title: Purification and properties of pyruvate kinase from Dictyostelium discoideum.
abstract: Pyruvate kinase (EC 2.7.1.40) from aggregating Dictyostelium discoideum cells has been purified to homogeneity. It has a monomeric molecular weight of 66kD and is tetrameric in low ionic strength buffers. The enzyme is not regulated by fructose 1,6-bisphosphate or by alanine and appears to resemble the M1 isoenzyme from rat liver most closely, although its activity is not inhibited by ATP.
authors.affiliation: School of Biological Sciences, Flinders University Bedford Park, S.A., Australia.
authors.forename: J
authors.initials: J
authors.lastname: Marshall
authors.forename: J F
authors.initials: JF
authors.lastname: Wheldrake
mesh_terms: D004023:Dictyostelium / Q000201:enzymology* / Q000254:growth & development; D005635:Fructosediphosphates / Q000494:pharmacology; D007700:Kinetics; D008970:Molecular Weight; D011487:Protein Conformation; D011770:Pyruvate Kinase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D005635:Fructosediphosphates; D011770:Pyruvate Kinase; C029063:fructose-1,6-diphosphate