Polyphosphatase PPN1 of Saccharomyces cerevisiae: switching of exopolyphosphatase and endopolyphosphatase activities.
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.
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, pr. Nauki 5, Pushchino, 142290, Russia.
Nadezhda
N
Andreeva
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, pr. Nauki 5, Pushchino, 142290, Russia.
Ludmila
L
Trilisenko
Centre "Bioengineering", Russian Academy of Sciences, pr. Shestidesyatiletiya Oktyabrya 7-1, Moscow, 117312, Russia.
Mikhail
M
Eldarov
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, pr. Nauki 5, Pushchino, 142290, Russia.
Tatiana
T
Kulakovskaya
D017766:Acid Anhydride Hydrolases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
D029701:Saccharomyces cerevisiae Proteins; D017766:Acid Anhydride Hydrolases; C022563:endopolyphosphatase; C020137:exopolyphosphatase