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2003 | 50 | 1 | 115-121
Article title

Rabbit muscle fructose-1,6-bisphosphatase is phosphorylated in vivo.

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Abstracts
EN
Phosphorylated fructose-1,6-bisphosphatase (FBPase) was isolated from rabbit muscle in an SDS/PAGE homogeneous form. Its dephosphorylation with alkaline phosphatase revealed 2.8 moles of inorganic phosphate per mole of FBPase. The phosphorylated FBPase (P-FBPase) differs from the dephosphorylated enzyme in terms of its kinetic properties like Km and kcat, which are two times higher for the phosphorylated FBPase, and in the affinity for aldolase, which is three times lower for the dephosphorylated enzyme. ephosphorylated FBPase can be a substrate for protein kinase A and the amount of phosphate incorporated per FBPase monomer can reach 2-3 molecules. Since interaction of muscle aldolase with muscle FBPase results in desensitisation of the latter toward AMP inhibition (Rakus & Dzugaj, 2000, Biochem. Biophys. Res. Commun. 275, 611-616), phosphorylation may be considered as a way of muscle FBPase activity regulation.
Publisher

Year
Volume
50
Issue
1
Pages
115-121
Physical description
Dates
published
2003
received
2002-10-14
revised
2002-11-11
accepted
2003-02-25
Contributors
author
  • Department of Animal Physiology, Zoological Institute, University of Wrocław, Z. Cybulskiego 30, 50-205 Wrocław, Poland
  • Department of Animal Physiology, Zoological Institute, University of Wrocław, Z. Cybulskiego 30, 50-205 Wrocław, Poland
  • Department of Animal Physiology, Zoological Institute, University of Wrocław, Z. Cybulskiego 30, 50-205 Wrocław, Poland
References
  • Al-Robaiy S, Eschrich K. (1999) Rat muscle fructose-1,6-bisphosphatase: cloning of the cDNA, expression of the recombinant enzyme, and expression analysis in different tissues. Biol Chem.; 380: 1079-85.
  • Blom N, Gammeltoft S, Brunak S. (1999) Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol.; 294: 1351-62.
  • Corbin JD, Reimann EM. (1974) Assay of cyclic AMP-dependent protein kinases. Meth Enzymol.; 38: 287-9.
  • Ekdahl K. (1987) Rat liver fructose-1,6-bisphosphatase. Identification of serine 338 as a third major phosphorylation site for cyclic AMP-dependent protein kinase and activity changes associated with multisite phosphorylation in vitro. J Biol Chem.; 262: 16699-703.
  • Ekdahl K. (1988) In vitro phosphorylation of fructose-1,6-bisphosphatase from rabbit and pig liver with cyclic AMP-dependent protein kinase. Arch Biochem Biophys.; 262: 27-31.
  • Gleeson TT. (1996) Post-exercise lactate metabolism: a comparative review of sites, pathways, and regulation. Annu Rev Physiol.; 58: 565-81.
  • Guex N, Peitsch MC. (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling. Electrophoresis.; 18: 2714-23.
  • Guex N, Diemand A, Peitsch MC. (1999) Protein modelling for all. Trends Biochem Sci.; 24: 364-7.
  • Laemmli UK. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature.; 227: 680-5.
  • Leatherbarrow RJ. (1992) GraFit 3.0. Erithacus Software, Staines, U.K.
  • Mizunuma H, Tashima Y. (1978) Fructose-1,6-bisphosphatase of the small intestine. Purification and comparison with liver and muscle fructose-1,6-bisphosphatases. J Biochem (Tokyo).; 84: 327-36.
  • Peitsch MC. (1995) Protein modelling by E-Mail. Bio/Technology.; 13: 658-60.
  • Pilkis SJ, El-Maghrabi MR, McGrane MM, Pilkis J, Claus TH. (1981) The role of fructose 2,6-bisphosphate in regulation of fructose-1,6-bisphosphatase. J Biol Chem.; 256: 3619-22.
  • Rakus D, Dzugaj A. (2000) Muscle aldolase decreases muscle FBPase sensitivity toward AMP inhibition. Biochem Biophys Res Commun.; 275: 611-6.
  • Rakus D, Skalecki K, Dzugaj A. (2000) Kinetic properties of pig (Sus scrofa domestica) and bovine (Bos taurus) D-fructose-1,6-bisphosphate 1-phosphohydrolase (F1,6BPase). Liver-like isoenzymes in mammalian lung tissue. Comp Biochem Physiol B Biochem Mol Biol.; 127: 123-34.
  • Rousseau GG, Hue L. (1993) Mammalian 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: a bifunctional enzyme that controls glycolysis. Prog Nucleic Acid Res Mol Biol.; 45: 99-127.
  • Ryan C, Radziuk J. (1995) Distinguishable substrate pools for muscle glyconeogenesis in lactate-supplemented recovery from exercise. Am J Physiol.; 269: E538-50.
  • Skalecki K, Mularczyk W, Dzugaj A. (1995) Kinetic properties of D-fructose-1,6-bisphosphate-1-phosphohydrolase isolated from human muscle. Biochem J.; 310: 1029-35.
  • Tejwani GA. (1983) Regulation of fructose-bisphosphatase activity. Adv Enzymol Relat Areas Mol Biol.; 54: 121-94.
  • Van Schaftingen E, Hers HG. (1981) Control of liver 6-phosphofructokinase by fructose 2,6-bisphosphate and other effectors. Proc Natl Acad Sci U S A.; 78: 2861-3.
  • Vidal H, Roux B, Riou JP. (1986) Phosphorylation- and ligand-induced conformational changes of rat liver fructose-1,6-bisphosphatase. Arch Biochem Biophys.; 248: 604-11.
Document Type
Publication order reference
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YADDA identifier
bwmeta1.element.bwnjournal-article-abpv50i1p115kz
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