CLONING AND SEQUENCE-ANALYSIS OF THE GENE ENCODING PYRUVATE-KINASE IN TRYPANOPLASMA-BORELLI

The gene coding for pyruvate kinase in Trypanoplasma borelli has been cloned and characterized. A single gene copy was found with an open reading frame for a polypeptide of 496 amino acids and a molecular mass of 54337. The deduced amino acid sequence has a calculated net charge of -3. Comparison of the sequence with those of pyruvate kinases from members of the family Trypanosomatidae revealed amino acid identities of 58.4-61.5%, and, to some extent, conservation of residues supposed to be involved in the binding of the allosteric effector fructose 2,6-bisphosphate. Some kinetic properties of Trypanoplasma borelli pyruvate kinase have been determined and appear to be similar to those of the enzyme from Trypanosoma brucei and Leishmania mexicana. (C) 1994 Academic Press, Inc.