NMNAT1 transfers an adenylyl group from ATP to NAMN to yield NAAD

Stable Identifier
Reaction [transition]
Homo sapiens
Nicotinate D-ribonucleotide + ATP => deamino-NAD+ + pyrophosphate [NMNAT1]
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NMNAT1 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form deamino-NAD+ (nicotinate adenine dinucleotide) and pyrophosphate (Schweiger et al. 2001). The active form of the enzyme in vitro is a hexamer (Zhou et al. 2002), and its activity is substantially greater in the presence of Zn++ than of Mg++ (Sorci et al. 2007). The predicted amino acid sequence of the enzyme contains a nuclear localization domain and the protein is observed to localize to the nucleus (Schweiger et al. 2001; Berger et al. 2005).
Literature References
PubMed ID Title Journal Year
17402747 Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis

Magni, G, Petrelli, R, Scotti, S, Orsomando, G, Cimadamore, F, Franchetti, P, Sorci, L, Cappellacci, L

Biochemistry 2007
11788603 Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin.

Kurnasov, OV, Marquez, VE, Binns, DD, Osterman, AL, Tomchick, DR, Zhang, H, Zhou, T, Grishin, NV

J Biol Chem 2002
11248244 Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis

Oei, SL, Hirsch-Kauffmann, M, Hennig, K, Ziegler, M, Lerner, F, Schweiger, M, Weise, C, Specht, T, Niere, M

FEBS Lett 2001
16118205 Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms

Ziegler, M, Berger, F, Dahlmann, M, Lau, C

J Biol Chem 2005
Catalyst Activity

nicotinate-nucleotide adenylyltransferase activity of 6xNMNAT1:6xZn2+ [nucleoplasm]

Orthologous Events
Cross References
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