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- Title
Uncoupling the MgATP-induced inhibition and aggregation of Escherichia coli phosphofructokinase-2 by C-terminal mutations
- Authors
Baez, Mauricio; Merino, Felipe; Astorga, Guadalupe; Babul, Jorge
- Abstract
Abstract: Binding of MgATP to an allosteric site of Escherichia coli phosphofructokinase-2 (Pfk-2) provoked inhibition and a dimer–tetramer (D–T) conversion of the enzyme. Successive deletions of up to 10 residues and point mutations at the C-terminal end led to mutants with elevated K Mapp values for MgATP which failed to show the D–T conversion, but were still inhibited by the nucleotide. Y306 was required for the quaternary packing involved in the D–T conversion and the next residue, L307, was crucial for the ternary packing necessary for the catalytic MgATP-binding site. These results show that the D–T conversion could be uncoupled from the conformational changes that lead to the MgATP-induced allosteric inhibition.
- Subjects
ESCHERICHIA coli; PHOSPHOFRUCTOKINASE 1; GENETIC mutation; NUCLEOTIDES
- Publication
FEBS Letters, 2008, Vol 582, Issue 13, p1907
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2008.05.011