Abstract
The polyphosphatase PPN1 of Saccharomyces cerevisiae shows an exopolyphosphatase activity splitting phosphate from chain end and an endopolyphosphatase activity fragmenting high molecular inorganic polyphosphates into shorter polymers. We revealed the compounds switching these activities of PPN1. Phosphate release and fragmentation of high molecular polyphosphate prevailed in the presence of Co2+ and Mg2+, respectively. Phosphate release and polyphosphate chain shortening in the presence of Co2+ were inhibited by ADP but not affected by ATP and argininе. The polyphosphate chain shortening in the presence of Mg2+ was activated by ADP and arginine but inhibited by ATP.
Highlights
Inorganic polyphosphate (PolyP), the linear polymer containing a few to several hundred phosphate residues, performs many functions in living cells
The purified recombinant PPN1 was obtained from the cells of the strain CRN/pMB1_PPN1 Sc (Table 1)
The PPN1 gene encodes a polypeptide with the predicted molecular mass of 78 kDa, whereas the monomer molecular mass of the mature PPN1 purified from wild yeast strains is about 33– 35 kDa [20,21]
Summary
Inorganic polyphosphate (PolyP), the linear polymer containing a few to several hundred phosphate residues, performs many functions in living cells. PolyP participates in the regulation of gene expression, stress response and virulence in bacterial cells [1,2,3,4]. There is a relationship between the multiple functions of PolyP and the ability of enzymes of its metabolism to catalyze the conversion of other substrates. This ability is characteristic of many PolyP-depending enzymes. The enzymes belonging to the polyphosphate kinase 2 subfamily catalyze nucleoside monophosphate phosphorylation [14].
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