User menu

6-Phosphofructo-2-kinase and fructose-2,6-bisphosphatase in Trypanosomatidae. Molecular characterization, database searches, modelling studies and evolutionary analysis.

Bibliographic reference Chevalier, Nathalie ; Bertrand, Luc ; Rider, Mark ; Opperdoes, Frederik ; Rigden, Daniel J ; et. al. 6-Phosphofructo-2-kinase and fructose-2,6-bisphosphatase in Trypanosomatidae. Molecular characterization, database searches, modelling studies and evolutionary analysis.. In: The FEBS journal, Vol. 272, no. 14, p. 3542-60 (2005)
Permanent URL http://hdl.handle.net/2078.1/10252
  1. Rider MH, Biochem J, 381, 561 (2004)
  2. Pilkis S., Hormonal Regulation Of Hepatic Gluconeogenesis And Glycolysis, 10.1146/annurev.biochem.57.1.755
  3. Van Schaftingen E, Eur J Biochem, 153, 403 (1985)
  4. Van Schaftingen E, Eur J Biochem, 166, 653 (1987)
  5. Callens Mia, Kuntz Douglas A., Opperdoes Fred R., Characterization of pyruvate kinase of Trypanosoma brucei and its role in the regulation of carbohydrate metabolism, 10.1016/0166-6851(91)90144-u
  6. Ernest I, Mol Biochem Parasitol, 64, 43 (1994)
  7. Ernest Isabelle, Callens Mia, Uttaro Antonio D., Chevalier Nathalie, Opperdoes Fred R., Muirhead Hilary, Michels Paul A.M., Pyruvate Kinase ofTrypanosoma brucei:Overexpression, Purification, and Functional Characterization of Wild-Type and Mutated Enzyme, 10.1006/prep.1998.0918
  8. Hannaert V, FEBS Lett, 514, 255 (2002)
  9. Cazzulo JJ, FEMS Microbiol Lett, 59, 259 (1989)
  10. Opperdoes Fred R., Borst Piet, Localization of nine glycolytic enzymes in a microbody-like organelle inTrypanosoma brucei: The glycosome, 10.1016/0014-5793(77)80476-6
  11. Opperdoes F., Compartmentation Of Carbohydrate Metabolism In Trypanosomes, 10.1146/annurev.micro.41.1.127
  12. Michels P.A.M., Hannaert V., Bringaud F., Metabolic Aspects of Glycosomes in Trypanosomatidae – New Data and Views, 10.1016/s0169-4758(00)01810-x
  13. Fothergill-Gilmore Linda A., Michels Paul A.M., Evolution of glycolysis, 10.1016/0079-6107(93)90001-z
  14. Bakker BM, J Bioenerg Biomembr, 27, 513 (1995)
  15. Bakker B. M., Mensonides F. I. C., Teusink B., van Hoek P., Michels P. A. M., Westerhoff H. V., Compartmentation protects trypanosomes from the dangerous design of glycolysis, 10.1073/pnas.030539197
  16. Okar David A., Lange Alex J., Manzano Ànna, Navarro-Sabatè Aurèa, Riera Lluı̀s, Bartrons Ramon, PFK-2/FBPase-2: maker and breaker of the essential biofactor fructose-2,6-bisphosphate, 10.1016/s0968-0004(00)01699-6
  17. Pilkis S., 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase: A Metabolic Signaling Enzyme, 10.1146/annurev.biochem.64.1.799
  18. Villadsen Dorthe, Rung Jesper Henrik, Draborg Henriette, Nielsen Tom Hamborg, Structure and heterologous expression of a gene encoding fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase from Arabidopsis thaliana, 10.1016/s0167-4781(00)00134-2
  19. Kretschmer M, Biochemistry, 30, 10663 (1991)
  20. Paravicini G, Biochemistry, 31, 7126 (1992)
  21. Boles E, Mol Microbiol, 20, 65 (1996)
  22. Tauler A, Proc Natl Acad Sci USA, 86, 7316 (1989)
  23. Tauler A, Proc Natl Acad Sci USA, 85, 6642 (1988)
  24. Hasemann Charles A, Istvan Eva S, Uyeda Kosaku, Deisenhofer Johann, The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies, 10.1016/s0969-2126(96)00109-8
  25. Lee YH, J Biol Chem, 278, 523 (2003)
  26. BERTRAND Luc, VERTOMMEN Didier, DEPIEREUX Eric, HUE Louis, RIDER Mark H., FEYTMANS Ernest, Modelling the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase on adenylate kinase, 10.1042/bj3210615
  27. Hue L, Rider M H, Role of fructose 2,6-bisphosphate in the control of glycolysis in mammalian tissues, 10.1042/bj2450313
  28. FRANCOIS Jean, SCHAFTINGEN Emile, HERS Henri-Gery, Characterization of phosphofructokinase 2 and of enzymes involved in the degradation of fructose 2,6-bisphosphate in yeast, 10.1111/j.1432-1033.1988.tb13830.x
  29. KRETSCHMER Matthias, TEMPST Paul, FRAENKEL Dan G., Identification and cloning of yeast phosphofructokinase 2, 10.1111/j.1432-1033.1991.tb15920.x
  30. Dihazi Hassan, Kessler Renate, Eschrich Klaus, Phosphorylation and Inactivation of Yeast 6-Phosphofructo-2-kinase Contribute to the Regulation of Glycolysis under Hypotonic Stress†, 10.1021/bi0155549
  31. Rider M H, Foret D, Hue L, Comparison of purified bovine heart and rat liver 6-phosphofructo-2-kinase. Evidence for distinct isoenzymes, 10.1042/bj2310193
  32. Machado C. A., Ayala F. J., Nucleotide sequences provide evidence of genetic exchange among distantly related lineages of Trypanosoma cruzi, 10.1073/pnas.121187198
  33. Vertommen Didier, Bertrand Luc, Sontag Bruno, Di Pietro Attilio, Louckx Marc P., Vidal Hubert, Hue Louis, Rider Mark H., The ATP-binding Site in the 2-Kinase Domain of Liver 6-Phosphofructo-2-kinase/Fructose-2,6-bisphosphatase : STUDY OF THE ROLE OF Lys-54 AND Thr-55 BY SITE-DIRECTED MUTAGENESIS, 10.1074/jbc.271.30.17875
  34. Rider M H, Crepin K M, De Cloedt M, Bertrand L, Hue L, Site-directed mutagenesis of rat muscle 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: role of Asp-130 in the 2-kinase domain, 10.1042/bj3000111
  35. BERTRAND Luc, DEPREZ Johan, VERTOMMEN Didier, PIETRO Attilio DI, HUE Louis, RIDER Mark H., Site-directed mutagenesis of Lys-174, Asp-179 and Asp-191 in the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, 10.1042/bj3210623
  36. Tauler A, J Biol Chem, 265, 15617 (1990)
  37. Lin K, J Biol Chem, 267, 19163 (1992)
  38. Lin K, J Biol Chem, 267, 6556 (1992)
  39. Yuen Mi H., Mizuguchi Hiroyuki, Lee Yong-Hwan, Cook Paul F., Uyeda Kosaku, Hasemann Charles A., 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, 10.1074/jbc.274.4.2176
  40. Rider M H, Crepin K M, De Cloedt M, Bertrand L, Vertommen D, Hue L, Study of the roles of Arg-104 and Arg-225 in the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase by site-directed mutagenesis, 10.1042/bj3090341
  41. BERTRAND Luc, VERTOMMEN Didier, FEYTMANS Ernest, PIETRO Attilio Di, RIDER Mark H., HUE Louis, Mutagenesis of charged residues in a conserved sequence in the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, 10.1042/bj3210609
  42. Bertrand L, Eur J Biochem, 254, 490 (1998)
  43. Lee YH, Nat Struct Biol, 4, 615 (1997)
  44. Mizuguchi H, J Biol Chem, 274, 2166 (1999)
  45. Rigden Daniel J., Unexpected catalytic site variation in phosphoprotein phosphatase homologues of cofactor-dependent phosphoglycerate mutase, 10.1016/s0014-5793(03)00014-0
  46. Oza SL, Biochem J, 364, 679 (2002)
  47. VILLADSEN Dorthe, NIELSEN Tom H., N-terminal truncation affects the kinetics and structure of fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase from Arabidopsis thaliana, 10.1042/0264-6021:3590591
  48. Draborg Henriette, Villadsen Dorthe, Hamborg Nielsen Tom, 10.1023/a:1006102412693
  49. Muller S, Microbiology, 143, 3055 (1997)
  50. Oliver Stephen G., Raamsdonk Léonie M., Teusink Bas, Broadhurst David, Zhang Nianshu, Hayes Andrew, Walsh Michael C., Berden Jan A., Brindle Kevin M., Kell Douglas B., Rowland Jem J., Westerhoff Hans V., van Dam Karel, 10.1038/83496
  51. Neuberger G, J Mol Biol, 328, 567 (2003)
  52. El-Sayed Najib M.A., Alarcon Clara M., Beck John C., Sheffield Val C., Donelson John E., cDNA expressed sequence tags of Trypanosoma brucei rhodesiense provide new insights into the biology of the parasite, 10.1016/0166-6851(95)00098-l
  53. Huang J, EMBO J, 10, 3877 (1991)
  54. Clayton C. E., NEW EMBO MEMBER'S REVIEW Life without transcriptional control? From fly to man and back again, 10.1093/emboj/21.8.1881
  55. MAIR GUNNAR, SHI HUAFANG, LI HONGJIE, DJIKENG APPOLINAIRE, AVILES HERNAN O., BISHOP JOSEPH R., FALCONE FRANCO H., GAVRILESCU CRISTINA, MONTGOMERY JACQUI L., SANTORI M. ISABEL, STERN LEAH S., WANG ZEFENG, ULLU ELISABETTA, TSCHUDI CHRISTIAN, A new twist in trypanosome RNA metabolism: cis-splicing of pre-mRNA, 10.1017/s135583820099229x
  56. Mosavi L. K., Minor D. L., Peng Z.-y., Consensus-derived structural determinants of the ankyrin repeat motif, 10.1073/pnas.252537899
  57. Kohl A, Proc Natl Acad Sci USA, 100, 1700 (2003)
  58. Heger A, Proteins, 41, 224 (2000)
  59. Sedgwick Steven G, Smerdon Stephen J, The ankyrin repeat: a diversity of interactions on a common structural framework, 10.1016/s0968-0004(99)01426-7
  60. Massa L, Diabetes, 53, 1020 (2004)
  61. Muller Susanne, Boles Eckhard, Zimmermann Friedrich K., A Two-Hybrid System Analysis Shows Interactions Between 6-Phosphofructo-1-Kinase and 6-Phosphofructo-2-Kinase but not Between Other Glycolytic Enzymes of the Yeast Saccharomyces cerevisiae, 10.1111/j.1432-1033.1996.00626.x
  62. Pozuelo-Rubio M, EMBO J, 22, 3514 (2003)
  63. Kulma Anna, Villadsen Dorthe, Campbell David G., Meek Sarah E. M., E. Harthill Jean, Nielsen Tom H., MacKintosh Carol, Phosphorylation and 14-3-3 binding of Arabidopsis 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, 10.1111/j.1365-313x.2003.01992.x
  64. Opperdoes F. R., Purification, morphometric analysis, and characterization of the glycosomes (microbodies) of the protozoan hemoflagellate Trypanosoma brucei, 10.1083/jcb.98.4.1178
  65. Altschul S., Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, 10.1093/nar/25.17.3389
  66. Hertz-Fowler C., GeneDB: a resource for prokaryotic and eukaryotic organisms, 10.1093/nar/gkh007
  67. Luchtan M, Nucleic Acids Res, 32, D344 (2004)
  68. Gasteiger E., ExPASy: the proteomics server for in-depth protein knowledge and analysis, 10.1093/nar/gkg563
  69. Wheeler D. L., Database resources of the National Center for Biotechnology, 10.1093/nar/gkg033
  70. Marchler-Bauer A., CDD: a curated Entrez database of conserved domain alignments, 10.1093/nar/gkg087
  71. Ginalski K, Bioinformatics, 19, 1015 (2003)
  72. Rychlewski L, Proteins, 53, 542 (2003)
  73. Notredame Cédric, Higgins Desmond G, Heringa Jaap, T-coffee: a novel method for fast and accurate multiple sequence alignment 1 1Edited by J. Thornton, 10.1006/jmbi.2000.4042
  74. Edgar R. C., MUSCLE: multiple sequence alignment with high accuracy and high throughput, 10.1093/nar/gkh340
  75. Clamp M., Cuff J., Searle S. M., Barton G. J., The Jalview Java alignment editor, 10.1093/bioinformatics/btg430
  76. Šali Andrej, Blundell Tom L., Comparative Protein Modelling by Satisfaction of Spatial Restraints, 10.1006/jmbi.1993.1626
  77. May AC, Structure, 12, 737 (2004)
  78. Jones TA, Acta Crystallogr, 47, 110 (1991)
  79. Jones David T, Protein secondary structure prediction based on position-specific scoring matrices 1 1Edited by G. Von Heijne, 10.1006/jmbi.1999.3091
  80. Thompson J., The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools, 10.1093/nar/25.24.4876
  81. MICHELS Paul A. M., MARCHAND Martine, KOHL Linda, ALLERT Sylvie, WIERENGA Rik K., OPPERDOES Fred R., The cytosolic and glycosomal isoenzymes of glyceraldehyde-3-phosphate dehydrogenase in Trypanosoma brucei have a distant evolutionary relationship, 10.1111/j.1432-1033.1991.tb16031.x
  82. Sambrook JE, Molecular cloning: a laboratory manual. (1989)
  83. Bradford M, A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding, 10.1006/abio.1976.9999
  84. Laemmli UK, Nature, 227, 680 (1970)
  85. Towbin H, Proc Natl Acad Sci USA, 76, 4350 (1979)
  86. Crepin KM, J Biol Chem, 267, 21698 (1992)
  87. Rider M H, Hue L, Phosphorylation of purified bovine heart and rat liver 6-phosphofructo-2-kinase by protein kinase C and comparison of the fructose-2,6-bisphosphatase activity of the two enzymes, 10.1042/bj2400057
  88. Barton GJ, Prot Eng, 6, 37 (1993)