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

Title
FrsA functions as a cofactor-independent decarboxylase to control metabolic flux
Authors
Yeong-Jae Seok;Kyung-Jo Lee;Sun-Shin Cha;Kyu-Ho Lee;Jung-Hyun Lee;Pil Kim;Soon-Jung Park;Hyun-Jung Lee;Young Jun An;Chang-Sook Jeong
Issue Date
2011
Journal Title
Nature Chemical Biology
ISSN
1552-4450
Citation
Nature Chemical Biology, Vol.7(7) : 434~436, 2011
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).
URI
http://www.nature.com/nchembio/journal/v7/n7/full/nchembio.589.html

http://ir.ymlib.yonsei.ac.kr/handle/22282913/95317
DOI
10.1038/nchembio.589
Appears in Collections:
1. 연구논문 > 1. College of Medicine > Dept. of Environmental Medical Biology
Yonsei Authors
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