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Originally published In Press as doi:10.1074/jbc.M101829200 on May 7, 2001

J. Biol. Chem., Vol. 276, Issue 27, 24511-24518, July 6, 2001
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Quaternary Structure and Metal Ion Requirement of Family II Pyrophosphatases from Bacillus subtilis, Streptococcus gordonii, and Streptococcus mutans*

Alexey N. ParfenyevDagger , Anu Salminen§, Pasi Halonen§, Akira Hachimori, Alexander A. BaykovDagger ||, and Reijo Lahti§||

From the Dagger  A. N. Belozersky Institute of Physico-Chemical Biology and School of Chemistry, Moscow State University, Moscow 119899, Russia, the § Department of Biochemistry, University of Turku, FIN-20500 Turku, Finland, and the  Institute of High Polymer Research, Faculty of Textile Science and Technology, Shinshu University, 3-15-1 Tokida, Ueda, Nagano 386-8856, Japan

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+. In the present work, we cloned and overexpressed in Escherichia coli putative genes for two more family II PPases (from Streptococcus mutans and Streptococcus gordonii), isolated the recombinant proteins, and showed them to be highly specific and active PPases (catalytic constants of 1700-3300 s-1 at 25 °C in comparison with 200-400 s-1 for family I). All three family II PPases were found to be dimeric manganese metalloenzymes, dissociating into much less active monomers upon removal of Mn2+. The dimers were found to have one high affinity manganese-specific site (Kd of 0.2-3 nM for Mn2+ and 10-80 µM for Mg2+) and two or three moderate affinity sites (Kd ~ 1 mM for both cations) per subunit. Mn2+ binding to the high affinity site, which occurs with a half-time of less than 10 s at 1.5 mM Mn2+, dramatically shifts the monomer left-right-arrow dimer equilibrium in the direction of the dimer, further activates the dimer, and allows substantial activity (60-180 s-1) against calcium pyrophosphate, a potent inhibitor of family I PPases.

* This work was supported by Russian Foundation for Basic Research Grants 00-04-48310, 00-15-97907, and 01-04-06111 and Academy of Finland Grants 35736 and 47513.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence may be addressed. Tel.: 7-095-939-5541; Fax: 7-095-939-3181; E-mail: baykov@genebee.msu.su (to A. B.) or Tel.: 358-2-333-6845; Fax: 358-2-333-6860; E-mail: reijo.lahti@utu.fi (to R. L.).

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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