Repressible acid phosphatase from yeast efficiently dephosphorylates in vitro some phosphorylated proteins and peptides.
Highly purified repressible acid phosphatase from Saccharomyces cerevisiae very efficiently dephosphorylates 32P-histones and the phosphopeptides Arg-Arg-Ala-Ser-(32P)-Val-Ala and Arg-Arg-Leu-Ser (32P)-Leu-Arg previously phosphorylated by either cAMP-dependent protein kinase or protein kinase-C. The Km values (0.03-1 microM) are very favourable if compared with those calculated for free phosphoaminoacids and p-nitrophenylphosphate which are three to six orders of magnitude higher. While also the phosphopeptide Asp-Ala-Gly-Tyr(32P)-Ala-Arg3-Gly is readily dephosphorylated, other phosphopeptides and phosphoproteins including phosphorylase kinase, phosvitin and casein phosphorylated by both casein kinase 1 and 2 are not appreciably affected by acid phosphatase. It is suggested that yeast repressible acid phosphatase may act in vivo as a phosphoprotein phosphatase.
D000135:Acid Phosphatase / Q000378:metabolism*; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000378:metabolism; D007700:Kinetics; D010748:Phosphopeptides / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D007527:Isoenzymes; D010748:Phosphopeptides; D010750:Phosphoproteins; D000135:Acid Phosphatase