characterization of the family i inorganic pyrophosphatase from pyrococcus horikoshii ot3描述家庭的我从海床无机焦磷酸酶horikoshii ot3.pdfVIP

Archaea 1, 385–389 © 2005 Heron Publishing—Victoria, Canada Characterization of the Family I inorganic pyrophosphatase from Pyrococcus horikoshii OT3 1,2 3,4 SUNG-JONG JEON, and KAZUHIKO ISHIKAWA 1 Department of Biotechnology and Bioengineering, Dong-Eui University, Busan, 614-714, Korea 2 Department of Biomaterial Control, Dong-Eui University, Busan, 614-714, Korea 3 Research Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology (AIST Kansai), 1-8-31 Midorigaoka, Ikeda, Osaka 563-8577, Japan 4 Corresponding author (kazu-ishikawa@aist.go.jp) Received January 8, 2005; accepted February 2, 2005; published online May 31, 2005 Summary A gene encoding for a putative Family inorganic into Family I and Family II PPases (Shintani et al. 1998, pyrophosphatase (PPase, EC ) from the hyperthermo- Young et al. 1998). Family I PPases have a highly conserved philic archaeon Pyrococcus horikoshii OT3 was cloned and the active site structure formed by 14–16 amino acid residues and biochemical characteristics of the resulting recombinant pro- three to four Mg2+ ions and have similar catalytic properties tein were examined. The gene (Accession No. 1907) from (Harutyunyan et al. 1996, Heikinheimo et al. 1996, Baykov et P. horikoshii showed some identity with other Family I inor- al. 1999). Family II PPases are activated by Mn2+ and display ganic pyrophosphatases from archaea. The recombinant PPase 10–20 times greater activity than Family I PPases (Shintani et from P. horikoshii (PhPPase) has a molecular mass of al. 1998, Parfenyev et al. 2001). 24.5 kDa, determined by SDS. This enzyme specifi-