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- Title
FrsA functions as a cofactor-independent decarboxylase to control metabolic flux.
- Authors
Lee, Kyung-Jo; Jeong, Chang-Sook; An, Young Jun; Lee, Hyun-Jung; Park, Soon-Jung; Seok, Yeong-Jae; Kim, Pil; Lee, Jung-Hyun; Lee, Kyu-Ho; Cha, Sun-Shin
- Abstract
The interaction between fermentation-respiration switch (FrsA) protein and glucose-specific enzyme IIAGlc 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 IIAGlc (d-IIAGlc). Crystal structures of FrsA and its complex with d-IIAGlc revealed residues required for catalysis as well as the structural basis for the activation by d-IIAGlc.
- Subjects
GLUCOSE synthesis; FERMENTATION; DECARBOXYLASES; PYRUVATE carboxylase; ACETALDEHYDE; CARBON dioxide
- Publication
Nature Chemical Biology, 2011, Vol 7, Issue 7, p434
- ISSN
1552-4450
- Publication type
Academic Journal
- DOI
10.1038/nchembio.589