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Gene Review

ECs5204  -  inorganic pyrophosphatase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs5204

  • Replacements of His21 and His86 in mtPPase with the residues found in the corresponding positions of E. coli PPase had either no effect on the Mg2+- and Mn2+-supported reactions (H86K) or reduced Mg2+-supported activity (H21K) [1].
  • Here, we report the structural and functional characterization of a unique family I PPase from Mycobacterium tuberculosis (mtPPase) that has two His residues (His21 and His86) in the active site [1].
  • Pyrophosphatase (PPase) from Bacillus subtilis has recently been found to be the first example of a family II soluble PPase with a unique requirement for Mn2+ [2].
  • A protein phosphatase (PPase) from the bacteriophage lambda was overexpressed in Escherichia coli [3].
  • This suggests that B. subtilis PPase represents a new family of soluble PPases (a Bs family), putative members of which were found in Archaeoglobus fulgidus, Methanococcus jannaschii, Streptococcus mutans and Streptococcus gordonii [4].

High impact information on ECs5204


Chemical compound and disease context of ECs5204

  • Rabbit antiserum raised against the spinach leaf ADP-Glc PPase (but not the one raised against the enzyme from Escherichia coli) inhibited the activity of the purified algal enzyme, which migrated as a single protein band in native polyacrylamide gel electrophoresis [8].

Biological context of ECs5204

  • Antisera raised against the spinach leaf holoenzyme and against the 51-kD spinach subunit cross-reacted with both subunits of the algal ADP-Glc PPase in immunoblot hybridization, but the cross-reaction was stronger for the 50-kD algal subunit than for the 53-kD subunit [8].
  • A homolog to the eubacteria inorganic pyrophosphatase (PPase, EC was found in the genome of the hyperthermophilic archaeon Pyrococcus horikoshii [9].
  • At the same time, occupation of center IV eliminates the inhibition of inorganic pyrophosphate hydrolysis by high Mg2+ concentrations typical of wild-type PPase [10].
  • Furthermore, the partial amino acid sequence (residues 1 to 108) of E. coli PPase determined by S [11].
  • In exponentially growing cells the intracellular PPi concentration was in every case 1.5 nmol/mg (dry weight) or about 0.5 mM, even though the amount of PPase was varied from 15 to 2,600% of the control amount by mutation or by using a multicopy plasmid with an inserted gene (ppa) encoding PPase [12].

Associations of ECs5204 with chemical compounds


Analytical, diagnostic and therapeutic context of ECs5204

  • In contrast to wild-type PPase, which is hexameric, these variants can be dissociated into trimers by dilution, as shown by analytical ultracentrifugation and cross-linking [6].
  • The recombinant PPase from P. horikoshii (PhPPase) has a molecular mass of 24.5 kDa, determined by SDS-PAGE [18].
  • Differential scanning calorimetry has been used to determine the apparent enthalpy of thermal denaturation for the native PPase and its mutant variants Gly100Ala and Gly147Val [17].


  1. An unusual, His-dependent family I pyrophosphatase from Mycobacterium tuberculosis. Tammenkoski, M., Benini, S., Magretova, N.N., Baykov, A.A., Lahti, R. J. Biol. Chem. (2005) [Pubmed]
  2. Quaternary structure and metal ion requirement of family II pyrophosphatases from Bacillus subtilis, Streptococcus gordonii, and Streptococcus mutans. Parfenyev, A.N., Salminen, A., Halonen, P., Hachimori, A., Baykov, A.A., Lahti, R. J. Biol. Chem. (2001) [Pubmed]
  3. Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase. Zhuo, S., Clemens, J.C., Hakes, D.J., Barford, D., Dixon, J.E. J. Biol. Chem. (1993) [Pubmed]
  4. Cloning and expression of a unique inorganic pyrophosphatase from Bacillus subtilis: evidence for a new family of enzymes. Shintani, T., Uchiumi, T., Yonezawa, T., Salminen, A., Baykov, A.A., Lahti, R., Hachimori, A. FEBS Lett. (1998) [Pubmed]
  5. H+-pyrophosphatase of Rhodospirillum rubrum. High yield expression in Escherichia coli and identification of the Cys residues responsible for inactivation my mersalyl. Belogurov, G.A., Turkina, M.V., Penttinen, A., Huopalahti, S., Baykov, A.A., Lahti, R. J. Biol. Chem. (2002) [Pubmed]
  6. Dissociation of hexameric Escherichia coli inorganic pyrophosphatase into trimers on His-136-->Gln or His-140-->Gln substitution and its effect on enzyme catalytic properties. Baykov, A.A., Dudarenkov, V.Y., Käpylä, J., Salminen, T., Hyytiä, T., Kasho, V.N., Husgafvel, S., Cooperman, B.S., Goldman, A., Lahti, R. J. Biol. Chem. (1995) [Pubmed]
  7. ADP-glucose pyrophosphorylase from potato tuber: site-directed mutagenesis of homologous aspartic acid residues in the small and large subunits. Frueauf, J.B., Ballicora, M.A., Preiss, J. Plant J. (2003) [Pubmed]
  8. Characterization of the kinetic, regulatory, and structural properties of ADP-glucose pyrophosphorylase from Chlamydomonas reinhardtii. Iglesias, A.A., Charng, Y.Y., Ball, S., Preiss, J. Plant Physiol. (1994) [Pubmed]
  9. Crystal structure of the hyperthermophilic inorganic pyrophosphatase from the archaeon Pyrococcus horikoshii. Liu, B., Bartlam, M., Gao, R., Zhou, W., Pang, H., Liu, Y., Feng, Y., Rao, Z. Biophys. J. (2004) [Pubmed]
  10. Effect of D42N substitution in Escherichia coli inorganic pyrophosphatase on catalytic activity and Mg2+ binding. Avaeva, S.M., Rodina, E.V., Kurilova, S.A., Nazarova, T.I., Vorobyeva, N.N. FEBS Lett. (1996) [Pubmed]
  11. 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]
  12. Intracellular PPi concentration is not directly dependent on amount of inorganic pyrophosphatase in Escherichia coli K-12 cells. Kukko-Kalske, E., Lintunen, M., Inen, M.K., Lahti, R., Heinonen, J. J. Bacteriol. (1989) [Pubmed]
  13. 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]
  14. 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]
  15. An assay for adenosine 5'-diphosphate (ADP)-glucose pyrophosphorylase that measures the synthesis of radioactive ADP-glucose with glycogen synthase. Yep, A., Bejar, C.M., Ballicora, M.A., Dubay, J.R., Iglesias, A.A., Preiss, J. Anal. Biochem. (2004) [Pubmed]
  16. Effects of replacement of prolines with alanines on the catalytic activity and thermostability of inorganic pyrophosphatase from thermophilic bacterium PS-3. Masuda, H., Uchiumi, T., Wada, M., Ichiba, T., Hachimori, A. J. Biochem. (2002) [Pubmed]
  17. Effect of mutation of the conservative glycine residues Gly100 and Gly147 on stability of Escherichia coli inorganic pyrophosphatase. Moiseev, V.M., Rodina, E.V., Avaeva, S.M. Biochemistry Mosc. (2005) [Pubmed]
  18. Characterization of the Family I inorganic pyrophosphatase from Pyrococcus horikoshii OT3. Jeon, S.J., Ishikawa, K. Archaea (2005) [Pubmed]
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