Anu Salminen

3.5.2002
Department of Biochemistry and Food Chemistry, University of Turku, Turku

Discovery of a new family of soluble pyrophosphatases and the functional role of quaternary structure in pyrophosphatases

Reviewers:

Professor Herrick Baltsceffsky, Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden

Professor Mark S Johnson, Department of Biochemistry and Pharmacy, Åbo Akademi University, Turku, Finland

Opponent:

Dr. Inna Kuranova, Institute of Crystallography, Russian Academy of Sciences, Moscow, Russia

Custos:

Professor Reijo Lahti, Department of Biochemistry and Food Chemistry, University of Turku, Turku, Finland

Publications:

  1. Shintani T, Uchiumi T, Yonezawa T, Salminen A, Baykov AA, Lahti R, Hachimori, A. (1998) Cloning and expression of a unique inorganic pyrophosphatase from Bacillus subtilis: evidence for a new family of enzymes. FEBS Letters. 439:263-266
  2. Sivula T, Salminen A, Parfenyev AN, Pohjanjoki P, Goldman A, Cooperman BS, Baykov AA, Lahti R. (1999) Evolutionary aspects of inorganic pyrophosphatase. FEBS Letters. 454:75-80
  3. Efimova IS, Salminen A, Pohjanjoki P, Lapinniemi J, Magretova NN, Cooperman MS, Goldman A, Lahti R, Baykov AA. (1999) Directed Mutagenesis Studies of the Metal Binding Site at the Subunit Interface of Escherichia coli Inorganic Pyrophosphatase. J. Biol.Chem. 274:3294-3299
  4. Salminen A, Efimova IS, Parfenyev AN, Magretova NN, Mikalahti K, Goldman A, Baykov AA, Lahti R. (1999) Reciprocal Effects Substitutions at the Subunit Interfaces in Hexameric Pyrohosphatase of Escherichia coli, dimeric and monomeric forms of the enzyme. J. Biol. Chem. 274:33898-33904
  5. Merckel MC, Fabrichniy IP, Salminen A, Kalkkinen N, Baykov AA, Lahti R, Goldman A. (2001) Crystal Structure of Streptococcus mutans Pyrophosphatase: A New Fold for an Old Mechanism. Structure. 9:289-297
  6. Parfenyev AN, Salminen A, Halonen P, Hachimori A, Baykov AA, Lahti R. (2001) Quaternary Structure and Metal-Ion Requirement of Family II Pyrophosphatases from Bacillus subtilis, Streptococcus gordonii and Streptococcus mutans. J Biol. Chem. 276:24511-24518
  7. Salminen A, Parfenyev AN, Salli K, Efimova IS, Magretova NN, Goldman A, Baykov AA, Lahti R. (2002) Modulation of Dimer Stability in Yeast Pyrophosphatase by Mutans at the Subunit Interface and Ligand Binding to the Active Site. J. Biol. Chem. In press.