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

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

Stable Identifier

R-HSA-200512

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

Synonyms

Nicotinate D-ribonucleotide + ATP => deamino-NAD+ + pyrophosphate [NMNAT1]

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

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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
11788603	Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin. Zhou, T, Kurnasov, OV, Tomchick, DR, Binns, DD, Grishin, NV, Marquez, VE, Osterman, AL, Zhang, H	J Biol Chem	2002
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 Sorci, L, Cimadamore, F, Scotti, S, Petrelli, R, Cappellacci, L, Franchetti, P, Orsomando, G, Magni, G	Biochemistry	2007
11248244	Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis Schweiger, M, Hennig, K, Lerner, F, Niere, M, Hirsch-Kauffmann, M, Specht, T, Weise, C, Oei, SL, Ziegler, M	FEBS Lett	2001
16118205	Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms Berger, F, Lau, C, Dahlmann, M, Ziegler, M	J Biol Chem	2005