title: Purification and characterization of a type 2A protein phosphatase from Yarrowia lipolytica grown on a phosphate-deficient medium.
abstract: Intracellular protein phosphatase activity has been identified in the yeast Yarrowia lipolytica. This activity was maximal early in its exponential growth phase, and it was enhanced by Pi-deficiency of the culture medium. On a Pi-deficient medium, the major protein phosphatase was purified. This enzyme was dissociated with 80% ethanol treatment, its activity was slightly increased (30%) with heparine and largely enhanced (1.5 to 3-fold) with polycations. This enzyme could be classified as a type 2A protein phosphatase. It is composed of a catalytic subunit and other subunits. Its optimum pH value is 7.2, the apparent Km for casein is 37 microM and the apparent velocity 3.6 pmol hydrolyzed32 Pi min-1 pmol-1 enzyme.
authors.affiliation: Laboratoire de chimie biologique, Inra, Ina-PG, Centre de biotechnologies agro-industrielles, Thiverval-Grignon, France.
authors.forename: P
authors.initials: P
authors.lastname: Jolivet
authors.forename: C
authors.initials: C
authors.lastname: Queiroz-Claret
authors.forename: E
authors.initials: E
authors.lastname: Bergeron
authors.forename: J C
authors.initials: JC
authors.lastname: Meunier
mesh_terms: D002384:Catalysis; D003470:Culture Media; D010710:Phosphates / Q000172:deficiency; D010749:Phosphoprotein Phosphatases / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology*; D015003:Yeasts / Q000201:enzymology* / Q000254:growth & development
chemical_list: D003470:Culture Media; D010710:Phosphates; D010749:Phosphoprotein Phosphatases