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Lonetti, A., Szijgyarto, Z., Bosch, D., Loss, O., Azevedo, C. and Saiardi, A. (2011) Identification of an Evolutionarily Conserved Family of Inorganic Polyphosphate Endopolyphosphatases. Journal of Biological Chemistry, 286, 31966-31974.
https://doi.org/10.1074/jbc.M111.266320

has been cited by the following article:

• TITLE: Polyphosphatase PPN1 of Saccharomyces cerevisiae Is a Deoxyadenosine Triphosphate Phosphohydrolase

  AUTHORS: Nadezhda Andreeva, Ludmila Trilisenko, Mikhail Eldarov, Tatiana Kulakovskaya

  KEYWORDS: Polyphosphate, Yeast, PPN1, Polyphosphatase, Deoxyadenosine Triphosphate Phos-phohydrolase, dATP

  JOURNAL NAME: Advances in Enzyme Research, Vol.4 No.4, December 6, 2016

  ABSTRACT: 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.