Pasi Halonen

20.05.2005
Department of Biochemistry and Food Chemistry, University of Turku, Turku

Metal-activated phosphohydrolases: Soluble inorganic pyrophosphatase, a case study

Reviewers:

Docent A.C. Papageorgiou, Turku Centre for Biotechnology, University of Turku, Turku

Professor Juha Rouvinen, Department of Chemistry, University of Joensuu, Joensuu

Opponent:

Professor Aurelio Serrano, University of Sevilla, Sevilla, Spain

Custos:

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

Publications:

  1. Fabrichniy IP, Kasho VN, Hyytia T, Salminen T, Halonen P, Dudarenkov VY, Heikinheimo P, Chernyak VY, Goldman A, Lahti R, Cooperman BS, Baykov AA. (1997) Structural and functional consequences of substitutions at the tyrosine 55-lysine 104 hydrogen bond in Escherichia coli inorganic pyrophosphatase. Biochemistry 36:7746-53.
  2. Hyytiä T, Halonen P, Salminen A, Goldman A, Lahti R & Cooperman BS. (2001) Ligand binding sites in Escherichia coli inorganic pyrophosphatase. Effects of active site mutations. Biochemistry 40:4645-4653.
  3. Parfenyev AN, Salminen A, Halonen P, Pohjanjoki P, Goldman A, Hachimori A, Baykov A & 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.
  4. Halonen P, Baykov AA, Goldman A, Lahti R & Cooperman BS. (2002) Single-turnover kinetics of Saccharomyces cerevisiae inorganic pyrophosphatase. Biochemistry. 41:12025-12031.
  5. Halonen P, Tammenkoski M, Niiranen L, Huopalahti S, Parfenyev AN, Goldman A, Baykov A, Lahti R. (2005) Effects of active site mutations on the metal binding affinity, catalytic competence, and stability of the family II pyrophosphatase from Bacillus subtilis. Biochemistry 44:4004-10.