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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2011-6-20
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1552-4469
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
434-6
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pubmed:dateRevised |
2011-9-29
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pubmed:meshHeading |
pubmed-meshheading:21623357-Acetaldehyde,
pubmed-meshheading:21623357-Animals,
pubmed-meshheading:21623357-Base Sequence,
pubmed-meshheading:21623357-Carbon Dioxide,
pubmed-meshheading:21623357-Carboxy-Lyases,
pubmed-meshheading:21623357-Crystallography, X-Ray,
pubmed-meshheading:21623357-Decarboxylation,
pubmed-meshheading:21623357-Dose-Response Relationship, Drug,
pubmed-meshheading:21623357-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:21623357-Escherichia coli,
pubmed-meshheading:21623357-Escherichia coli Proteins,
pubmed-meshheading:21623357-Female,
pubmed-meshheading:21623357-Fermentation,
pubmed-meshheading:21623357-Glucose,
pubmed-meshheading:21623357-Kinetics,
pubmed-meshheading:21623357-Magnetic Resonance Spectroscopy,
pubmed-meshheading:21623357-Mice,
pubmed-meshheading:21623357-Mice, Inbred ICR,
pubmed-meshheading:21623357-Models, Molecular,
pubmed-meshheading:21623357-Molecular Sequence Data,
pubmed-meshheading:21623357-Mutagenesis, Site-Directed,
pubmed-meshheading:21623357-Phosphoenolpyruvate Sugar Phosphotransferase System,
pubmed-meshheading:21623357-Protein Conformation,
pubmed-meshheading:21623357-Pyruvic Acid,
pubmed-meshheading:21623357-Recombinant Proteins,
pubmed-meshheading:21623357-Substrate Specificity,
pubmed-meshheading:21623357-Vibrio vulnificus,
pubmed-meshheading:21623357-Virulence
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pubmed:year |
2011
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pubmed:articleTitle |
FrsA functions as a cofactor-independent decarboxylase to control metabolic flux.
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pubmed:affiliation |
Department of Environmental Science, Hankuk University of Foreign Studies, Yongin, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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