User menu

The putative effector-binding site of Leishmania mexicana pyruvate kinase studied by site-directed mutagenesis.

Bibliographic reference Hannaert, Véronique ; Yernaux, Cédric ; Rigden, Daniel J ; Fothergill-Gilmore, Linda A. ; Opperdoes, Frederik ; et. al. The putative effector-binding site of Leishmania mexicana pyruvate kinase studied by site-directed mutagenesis.. In: FEBS letters, Vol. 514, no. 2-3, p. 255-9 (2002)
Permanent URL
  1. 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
  2. Nwagwu, Acta Trop., 39, 61 (1982)
  3. Cronin C N, Tipton K F, The roles of magnesium ions in the reaction catalysed by phosphofructokinase fromTrypanosoma brucei, 10.1042/bj2470041
  4. SCHAFTINGEN Emile, OPPERDOES Fred. R., HERS Henri-Gery, Stimulation of Trypanosoma brucei pyruvate kinase by fructose 2,6-bisphosphate, 10.1111/j.1432-1033.1985.tb09316.x
  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 Isabelle, Callens Mia, Opperdoes Fred R., Michels Paul A.M., Pyruvate kinase of Leishmania mexicana mexicana Cloning and analysis of the gene, overexpression in Escherichia coli and characterization of the enzyme, 10.1016/0166-6851(94)90133-3
  7. ALLERT Sylvie, ERNEST Isabelle, POLISZCZAK Annick, OPPERDOES Fred R., MICHELS Paul A. M., Molecular cloning and analysis of two tandemly linked genes for pyruvate kinase of Trypanosoma brucei, 10.1111/j.1432-1033.1991.tb21043.x
  8. Callens Mia, Opperdoes Fred R., Some kinetic properties of pyruvate kinase from Trypanosoma brucei, 10.1016/0166-6851(92)90220-e
  9. Ernest I., Opperdoes F.R., Michels P.A.M., Cloning and Sequence Analysis of the Gene Encoding Pyruvate Kinase in Trypanoplasma borelli, 10.1006/bbrc.1994.1761
  10. 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
  11. Rigden Daniel J, Phillips Simon E.V, Michels Paul A.M, Fothergill-Gilmore Linda A, The structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity 1 1Edited by I. A. Wilson, 10.1006/jmbi.1999.2918
  12. Larsen Todd M., Laughlin L. Timothy, Holden Hazel M., Rayment Ivan, Reed George H., Structure of Rabbit Muscle Pyruvate Kinase Complexed with Mn2+, K+, and Pyruvate, 10.1021/bi00186a033
  13. Mattevi Andrea, Valentini Giovanna, Rizzi Menico, Speranza M.Luisa, Bolognesi Martino, Coda Alessandro, Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition, 10.1016/s0969-2126(01)00207-6
  14. Jurica Melissa S, Mesecar Andrew, Heath Patrick J, Shi Wuxian, Nowak Thomas, Stoddard Barry L, The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate, 10.1016/s0969-2126(98)00021-5
  15. Mikaelian Ivan, Sergeant Alain, A general and fast method to generate multiple site directed mutations, 10.1093/nar/20.2.376
  16. William Studier F., Rosenberg Alan H., Dunn John J., Dubendorff John W., [6] Use of T7 RNA polymerase to direct expression of cloned genes, Methods in Enzymology (1990) ISBN:9780121820862 p.60-89, 10.1016/0076-6879(90)85008-c
  17. Bradford Marion M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, 10.1016/0003-2697(76)90527-3
  18. LAEMMLI U. K., Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4, 10.1038/227680a0
  19. Claustre Samantha, Bringaud Frédéric, Azéma Laurent, Baron Rudi, Périé Jacques, Willson Michèle, An easy stereospecific synthesis of 1-amino-2,5-anhydro-1-deoxy-d-mannitol and arylamino derivatives, 10.1016/s0008-6215(99)00040-3
  20. Verlinde Christophe L.M.J., Hannaert Véronique, Blonski Casimir, Willson Michèle, Périé Jacques J., Fothergill-Gilmore Linda A., Opperdoes Fred R., Gelb Michael H., Hol Wim G.J., Michels Paul A.M., Glycolysis as a target for the design of new anti-trypanosome drugs, 10.1054/drup.2000.0177
  21. Kraulis P. J., MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, 10.1107/s0021889891004399
  22. Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard M., Improved methods for building protein models in electron density maps and the location of errors in these models, 10.1107/s0108767390010224