title: The purification and kinetic characterization of eel white muscle pyruvate kinase.
abstract: A stable, homogeneous preparation of pyruvate kinase from white muscle of the American eel, Anguilla rostrata with a specific activity of 350 units/mg has been obtained. The enzyme has a pH optimum in the range 6.3-6.5 and requires Mg2+ and K+ for maximum activity. Eel muscle pyruvate kinase exhibits slight co-operativity in the binding of the substrate phosphoenol-pyruvate. It is activated by fructose-1,6-bisphosphate in a pH dependent manner and is inhibited by both alanine and phenylalanine. These properties are very similar to the properties of the mammalian M2 isozyme.
mesh_terms: D000811:Anguilla / Q000378:metabolism*; D000818:Animals; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D010649:Phenylalanine / Q000494:pharmacology; D010728:Phosphoenolpyruvate; D011770:Pyruvate Kinase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D010649:Phenylalanine; D010728:Phosphoenolpyruvate; D011770:Pyruvate Kinase