title: Fructose 2,6 bisphosphate promotes the monomer-tetramer conservation of Leishmania mexicana amazonensis pyruvate kinase type two.
abstract: The enzyme pyruvate kinase of Leishmania mexicana amazonensis presents two forms with different kinetic properties and behavior for the heterotrophic activator fructose 2,6 bisphosphate. Pyruvate kinase 1, which is isolated as a tetramer, is inhibited by this metabolite. The second activity, Pyruvate kinase 2, is activated by fructose 2,6 bisphosphate, which promotes the monomer-tetramer conversion of this enzyme.
authors.affiliation: Instituto de Medicina Experimental, Facultad de Medicina, Universidad Central de Venezuela, Caracas.
authors.forename: A
authors.initials: A
authors.lastname: Ponte-Sucre
authors.forename: J L
authors.initials: JL
authors.lastname: Ramirez
mesh_terms: D000818:Animals; D005635:Fructosediphosphates / Q000378:metabolism*; D007700:Kinetics; D007894:Leishmania mexicana / Q000201:enzymology*; D008970:Molecular Weight; D011770:Pyruvate Kinase / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D005635:Fructosediphosphates; C027652:fructose 2,6-diphosphate; D011770:Pyruvate Kinase