Biochemical and genetic evidence that yeast extracellular protein phosphatase activity is due to acid phosphatase.
In this paper evidences are presented strongly confirming that an extracellular 32P-phosphopeptide phosphatase activity of yeast is accounted for by acid phosphatase. Dephosphorylation of 32P phosphoseryl peptides was achieved with whole yeast cells, thus demonstrating extracellular location of protein phosphatase activity. The acid phosphatase and protein phosphatase activity copurified throughout purification procedure. Purified enzyme showed the same pH-profile and had the same Km value with phosphopeptide substrate as intact cells. Protein phosphatase activity is repressed by phosphate in the same manner as acid phosphatase activity, showing that not only repressible but also constitutive acid phosphatase displays protein phosphatase activity. Using mutant strains defective in acid phosphatase activity it was confirmed that acid phosphatase and protein phosphatase activities are the products of the same gene(s).
Lopandic
K
K
Istituto di Chimica Biologica, Università di Padova, Italy.
Deana
A D
AD
Barbaric
S
S
Pinna
L A
LA
D000135:Acid Phosphatase / Q000235:genetics / Q000302:isolation & purification*; D003470:Culture Media; D009154:Mutation; D010749:Phosphoprotein Phosphatases / Q000235:genetics / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics
D003470:Culture Media; D010749:Phosphoprotein Phosphatases; D000135:Acid Phosphatase