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Uncoupling the MgATP‐induced inhibition and aggregation of Escherichia coli phosphofructokinase‐2 by C‐terminal mutations
Author(s) -
Baez Mauricio,
Merino Felipe,
Astorga Guadalupe,
Babul Jorge
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.05.011
Subject(s) - escherichia coli , phosphofructokinase , terminal (telecommunication) , chemistry , biochemistry , diphosphoglycerate , biophysics , glycolysis , enzyme , biology , gene , hemoglobin , telecommunications , computer science
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.