Reactome | NMNAT2 transfers an adenylyl group from ATP to NAMN to yield NAAD

NMNAT2 transfers an adenylyl group from ATP to NAMN to yield NAAD

Stable Identifier

R-HSA-197235

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol, Golgi membrane

Synonyms

Nicotinate D-ribonucleotide + ATP => deamino-NAD+ + pyrophosphate [NMNAT2]

ReviewStatus

5/5

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NMNAT2 transfers an adenylyl group from ATP to NAMN to yield NAAD

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NMNAT2 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form deamino-NAD+ (nicotinate adenine dinucleotide) and pyrophosphate (Sorci et al. 2007). The active form of the enzyme is a monomer in vitro; Mg2+ is required for activity (Raffaelli et al. 2002; Sorci et al. 2007). Although the predicted amino acid sequence of the enzyme lacks an obvious signal sequence or transmembrane domain (Yalowitz et al. 2004), recombinant FLAG-tagged protein expressed in HeLa cells localizes predominantly to the Golgi apparatus (Berger et al. 2005). Its localization within the Golgi apparatus is unknown and the annotation here is based on the plausible but speculative assumption that the enzyme is associated with the Gogi membrane and accessible from the cytosol. Immunostaining studies indicate that the protein is abundant in Islets of Langerhans and in several regions of the brain (Yalowitz et al. 2004).

Literature References

PubMed ID	Title	Journal	Year
14516279	Characterization of human brain nicotinamide 5'-mononucleotide adenylyltransferase-2 and expression in human pancreas Deeg, MA, Biju, MP, Yalowitz, JA, Cummings, OW, Antony, AC, Jayaram, HN, Xiao, S	Biochem J	2004
12359228	Identification of a novel human nicotinamide mononucleotide adenylyltransferase Mazzola, F, Magni, G, Amici, A, Emanuelli, M, Sorci, L, Raffaelli, N	Biochem Biophys Res Commun	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 Magni, G, Petrelli, R, Scotti, S, Orsomando, G, Cimadamore, F, Franchetti, P, Sorci, L, Cappellacci, L	Biochemistry	2007
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