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Fructose‐6‐phosphate modifies the pathway of the urea‐induced dissociation of the allosteric phosphofructokinase from Escherichia coli
Author(s) -
Teschner Wolfgang,
Deville-Bonne Dominique,
Garel Jean-Renaud
Publication year - 1990
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 - 10.1016/0014-5793(90)80297-v
Subject(s) - allosteric regulation , phosphofructokinase , fructose , tetramer , chemistry , urea , biochemistry , escherichia coli , protein subunit , phosphate , phosphofructokinase 1 , glucose 6 phosphate , fructose 1,6 bisphosphatase , hexokinase , stereochemistry , enzyme , glycolysis , gene
Phosphofructokinase from Escherichia coli binds fructose‐6‐phosphate with the sugar moiety of the substrate interacting with one subunit and the phosphate group with another one, so that bound fructose‐6‐phosphate lies across the interface between the subunits [(1988) J. Mol. Biol. 204, 973‐994]. When this interface is ‘cross‐linked’ by fructose‐6‐phosphate. it becomes more stable because of the extra interactions between subunits: inactivation upon dissociation occurs only above 5 M urea, instead of 1 M urea for the free protein. At saturation in fructose‐6‐phosphate. this interface is no longer the first to dissociate as in the free protein [(1989) Biochemistry 28, 6836‐6841]: instead, the addition of urea to phosphofructo‐kinase in the presence of fructose‐6‐phosphate induces a conformational change within the tetramer which alters the environment of Trp‐311 and distorts the regulatory site.