The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

PPA2  -  inorganic diphosphatase PPA2

Saccharomyces cerevisiae S288c

Synonyms: IPP2, Inorganic pyrophosphatase, mitochondrial, PPase, Pyrophosphate phospho-hydrolase, YM8156.09, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of PPA2

  • When the bovine PPase cDNA was expressed in Escherichia coli, catalytically active PPase was produced that comigrated with bovine retinal PPase in a nondenaturing gel and was clearly distinguishable from the host PPase [1].

High impact information on PPA2

  • These results demonstrate that hydrolysis of cytosolic PPi is essential for yeast growth and that this function is not substantially affected by the intrinsic characteristics of the PPase protein that accomplishes it [2].
  • Our structures of the yeast PPase product complex at 1.15 A and fluoride-inhibited complex at 1.9 A visualize the active site in three different states: substrate-bound, immediate product bound, and relaxed product bound [3].
  • Yeast exopolyphosphatase (scPPX) processively splits off the terminal phosphate group from linear polyphosphates longer than pyrophosphate. scPPX belongs to the DHH phosphoesterase superfamily and is evolutionarily close to the well characterized family II pyrophosphatase (PPase) [4].
  • The effects of fluoride on the Y-PPase variants confirmed that PPase catalysis involves two enzyme.PP(i) intermediates, which bind fluoride with greatly different rates (Baykov, A. A., Fabrichniy, I. P., Pohjanjoki, P., Zyryanov, A. B., and Lahti, R. (2000) Biochemistry 39, 11939-11947) [5].
  • Mutations at P2 subsite residues (Y93F and K56R) caused a much greater decrease in phosphate binding affinity of yeast PPase in the presence of Mn(2+) or Co(2+) than mutations at P1 subsite residues (R78K and K193R) [6].

Biological context of PPA2

  • The new gene, PPA2, is located on chromosome 13 and encodes a protein whose sequence is 49% identical to the cytoplasmic enzyme [7].
  • Uncouplers stimulate the PPase activity several-fold in mitochondria from both cells that overexpress PPA2 from a high copy number plasmid and cells with normal expression [8].
  • We conclude that the mitochondrial PPase encoded by PPA2 is essential for mitochondrial function and maintenance of the mitochondrial genome [7].
  • The deduced amino acid sequence is 49.5% identical to that of PPase from Saccharomyces cerevisiae, and contains identical amino acid residues at all of the positions previously identified as essential for catalytic activity in that enzyme [1].
  • This sequence information was used to clone PPase cDNA from a retinal cDNA library [1].

Anatomical context of PPA2

  • The other, PPA2, is located in the mitochondria and appears to be energy-linked [9].
  • This stimulation is much higher, whereas basal PPase activity is lower, in isotonic than in hypotonic solution, which indicates that intact membranes are a prerequisite for maximal effects [8].
  • Phosphoprotein phosphatases (PPase) were isolated from either the rabbit cerebral cortex or Baker's yeast by excluding endogenous megamodulin with histone, and then by desalting cations with Bio-Gel P-6DG filtration [10].

Associations of PPA2 with chemical compounds


Other interactions of PPA2


  1. Molecular cloning and functional expression of cDNA encoding a mammalian inorganic pyrophosphatase. Yang, Z., Wensel, T.G. J. Biol. Chem. (1992) [Pubmed]
  2. Functional complementation of yeast cytosolic pyrophosphatase by bacterial and plant H+-translocating pyrophosphatases. Perez-Castineira, J.R., Lopez-Marques, R.L., Villalba, J.M., Losada, M., Serrano, A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  3. Toward a quantum-mechanical description of metal-assisted phosphoryl transfer in pyrophosphatase. Heikinheimo, P., Tuominen, V., Ahonen, A.K., Teplyakov, A., Cooperman, B.S., Baykov, A.A., Lahti, R., Goldman, A. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  4. Kinetic and Mutational Analyses of the Major Cytosolic Exopolyphosphatase from Saccharomyces cerevisiae. Tammenkoski, M., Moiseev, V.M., Lahti, M., Ugochukwu, E., Brondijk, T.H., White, S.A., Lahti, R., Baykov, A.A. J. Biol. Chem. (2007) [Pubmed]
  5. Probing essential water in yeast pyrophosphatase by directed mutagenesis and fluoride inhibition measurements. Pohjanjoki, P., Fabrichniy, I.P., Kasho, V.N., Cooperman, B.S., Goldman, A., Baykov, A.A., Lahti, R. J. Biol. Chem. (2001) [Pubmed]
  6. The electrophilic and leaving group phosphates in the catalytic mechanism of yeast pyrophosphatase. Zyryanov, A.B., Pohjanjoki, P., Kasho, V.N., Shestakov, A.S., Goldman, A., Lahti, R., Baykov, A.A. J. Biol. Chem. (2001) [Pubmed]
  7. Yeast PPA2 gene encodes a mitochondrial inorganic pyrophosphatase that is essential for mitochondrial function. Lundin, M., Baltscheffsky, H., Ronne, H. J. Biol. Chem. (1991) [Pubmed]
  8. Characterization of a mitochondrial inorganic pyrophosphatase in Saccharomyces cerevisiae. Lundin, M., Deopujari, S.W., Lichko, L., da Silva, L.P., Baltscheffsky, H. Biochim. Biophys. Acta (1992) [Pubmed]
  9. Computer modeling of two inorganic pyrophosphatases. Vihinen, M., Lundin, M., Baltscheffsky, H. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  10. Stimulation of mammalian and yeast phosphoprotein phosphatases by megamodulins from various sources. Kuo, W.N. Biochem. Biophys. Res. Commun. (1983) [Pubmed]
  11. Single-turnover kinetics of Saccharomyces cerevisiae inorganic pyrophosphatase. Halonen, P., Baykov, A.A., Goldman, A., Lahti, R., Cooperman, B.S. Biochemistry (2002) [Pubmed]
  12. Evolutionary conservation of enzymatic catalysis: quantitative comparison of the effects of mutation of aligned residues in Saccharomyces cerevisiae and Escherichia coli inorganic pyrophosphatases on enzymatic activity. Pohjanjoki, P., Lahti, R., Goldman, A., Cooperman, B.S. Biochemistry (1998) [Pubmed]
WikiGenes - Universities