Abstract
Fructose 2,6-bisphosphate (Fru-2,6-P2) is a potent stimulator of 6-phosphofructo 1-kinase which has been identified in all eukaryotic cells. Its synthesis and breakdown are catalyzed by 6-phosphofructo 2-kinase (PFK-2) and fructose 2,6-bisphosphatase (FBPase-2), respectively. These two activities belong to separate domains of the same homodimeric protein (Van Schaftingen, 1987; Pilkis & EL-Maghrabi, 1988). Differences between tissues in the PFK-2/FBPase-2 activity ratio, kinetic and antigenic properties have suggested the existence of several PFK-2/FBPase-2 isoenzymes (Hue & Rider, 1987; Taniyama et al., 1988). The liver “L” and the muscle “M” isozymes have a common sequence of 438 aminoacids and differ at the N-terminus. In the “L” type, the divergent sequence is 32 residues long and contains the serine phosphorylated by cAMP-dependent protein kinase (PKA). The “M” type has a divergent sequence of 10 residues, containing a protein kinase C (PKC) target (Lively et al.,1988; Darville et al.,1989). The bovine heart “H” isozyme has a well-conserved sequence of 530 aminoacids, differing only at the N and C-terminus. Interestingly, it has phosphorylation targets for both PKA and PKC at the C-terminus (Sakata & Uyeda, 1990).
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References
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© 1991 Springer-Verlag Berlin Heidelberg
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Ventura, F., Rosa, J.L., Ambrosio, S., Gil, J., Tauler, A., Bartrons, R. (1991). 6-Phosphofructo 2-Kinase/Fructose 2, 6-Bisphosphatase: Kinetic Changes Induced by Phosphorylation. In: Heilmeyer, L.M.G. (eds) Cellular Regulation by Protein Phosphorylation. NATO ASI Series, vol 56. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75142-4_16
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DOI: https://doi.org/10.1007/978-3-642-75142-4_16
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