FrsA functions as a cofactor-independent decarboxylase to control metabolic flux.
Nat Chem Biol
; 7(7): 434-6, 2011 May 29.
Article
in En
| MEDLINE
| ID: mdl-21623357
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:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Recombinant Proteins
/
Phosphoenolpyruvate Sugar Phosphotransferase System
/
Carboxy-Lyases
/
Pyruvic Acid
/
Escherichia coli Proteins
/
Glucose
Language:
En
Journal:
Nat Chem Biol
Journal subject:
BIOLOGIA
/
QUIMICA
Year:
2011
Document type:
Article