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HORT640 - Metabolic Plant Physiology
References, fructose-2,6-bisphosphatase
Bazan JF, Fletterick RJ, Pilkis SJ. Evolution of a bifunctional enzyme: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Proc. Natl. Acad. Sci. U.S.A. 86: 9642-9646 (1989).
Bertrand L, Vertommen D, Depiereux E, Hue L, Rider MH, Feytmans E. Modelling the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase on adenylate kinase. Biochem. J. 321: 615-621 (1997).
Boada J, Roig T, Perez X, Gamez A, Bartrons R, Cascante M, Bermudez J. Cells overexpressing fructose-2,6-bisphosphatase showed enhanced pentose phosphate pathway flux and resistance to oxidative stress. FEBS Lett. 480: 261-264 (2000).
Boles E, Gohlmann HW, Zimmermann FK. Cloning of a second gene encoding 5-phosphofructo-2-kinase in yeast, and characterization of mutant strains without fructose-2,6-bisphosphate. Mol. Microbiol. 20: 65-76 (1996).
Bourgis F, Botha FC, Mani S, Hiten FN, Rigden DJ, Verbruggen N. Characterization and functional investigation of an Arabidopsis cDNA encoding a homologue to the d-PGMase superfamily. J. Exp. Bot. 56: 1129-1142 (2005).
Choi IY, Wu C, Okar DA, Lange AJ, Gruetter R. Elucidation of the role of fructose 2,6-bisphosphate in the regulation of glucose fluxes in mice using in vivo (13)C NMR measurements of hepatic carbohydrate metabolism. Eur. J. Biochem. 269: 4418-4426 (2002).
Draborg H, Villadsen D, Nielsen TH. Cloning, characterization and expression of a bifunctional fructose-6-phosphate, 2-kinase/fructose-2,6-bisphosphatase from potato. Plant Mol. Biol. 39: 709-720 (1999).
Draborg H, Villadsen D, Nielsen TH. Transgenic Arabidopsis plants with decreased activity of fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase have altered carbon partitioning. Plant Physiol. 126: 750-758 (2001).
Dupriez VJ, Rousseau GG. Glucose response elements in a gene that codes for 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. DNA Cell Biol. 16: 1075-1085 (1997).
Durante P, Gueuning MA, Darville MI, Hue L, Rousseau GG. Apoptosis induced by growth factor withdrawal in fibroblasts overproducing fructose 2,6-bisphosphate. FEBS Lett. 448: 239-243 (1999).
Fernie AR, Roscher A, Ratcliffe RG, Kruger NJ. Activation of pyrophosphate:fructose-6-phosphate 1-phosphotransferase by fructose 2,6-bisphosphate stimulates conversion of hexose phosphates to triose phosphates but does not influence accumulation of carbohydrates in phosphate-deficient tobacco cells. Physiol. Plant. 114: 172-181 (2002).
Fernie AR, Roscher A, Ratcliffe RG, Kruger NJ. Fructose 2,6-bisphosphate activates pyrophosphate: fructose-6-phosphate 1-phosphotransferase and increases triose phosphate to hexose phosphate cycling in heterotrophic cells. Planta 212: 250-263 (2001).
Hansson O, Donsmark M, Ling C, Nevsten P, Danfelter M, Andersen JL, Galbo H, Holm C. Transcriptome and proteome analysis of soleus muscle of hormone-sensitive lipase-null mice. J. Lipid Res. 46: 2614-2623 (2005).
Harthill JE, Meek SE, Morrice N, Peggie MW, Borch J, Wong BH, Mackintosh C. Phosphorylation and 14-3-3 binding of Arabidopsis trehalose-phosphate synthase 5 in response to 2-deoxyglucose. Plant J. 47: 211-223 (2006).
Hasemann CA, Istvan ES, Uyeda K, Deisenhofer J. The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies. Structure 4: 1017-1029 (1996).
Hofmann E, Bedri A, Kessler R, Kretschmer M, Schellenberger W. 6-Phosphofructo-2-kinase and fructose-2,6-bisphosphatase from Saccharomyces cerevisiae. Adv. Enzyme Reg. 28: 283-306 (1989).
Kretschmer M, Langer C, Prinz W. Mutation of monofunctional 6-phosphofructo-2-kinase in yeast to bifunctional 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase. Biochemistry 32: 11143-11148 (1993).
Kulma A, Villadsen D, Campbell DG, Meek SE, Harthill JE, Nielsen TH, MacKintosh C. Phosphorylation and 14-3-3 binding of Arabidopsis 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Plant J. 37: 654-667 (2004).
Li L, Lin K, Correia JJ, Pilkis SJ. Lysine 356 is a critical residue for binding the C-6 phospho group of fructose 2,6-bisphosphate to the fructose-2,6-bisphosphatase domain of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. J. Biol. Chem. 267: 16669-16675 (1992).
Li L, Ling S, Wu Cl, Yao W, Xu G. Separate bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: the role of the C-terminal tail in modulating enzyme activity. Biochem. J. 328: 751-756 (1997).
Macdonald FD, Chou Q, Buchanan BB. Ion-exchange chromatography separates activities synthesizing and degrading fructose 2,6-bisphosphate from C3 and C4 leaves but not from rat liver. Plant Physiol. 85: 13-16 (1987).
Markham JE, Kruger NJ. Kinetic properties of bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase from spinach leaves. Eur. J. Biochem. 269: 1267-1277 (2002).
Minchenko A, Leshchinsky I, Opentanova I, Sang N, Srinivas V, Armstead V, Caro J. Hypoxia-inducible factor-1-mediated expression of the 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3) gene. Its possible role in the Warburg effect. J. Biol. Chem. 277: 6183-6187 (2002).
Okar DA, Lange AJ. Fructose-2,6-bisphosphate and control of carbohydrate metabolism in eukaryotes. Biofactors 10: 1-14 (1999).
Perez JX, Roig T, Manzano A, Dalmau M, Boada J, Ventura F, Rosa JL, Bermudez J, Bartrons R. Overexpression of fructose 2,6-bisphosphatase decreases glycolysis and delays cell cycle progression. Am. J. Physiol. Cell Physiol. 279: C1359-C1365 (2000).
Pilkis SJ, Claus TH, Kurland IJ, Lange AJ. 6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase: a metabolic signaling enzyme. Annu. Rev. Biochem. 64: 799-835 (1995).
Rung JH, Draborg HH, Jorgensen K, Nielsen TH. Carbon partitioning in leaves and tubers of transgenic potato plants with reduced activity of fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase. Physiol. Plant. 121: 204-214 (2004).
Scott P, Lange AJ, Kruger NJ. Photosynthetic carbon metabolism in leaves of transgenic tobacco (Nicotiana tabacum L.) containing decreased amounts of fructose 2,6-bisphosphate. Planta 211: 864-873 (2000).
Tauler A, el-Maghrabi MR, Pilkis SJ. Functional homology of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphoglycerate mutase, and 2,3-bisphosphoglycerate mutase. J. Biol. Chem. 262: 16808-16815 (1987).
Tauler A, Rosenberg AH, Colosia A, Studier FW, Pilkis SJ. Expression of the bisphosphatase domain of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 85: 6642-6646 (1988).
Yuen MH, Mizuguchi H, Lee YH, Cook PF, Uyeda K, Hasemann CA. Crystal structure of the H256A mutant of rat testis fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase. Fructose 6-phosphate in the active site leads to mechanisms for both mutant and wild type bisphosphatase activities. J. Biol. Chem. 274: 2176-2184 (1999).
Number of references = 31
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