Fructose‐6‐phosphate modifies the pathway of the urea‐induced dissociation of the allosteric phosphofructokinase from Escherichia coli
- 2 July 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 267 (1), 96-98
- https://doi.org/10.1016/0014-5793(90)80297-v
Abstract
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.Keywords
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