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J. Biol. Chem., Vol. 280, Issue 47, 39200-39207, November 25, 2005

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MJ0917 in Archaeon Methanococcus jannaschii Is a Novel NADP Phosphatase/NAD Kinase^*

From the Department of Basic and Applied Molecular Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan

NAD kinase phosphorylates NAD⁺ to form NADP⁺. Conversely, NADP phosphatase, which has not yet been identified, dephosphorylates NADP⁺ to produce NAD⁺. Among the NAD kinase homologs, the primary structure of MJ0917 of hyperthermophilic archaeal Methanococcus jannaschii is unique. MJ0917 possesses an NAD kinase homologous region in its C-terminal half and an inositol-1-phosphatase homologous region in its N-terminal half. In this study, MJ0917 was biochemically shown to possess both NAD kinase and phosphatase activities toward NADP⁺, NADPH, and fructose 1,6-bisphosphate, but not toward inositol 1-phosphate. With regard to the phosphatase activity, kinetic values indicated that NADP⁺ is the preferred substrate and that MJ0917 would function as a novel NADP phosphatase/NAD kinase showing conflicting dual activities, viz. synthesis and degradation of an essential NADP⁺. Furthermore, in vitro analysis of MJ0917 showed that, although MJ0917 could supply NADP⁺, it prevented excess accumulation of NADP⁺; thus, it has the ability to maintain a high NAD⁺/NADP⁺ ratio, whereas 5'-AMP would decrease this ratio. The evolutionary process during which MJ0917 arose is also discussed.

Received for publication, June 13, 2005 , and in revised form, September 27, 2005.

^* This work was supported in part by Grant-in-aid 15780212 from the Ministry of Education, Culture, Sports, Science, and Technology of Japan and by the Program for Promotion of Basic Research Activities for Innovative Biosciences. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental TABLES 1S and 2S.

¹ To whom correspondence should be addressed. Tel.: 81-774-38-3766; Fax: 81-774-38-3767; E-mail: kmurata{at}kais.kyoto-u.ac.jp.

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