Ponte-Sucre A, Ramirez J L
Instituto de Medicina Experimental, Facultad de Medicina, Universidad Central de Venezuela, Caracas.
Biol Res. 1993;26(1-2):131-4.
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.
亚马逊利什曼原虫的丙酮酸激酶呈现出两种形式，它们对异养激活剂果糖2,6-二磷酸具有不同的动力学特性和行为。作为四聚体分离出来的丙酮酸激酶1被这种代谢物抑制。第二种活性，即丙酮酸激酶2，被果糖2,6-二磷酸激活，果糖2,6-二磷酸促进该酶的单体-四聚体转化。
