ , Seok YJ , Kim P , Lee JH , Lee KH , Cha SS |
| Ref : Nat Chemical Biology , 7 :434 , 2011 |
|
Abstract :
The interaction between fermentation-respiration switch (FrsA) protein and glucose-specific enzyme IIA(Glc) increases glucose fermentation under oxygen-limited conditions. We show that FrsA converts pyruvate to acetaldehyde and carbon dioxide in a cofactor-independent manner and that its pyruvate decarboxylation activity is enhanced by the dephosphorylated form of IIA(Glc) (d-IIA(Glc)). Crystal structures of FrsA and its complex with d-IIA(Glc) revealed residues required for catalysis as well as the structural basis for the activation by d-IIA(Glc). |
| PubMedSearch : Lee_2011_Nat.Chem.Biol_7_434 |
| PubMedID: 21623357 |
| Gene_locus related to this paper: vibvy-y856 |
| Gene_locus | vibvy-y856 |
| Family | UPF0255 Duf_1100-S Duf_1100-R |
| Structure | 3MVE 3OUR |
Lee KJ, Jeong CS, An YJ, Lee HJ, Park SJ, Seok YJ, Kim P, Lee JH, Lee KH, Cha SS (2011)
FrsA functions as a cofactor-independent decarboxylase to control metabolic flux
Nat Chemical Biology
7 :434
Lee KJ, Jeong CS, An YJ, Lee HJ, Park SJ, Seok YJ, Kim P, Lee JH, Lee KH, Cha SS (2011)
Nat Chemical Biology
7 :434