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Originally published In Press as doi:10.1074/jbc.M300073200 on February 6, 2003

J. Biol. Chem., Vol. 278, Issue 15, 13503-13511, April 11, 2003
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Structural Characterization of a Human Cytosolic NMN/NaMN Adenylyltransferase and Implication in Human NAD Biosynthesis*,

Xuejun ZhangDagger , Oleg V. Kurnasov§, Subramanian KarthikeyanDagger , Nick V. GrishinDagger , Andrei L. Osterman§, and Hong ZhangDagger ||

From the Dagger  Department of Biochemistry and  Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390 and § Integrated Genomics, Inc., Chicago, Illinois 60612

Pyridine dinucleotides (NAD and NADP) are ubiquitous cofactors involved in hundreds of redox reactions essential for the energy transduction and metabolism in all living cells. In addition, NAD also serves as a substrate for ADP-ribosylation of a number of nuclear proteins, for silent information regulator 2 (Sir2)-like histone deacetylase that is involved in gene silencing regulation, and for cyclic ADP ribose (cADPR)-dependent Ca2+ signaling. Pyridine nucleotide adenylyltransferase (PNAT) is an indispensable central enzyme in the NAD biosynthesis pathways catalyzing the condensation of pyridine mononucleotide (NMN or NaMN) with the AMP moiety of ATP to form NAD (or NaAD). Here we report the identification and structural characterization of a novel human PNAT (hsPNAT-3) that is located in the cytoplasm and mitochondria. Its subcellular localization and tissue distribution are distinct from the previously identified human nuclear PNAT-1 and PNAT-2. Detailed structural analysis of PNAT-3 in its apo form and in complex with its substrate(s) or product revealed the catalytic mechanism of the enzyme. The characterization of the cytosolic human PNAT-3 provided compelling evidence that the final steps of NAD biosynthesis pathways may exist in mammalian cytoplasm and mitochondria, potentially contributing to their NAD/NADP pool.

* This work was supported by National Institutes of Health Grant GM65243 (to H. Z.) and The Robert A. Welch Foundation Grant I-5051 (to N. V. G.).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.

The on-line version of this article (available at http://www.jbc.org) contains Fig. S1 and its legend on one text page.

The atomic coordinates and the structure factors (code 1NUP, 1NUQ, 1NUR, 1NUS, 1NUT, and 1NUU) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

|| To whom correspondence should be addressed. Tel.: 214-648-9299; Fax: 214-648-9099; E-mail: zhang@chop.swmed.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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