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- Title
Chimeric phosphofructokinases involving exchange of the N- and C-terminal halves of mammalian isozymes: Implications for ligand binding sites
- Authors
Martínez-Costa, Oscar H.; Sánchez-Martínez, Cristina; Sánchez, Valentina; Aragón, Juan J.
- Abstract
Abstract: Two phosphofructokinase (PFK) chimeras were constructed by exchanging the N- and C-terminal halves of the mammalian M- and C-type isozymes, to investigate the contribution of each terminus to the catalytic site and the fructose-2,6-P2/fructose-1,6-P2 allosteric site. The homogeneously-purified chimeric enzymes organized into tetramers, and exhibited kinetic properties for fructose-6-P and MgATP similar to those of the native enzyme that furnished the N-terminal domain in each case, whereas their fructose-2,6-P2 activatory characteristics coincided with those of the isozyme that provided the C-terminal half. This reflected the role of each domain in the formation of the corresponding binding site. Grafting the N-terminus of PFK-M onto the C-terminus of the fructose-1,6-P2 insensitive PFK-C restored transduction of this signal to the catalytic site, which significance is also discussed.
- Subjects
PHOSPHOFRUCTOKINASE 1; ISOENZYMES; LIGANDS (Biochemistry); GLYCOLYSIS
- Publication
FEBS Letters, 2007, Vol 581, Issue 16, p3033
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2007.05.059