title: A specific alkaline phosphatase from Saccharomyces cerevisiae with protein phosphatase activity.
abstract: 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.
authors.affiliation: Department of Microbial Biochemistry and Biosynthesis, Bulgarian Academy of Sciences, Sofia, Bulgaria.
authors.forename: B
authors.initials: B
authors.lastname: Tuleva
authors.forename: E
authors.initials: E
authors.lastname: Vasileva-Tonkova
authors.forename: D
authors.initials: D
authors.lastname: Galabova
mesh_terms: 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
chemical_list: D029701:Saccharomyces cerevisiae Proteins; C000602301:Pho13 protein, S cerevisiae; D000469:Alkaline Phosphatase; D010749:Phosphoprotein Phosphatases; D010744:Phosphoric Monoester Hydrolases