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

Title
FrsA functions as a cofactor-independent decarboxylase to control metabolic flux
Author(s)
차선신
Publication Year
2011-09-30
Abstract
The interaction between fermentation-respiration switch(FrsA) protein and glucose-specific enzyme IIAGlc increasesglucose fermentation under oxygen-limited conditions. Weshow that FrsA converts pyruvate to acetaldehyde and carbondioxide in a cofactor-independent manner and that its pyruvatedecarboxylation activity is enhanced by the dephosphorylatedform of IIAGlc (d-IIAGlc). Crystal structures of FrsA and itscomplex with d-IIAGlc revealed residues required for catalysisas well as the structural basis for the activation by d-IIAGlc.The bacterial phosphoenolpyruvate:sugar phosphotransferase
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/28198
Bibliographic Citation
The Korea chemical Society, 2011
Publisher
대한화학회
Type
Conference
Language
English
Publisher
대한화학회
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