Purification and characterization of a type 2A protein phosphatase from Yarrowia lipolytica grown on a phosphate-deficient medium.
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.
Jolivet
P
P
Laboratoire de chimie biologique, Inra, Ina-PG, Centre de biotechnologies agro-industrielles, Thiverval-Grignon, France.
Queiroz-Claret
C
C
Bergeron
E
E
Meunier
J C
JC
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
D003470:Culture Media; D010710:Phosphates; D010749:Phosphoprotein Phosphatases