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polyphosphatase PPN1 of Saccharomyces cerevisiae Is a Deoxyadenosine Triphosphate Phosphohydrolase

Advances in Enzyme Research 2016年第4期4卷 144-151页

作者： Nadezhda Andreeva Ludmila Trilisenko Mikhail Eldarov Tatiana Kulakovskaya Skryabin Institute of Biochemistry and Physiology of Microorganisms Russian Academy of Sciences Pushchino Russia Institute of Bioengineering Centre of Biotechnology Russian Academy of Sciences Moscow Russia

The Saccharomyces cerevisiae polyphosphatase PPN1 (uniprot/Q04119) degrades inorganic polyphosphates both by cleaving Pi from the chain end and by fragmenting long-chain polymers into shorter ones. In this study, we have found a new activity of this protein: it releases phosphate from dATP. The dATP phosphohydrolase activity of pure PPN1 was ~7-fold lower compared to the exopolyphosphatase activity. This activity was strongly stimulated by Co2+ ions, as well as by ammonium ions, and inhibited by heparin and pyrophosphate similar to the exopolyphosphatase activity of PPN1. The Km value for dATP was 0.88 ± 0.14 mM. The dATP phosphohydrolase activity in the cells of PPN1-overexpressing yeast strain was several-fold higher than that in the parent strain. The other exopolyphosphatase of S. cerevisiae, PPX1, did not split Pi from dATP.

关键词： Polyphosphate Yeast PPN1 polyphosphatase Deoxyadenosine Triphosphate Phos-phohydrolase dATP

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polyphosphatase PPX1 of <i>Saccharomyces cerevisiae</i>as a Tool for Polyphosphate Assay

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Advances in Enzyme Research 2015年第4期3卷 93-100页

作者： Lidiya Lichko Tatiana Kulakovskaya Skryabin Institute of Biochemistry and Physiology of Microorganisms Russian Academy of Sciences Pushchino Russia

The recombinant exopolyphosphatase PPX1 with a specific activity of ~300 U/mg protein was purified from the strain of Saccharomyces cerevisiae with the inactivated PPN1 gene transformed by the expression vector carrying the yeast PPX1 gene. The recombinant PPX1 was similar to the PPX1 of wild strains in its substrate specificity and requirement for cations. PPX1 had the high substrate specificity to polyphosphates. The preparation was suitable for polyphosphate assay in the presence of orthophosphate and nucleoside phosphates not hydrolyzed by PPX1. The yield of the enzyme preparation was 250 assays per 1 g of the biomass. The recombinant PPX1 was successfully used in polyphosphate assay in different yeast species and some foodstuffs.

关键词： Saccharomyces cerevisiae PPX1 Polyphosphate polyphosphatase Assay Food

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