FrsA functions as a cofactor-independent decarboxylase to control metabolic flux
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | 차선신 | - |
| dc.date.accessioned | 2020-07-16T14:51:40Z | - |
| dc.date.available | 2020-07-16T14:51:40Z | - |
| dc.date.created | 2020-02-11 | - |
| dc.date.issued | 2011-09-30 | - |
| dc.identifier.uri | https://sciwatch.kiost.ac.kr/handle/2020.kiost/28198 | - |
| dc.description.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 | - |
| dc.description.uri | 2 | - |
| dc.language | English | - |
| dc.publisher | 대한화학회 | - |
| dc.relation.isPartOf | The Korea chemical Society | - |
| dc.title | FrsA functions as a cofactor-independent decarboxylase to control metabolic flux | - |
| dc.type | Conference | - |
| dc.citation.conferencePlace | KO | - |
| dc.citation.title | The Korea chemical Society | - |
| dc.contributor.alternativeName | 차선신 | - |
| dc.identifier.bibliographicCitation | The Korea chemical Society | - |
| dc.description.journalClass | 2 | - |
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