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Nat Chem Biol. 2011 May 29;7(7):434-6. doi: 10.1038/nchembio.589.

FrsA functions as a cofactor-independent decarboxylase to control metabolic flux.

Author information

1
Department 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).

PMID:
21623357
DOI:
10.1038/nchembio.589
[Indexed for MEDLINE]

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