FrsA functions as a cofactor-independent decarboxylase to control metabolic flux
Kyung-Jo Lee1, Chang-Sook Jeong, Young Jun An
1Department of Environmental Science, Hankuk University of Foreign Studies, Yongin, Republic of Korea.
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).
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