The putative effector-binding site of Leishmania mexicana pyruvate kinase studied by site-directed mutagenesis.
(2002) FEBS Letters — Vol. 514, n° 2-3, p. 255-259 (2002)
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- Abstract
- The activity of pyruvate kinase of Leishmania mexicana is allosterically regulated by fructose 2,6-bisphosphate (F-2,6-P(2)), contrary to the pyruvate kinases from other eukaryotes that are usually stimulated by fructose 1,6-bisphosphate (F-1,6-P(2)). Based on the comparison of the three-dimensional structure of Saccharomyces cerevisiae pyruvate kinase crystallized with F-1,6-P(2) 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-P(2) appeared to be entirely abrogated in the mutated enzymes confirming our predictions.
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Hannaert, V., Yernaux, C., Rigden, D. J., Fothergill-Gilmore, L. A., Opperdoes, F., & Michels, P. (2002). The putative effector-binding site of Leishmania mexicana pyruvate kinase studied by site-directed mutagenesis. FEBS Letters, 514(2-3), 255-259. https://doi.org/10.1016/S0014-5793(02)02374-8 (Original work published 2002)