Purification and properties of exopolyphosphatase isolated from Saccharomyces cerevisiae vacuoles

FEBS Letters
N A AndreevaI Kulaev

Abstract

An exopolyphosphatase (polyPase) with a specific activity of 60 U/mg protein has been purified from the vacuolar sap of Saccharomyces cerevisiae. The molecular mass of the intact enzyme was found to be 245 kDa. It is highly specific towards high-molecular polyphosphates (polyP). The activity with polyP9 is 24% of that with polyP208. The apparent Km for polyP15 and polyP208 hydrolysis is 93 and 2.4 microM, respectively. The enzyme is slightly active with polyP3 and adenosine-5'-tetraphosphate, but does not hydrolyze pyrophosphate, ATP, GTP and p-nitrophenylphosphate. It is stimulated by divalent metal cations. Co2+, the best activator, stimulates it 6-fold. Antibodies that inhibit the cell envelope and cytosol polyPases of S. cerevisiae have no effect on the vacuolar polyPase. The vacuolar polyPase differs from other yeast polyPases in molecular mass, substrate specificity and effects of activators.

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Citations

Oct 20, 2005·Journal of Bioscience and Bioengineering·I KulaevT Kulakovskaya
Nov 13, 2008·Proceedings of the National Academy of Sciences of the United States of America·Boguslaw NocekAlexander F Yakunin
Jun 29, 2000·Annual Review of Biochemistry·A KornbergD Ault-Riché
Jul 12, 2001·Proceedings of the National Academy of Sciences of the United States of America·A SethuramanA Kornberg
Oct 6, 2000·Annual Review of Microbiology·I Kulaev, T Kulakovskaya
Dec 15, 2006·BMC Genomics·Adrian K ArakakiJeffrey Skolnick
Jun 6, 2009·PloS One·Sidney OmelonMarc D Grynpas
May 1, 2009·PloS One·Eleonora ZakharianTibor Rohacs
Apr 12, 2003·FEMS Yeast Research·Lidia P LichkoIgor S Kulaev
Apr 9, 2021·Biochemistry. Biokhimii︠a︡·Tatiana V KulakovskayaMichail A Eldarov
Apr 20, 1999·Biochemical and Biophysical Research Communications·K NishimuraY Kakinuma

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