Fructose 2, 6 bisphosphate promotes the monomer-tetramer conservation of Leishmania mexicana amazonensis pyruvate kinase type two

Ponte-Sucre, Alicia; Ramirez, Jose L

Ponte-Sucre, Alicia; Ramirez, Jose L.

Ponte-Sucre, Alicia; Universidad Central de Venezuela. Instituto de Medicina Experimental.
Ramirez, Jose L; Universidad Central de Venezuela. Grupo de Genética Molecular.

Biol. Res ; 26(1/2): 131-4, 1993. graf

Article in English | LILACS | ID: lil-228599

RESUMO

RESUMO

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

Subject(s)

Animals; Fructosediphosphates/metabolism; Leishmania mexicana/enzymology; Pyruvate Kinase/metabolism; Kinetics; Molecular Weight; Pyruvate Kinase/isolation & purification

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Index: LILACS (Americas) Main subject: Pyruvate Kinase / Leishmania mexicana / Fructosediphosphates Limits: Animals Country/Region as subject: Mexico Language: English Journal: Biol. Res Journal subject: Biology Year: 1993 Type: Article

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