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

Authors
 Kyung-Jo Lee  ;  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 
Citation
 NATURE CHEMICAL BIOLOGY, Vol.7(7) : 434-436, 2011 
Journal Title
 NATURE CHEMICAL BIOLOGY 
ISSN
 1552-4450 
Issue Date
2011
MeSH
Acetaldehyde/metabolism ; Animals ; Base Sequence ; Carbon Dioxide/metabolism ; Carboxy-Lyases/chemistry ; Carboxy-Lyases/genetics ; Carboxy-Lyases/metabolism* ; Carboxy-Lyases/pharmacology ; Crystallography, X-Ray ; Decarboxylation ; Dose-Response Relationship, Drug ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/genetics ; Escherichia coli/growth & development ; Escherichia coli/metabolism ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism* ; Female ; Fermentation ; Glucose/metabolism* ; Kinetics ; Magnetic Resonance Spectroscopy ; Mice ; Mice, Inbred ICR ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phosphoenolpyruvate Sugar Phosphotransferase System/chemistry ; Phosphoenolpyruvate Sugar Phosphotransferase System/genetics ; Phosphoenolpyruvate Sugar Phosphotransferase System/metabolism* ; Protein Conformation ; Pyruvic Acid/metabolism* ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism* ; Recombinant Proteins/pharmacology ; Substrate Specificity ; Vibrio vulnificus/genetics ; Vibrio vulnificus/metabolism ; Vibrio vulnificus/pathogenicity ; Virulence
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).
Full Text
http://www.nature.com/nchembio/journal/v7/n7/full/nchembio.589.html
DOI
10.1038/nchembio.589
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Environmental Medical Biology (환경의생물학교실) > 1. Journal Papers
Yonsei Authors
Park, Soon Jung(박순정) ORCID logo https://orcid.org/0000-0002-0423-1944
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/95317
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