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- Title
The putative effector-binding site of Leishmania mexicana pyruvate kinase studied by site-directed mutagenesis
- Authors
Hannaert, Véronique; Yernaux, Cédric; Rigden, Daniel J.; Fothergill-Gilmore, Linda A.; Opperdoes, Fred R.; Michels, Paul A.M.
- Abstract
The activity of pyruvate kinase of Leishmania mexicana is allosterically regulated by fructose 2,6-bisphosphate (F-2,6-P2), contrary to the pyruvate kinases from other eukaryotes that are usually stimulated by fructose 1,6-bisphosphate (F-1,6-P2). Based on the comparison of the three-dimensional structure of Saccharomyces cerevisiae pyruvate kinase crystallized with F-1,6-P2 present at the effector site (R-state) and the L. mexicana enzyme crystallized in the T-state, two residues (Lys453 and His480) were proposed to bind the 2-phospho group of the effector. This hypothesis was tested by site-directed mutagenesis. The allosteric activation by F-2,6-P2 appeared to be entirely abrogated in the mutated enzymes confirming our predictions.
- Subjects
PYRUVATE kinase; LEISHMANIA; EUKARYOTIC cells
- Publication
FEBS Letters, 2002, Vol 514, Issue 2/3, p255
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(02)02374-8