| Literature DB >> 21623357 |
Kyung-Jo Lee1, Chang-Sook Jeong, Young Jun An, Hyun-Jung Lee, Soon-Jung Park, Yeong-Jae Seok, Pil Kim, Jung-Hyun Lee, Kyu-Ho Lee, Sun-Shin Cha.
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).Entities:
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Year: 2011 PMID: 21623357 DOI: 10.1038/nchembio.589
Source DB: PubMed Journal: Nat Chem Biol ISSN: 1552-4450 Impact factor: 15.040