FrsA functions as a cofactor-independent decarboxylase to control metabolic flux
Yeong-Jae Seok ; Kyung-Jo Lee ; Sun-Shin Cha ; Kyu-Ho Lee ; Jung-Hyun Lee ; Pil Kim ; Soon-Jung Park ; Hyun-Jung Lee ; Young Jun An ; Chang-Sook Jeong
Nature Chemical Biology, Vol.7(7) : 434~436, 2011
Nature Chemical Biology
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).