Journal
NATURE CHEMICAL BIOLOGY
Volume 7, Issue 7, Pages 434-436Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.589
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Funding
- Ministry of Land, Transport and Maritime Affairs
- Ministry of Education, Science and Technology [2009-0092822]
- KORDI in-house program [PE98513]
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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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