title: Acylphosphatase possesses nucleoside triphosphatase and nucleoside diphosphatase activities.
abstract: We have demonstrated that acylphosphatase possesses ATP-diphosphohydrolase (apyrase-like) activity. In fact, acylphosphatase first catalyses the hydrolysis of the gamma-phosphate group of nucleoside triphosphates, and then attacks the beta-phosphate group of the initially produced nucleoside diphosphates, generating nucleoside monophosphates. In contrast, it binds nucleoside monophosphates but does not catalyse their hydrolyses. The calculated k(cat) values for the nucleoside triphosphatase activity of acylphosphatase are of the same order of magnitude as those displayed by certain G-proteins. An acidic environment enhances the apyrase-like activity of acylphosphatase. The true nucleotide substrates of acylphosphatase are free nucleoside di- and triphosphates, as indicated by the Mg(2+) ion inhibition of the activity. We have also demonstrated that, although nucleoside triphosphates are still hydrolysed at pH 7.2 and 37 degrees C, in the presence of millimolar Mg(2+) concentrations this occurs at a lower rate. Taken together with the previously observed strong increase of acylphosphatase levels during induced cell differentiation, our findings suggest that acylphosphatase plays an active role in the differentiation process (as well as in other processes, such as apoptosis) by modulating the ratio between the cellular levels of nucleoside diphosphates and nucleoside triphosphates.
authors.affiliation: Dipartimento di Scienze Biochimiche, Università di Firenze, Viale Morgagni 50, 50134 Firenze, Italy.
authors.forename: P
authors.initials: P
authors.lastname: Paoli
authors.forename: G
authors.initials: G
authors.lastname: Camici
authors.forename: G
authors.initials: G
authors.lastname: Manao
authors.forename: E
authors.initials: E
authors.lastname: Giannoni
authors.forename: G
authors.initials: G
authors.lastname: Ramponi
mesh_terms: D017766:Acid Anhydride Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000378:metabolism; D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007477:Ions; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D016296:Mutagenesis; D009154:Mutation; D043583:Nucleoside-Triphosphatase; D010710:Phosphates / Q000378:metabolism; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism; D000097024:Acylphosphatase
chemical_list: D017766:Acid Anhydride Hydrolases; D000244:Adenosine Diphosphate; D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D007477:Ions; D008274:Magnesium; D043583:Nucleoside-Triphosphatase; D010710:Phosphates; D011994:Recombinant Proteins; D000097024:Acylphosphatase; C023837:nucleoside-diphosphatase