Characterization of major protein phosphatases from selected species of Kluyveromyces. Comparison with protein phosphatases from Yarrowia lipolytica.
Casein phosphatase activities have been identified in five yeast strains grown on Pi-deficient medium. Maximal endocellular activities appeared in the exponential phase. Exocellular phosphatases were significantly produced from Yarrowia lipolytica W-29 and Kluyveromyces marxianus, in the early stationary phase. Major phosphatases from K. marxianus were one heavy acid phosphatase composed of 64-67 kDa subunits, which could be secreted in the medium, and one type 2A protein phosphatase with an apparent molecular mass of 147 kDa and a 52 kDa catalytic subunit dissociated by 80% ethanol treatment. The characteristics of phosphatases purified from K. marxianus were compared with those previously purified from Y. lipolytica.
Jolivet
P
P
Institut national de la recherche agronomique, Institut national agronomique Paris-Grignon, Centre de Biotechnologie Agro-Industrielle, Thiverval-Grignon, France. jolivet@grignon.inra.fr
Bergeron
E
E
Benyair
H
H
Meunier
J C
JC
D003470:Culture Media; D007716:Kluyveromyces / Q000201:enzymology*; D008970:Molecular Weight; D010710:Phosphates; D010749:Phosphoprotein Phosphatases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D025062:Yarrowia / Q000201:enzymology*
D003470:Culture Media; D010710:Phosphates; D010749:Phosphoprotein Phosphatases