A specific alkaline phosphatase from Saccharomyces cerevisiae with protein phosphatase activity.
In this paper, specific PHO13 alkaline phosphatase from Saccharomyces cerevisiae was demonstrated to possess phosphoprotein phosphatase activity on the phosphoseryl proteins histone II-A and casein. The enzyme is a monomeric protein with molecular mass of 60 kDa and hydrolyzes p-nitrophenyl phosphate with maximal activity at pH 8.2 with strong dependence on Mg2+ ions and an apparent Km of 3.6 x 10(-5) M. No other substrates tested except phosphorylated histone II-A and casein were hydrolyzed at any significant rate. These data suggest that the physiological role of the p-nitrophenyl phosphate-specific phosphatase may involve participation in reversible protein phosphorylation. 1988 Federation of European Microbiological Societies.
Tuleva
B
B
Department of Microbial Biochemistry and Biosynthesis, Bulgarian Academy of Sciences, Sofia, Bulgaria.
Vasileva-Tonkova
E
E
Galabova
D
D
D000469:Alkaline Phosphatase / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D013379:Substrate Specificity
D029701:Saccharomyces cerevisiae Proteins; C000602301:Pho13 protein, S cerevisiae; D000469:Alkaline Phosphatase; D010749:Phosphoprotein Phosphatases; D010744:Phosphoric Monoester Hydrolases