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Gene Review

ppa  -  inorganic pyrophosphatase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK4222, JW4185
 
 
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Disease relevance of ppa

  • Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12 [1].
  • To study the role of PPi in phloem cells, a chimeric gene was constructed using the phloem-specific rolC promoter of Agrobacterium rhizogenes to drive the expression of the ppa gene [2].
  • Expression studies of two paralogous ppa genes encoding distinct Family I pyrophosphatases in marine unicellular cyanobacteria reveal inactivation of the typical cyanobacterial gene [3].
  • Protein sequence alignment and phylogenetic analysis indicated that the ppa gene proper of cyanobacteria (ppa1) encodes a presumably inactive mutant enzyme whereas the second gene (ppa2) might encode an active sPPase closely related to those of some proteobacteria [3].
  • We have cloned the inorganic pyrophosphatase gene (ppa) from the facultative intracellular pathogen Bartonella bacilliformis and characterized its encoded product [4].
 

High impact information on ppa

 

Chemical compound and disease context of ppa

 

Biological context of ppa

  • The structural gene of ppa contains 528 base pairs, from which a 175-amino-acid translation product, Mr 19,572, was deduced [1].
  • Many different L. pneumophila loci are able to transform L. pneumophila after addition of plasmid DNA, including gspA, ppa, asd, and pilEL [12].
  • Crystal structure of holo inorganic pyrophosphatase from Escherichia coli at 1.9 A resolution. Mechanism of hydrolysis [10].
  • The refined crystal structures of hexameric soluble inorganic pyrophosphatase from E. coli (E-PPase) are reported to R factors of 18.7 and 18.3% at 2.15 and 2.2 A, respectively [13].
  • A recombinant with a chromosomal ppa::Kanr lesion and a temperature-sensitive replicon with a ppa+ gene showed a temperature-sensitive growth phenotype, and a mutant with the sole ppa+ gene under control of the lac promoter showed inducer-dependent growth [14].
 

Anatomical context of ppa

 

Associations of ppa with chemical compounds

  • Inorganic pyrophosphatase (IPP) is an essential enzyme that plays a pivotal role in a broad spectrum of cellular biosynthetic reactions such as amino acid, nucleotide, polysaccharide, and fatty acid biosynthesis [16].
  • Reasons for this unexpectedly efficient conversion of sucrose to starch in the ppa 1 tubers were investigated [15].
  • Over-expression of PPase resulted in an accumulation of sucrose and UDP-glucose, and decreased concentrations of hexose phosphates and glycerate-3-phosphate in growing ppa 1 tubers [15].
  • An inorganic pyrophosphatase was purified over 600-fold to homogeneity as judged by polyacrylamide gel electrophoresis [17].
  • Use of biotinylated inorganic pyrophosphatase for detection of biotin bound to solid support [18].
 

Other interactions of ppa

  • The distal portion of chpBK was found to be adjacent to the ppa gene that encodes pyrophosphatase, whose map position had not been previously determined [19].
 

Analytical, diagnostic and therapeutic context of ppa

References

  1. Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12. Lahti, R., Pitkäranta, T., Valve, E., Ilta, I., Kukko-Kalske, E., Heinonen, J. J. Bacteriol. (1988) [Pubmed]
  2. Impaired photoassimilate partitioning caused by phloem-specific removal of pyrophosphate can be complemented by a phloem-specific cytosolic yeast-derived invertase in transgenic plants. Lerchl, J., Geigenberger, P., Stitt, M., Sonnewald, U. Plant Cell (1995) [Pubmed]
  3. Expression studies of two paralogous ppa genes encoding distinct Family I pyrophosphatases in marine unicellular cyanobacteria reveal inactivation of the typical cyanobacterial gene. Gómez-García, M.R., Serrano, A. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  4. Cloning, functional expression, and complementation analysis of an inorganic pyrophosphatase from Bartonella bacilliformis. Mitchell, S.J., Minnick, M.F. Can. J. Microbiol. (1997) [Pubmed]
  5. Directed mutagenesis studies of the metal binding site at the subunit interface of Escherichia coli inorganic pyrophosphatase. Efimova, I.S., Salminen, A., Pohjanjoki, P., Lapinniemi, J., Magretova, N.N., Cooperman, B.S., Goldman, A., Lahti, R., Baykov, A.A. J. Biol. Chem. (1999) [Pubmed]
  6. The structures of Escherichia coli inorganic pyrophosphatase complexed with Ca(2+) or CaPP(i) at atomic resolution and their mechanistic implications. Samygina, V.R., Popov, A.N., Rodina, E.V., Vorobyeva, N.N., Lamzin, V.S., Polyakov, K.M., Kurilova, S.A., Nazarova, T.I., Avaeva, S.M. J. Mol. Biol. (2001) [Pubmed]
  7. Expression of E. coli inorganic pyrophosphatase in transgenic plants alters photoassimilate partitioning. Sonnewald, U. Plant J. (1992) [Pubmed]
  8. Effect of replacement of His-118, His-125 and Trp-143 by alanine on the catalytic activity and subunit assembly of inorganic pyrophosphatase from thermophilic bacterium PS-3. Aoki, M., Uchiumi, T., Tsuji, E., Hachimori, A. Biochem. J. (1998) [Pubmed]
  9. Structural and functional consequences of substitutions at the tyrosine 55-lysine 104 hydrogen bond in Escherichia coli inorganic pyrophosphatase. Fabrichniy, I.P., Kasho, V.N., Hyytiä, T., Salminen, T., Halonen, P., Dudarenkov, V.Y., Heikinheimo, P., Chernyak, V.Y., Goldman, A., Lahti, R., Cooperman, B.S., Baykov, A.A. Biochemistry (1997) [Pubmed]
  10. Crystal structure of holo inorganic pyrophosphatase from Escherichia coli at 1.9 A resolution. Mechanism of hydrolysis. Harutyunyan, E.H., Oganessyan, V.Y., Oganessyan, N.N., Avaeva, S.M., Nazarova, T.I., Vorobyeva, N.N., Kurilova, S.A., Huber, R., Mather, T. Biochemistry (1997) [Pubmed]
  11. Crystal structure of Escherichia coli inorganic pyrophosphatase complexed with SO4(2-). Ligand-induced molecular asymmetry. Avaeva, S., Kurilova, S., Nazarova, T., Rodina, E., Vorobyeva, N., Sklyankina, V., Grigorjeva, O., Harutyunyan, E., Oganessyan, V., Wilson, K., Dauter, Z., Huber, R., Mather, T. FEBS Lett. (1997) [Pubmed]
  12. Natural competence for DNA transformation by Legionella pneumophila and its association with expression of type IV pili. Stone, B.J., Kwaik, Y.A. J. Bacteriol. (1999) [Pubmed]
  13. Structure of Escherichia coli inorganic pyrophosphatase at 2.2 A resolution. Kankare, J., Salminen, T., Lahti, R., Cooperman, B.S., Baykov, A.A., Goldman, A. Acta Crystallogr. D Biol. Crystallogr. (1996) [Pubmed]
  14. Pyrophosphatase is essential for growth of Escherichia coli. Chen, J., Brevet, A., Fromant, M., Lévêque, F., Schmitter, J.M., Blanquet, S., Plateau, P. J. Bacteriol. (1990) [Pubmed]
  15. Overexpression of pyrophosphatase leads to increased sucrose degradation and starch synthesis, increased activities of enzymes for sucrose-starch interconversions, and increased levels of nucleotides in growing potato tubers. Geigenberger, P., Hajirezaei, M., Geiger, M., Deiting, U., Sonnewald, U., Stitt, M. Planta (1998) [Pubmed]
  16. Cellular signaling mediated by calphoglin-induced activation of IPP and PGM. Takahashi, K., Inuzuka, M., Ingi, T. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  17. Purification and characterization of an inorganic pyrophosphatase from the extreme thermophile Thermus aquaticus. Verhoeven, J.A., Schenck, K.M., Meyer, R.R., Trela, J.M. J. Bacteriol. (1986) [Pubmed]
  18. Use of biotinylated inorganic pyrophosphatase for detection of biotin bound to solid support. Vener, A.V., Evtushenko, O.A., Baykov, A.A. Anal. Biochem. (1990) [Pubmed]
  19. chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100. Masuda, Y., Miyakawa, K., Nishimura, Y., Ohtsubo, E. J. Bacteriol. (1993) [Pubmed]
  20. A site-directed mutagenesis study on Escherichia coli inorganic pyrophosphatase. Glutamic acid-98 and lysine-104 are important for structural integrity, whereas aspartic acids-97 and -102 are essential for catalytic activity. Lahti, R., Pohjanoksa, K., Pitkäranta, T., Heikinheimo, P., Salminen, T., Meyer, P., Heinonen, J. Biochemistry (1990) [Pubmed]
  21. Genetic engineering of Escherichia coli inorganic pyrophosphatase. Tyr55 and Tyr141 are important for the structural integrity. Lahti, R., Salminen, T., Latonen, S., Heikinheimo, P., Pohjanoksa, K., Heinonen, J. Eur. J. Biochem. (1991) [Pubmed]
  22. Cloning and expression of the inorganic pyrophosphatase gene from the amino acid producer Brevibacterium lactofermentum ATCC 13869. Ramos, A., Adham, S.A., Gil, J.A. FEMS Microbiol. Lett. (2003) [Pubmed]
 
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