Reactome | NMNAT2 transfers an adenylyl group from ATP to NMN to yield NAD+

NMNAT2 transfers an adenylyl group from ATP to NMN to yield NAD+

Stable Identifier

R-HSA-8939959

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol, Golgi membrane

Synonyms

beta-nicotinamide D-ribonucleotide + ATP + H(+) => diphosphate + NAD(+)

ReviewStatus

4/5

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NMNAT2 transfers an adenylyl group from ATP to NMN to yield NAD+

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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). The protein localizes predominantly to the cytoplasmic face of the Golgi apparatus (Berger et al. 2005, Lau et al. 2010). 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
20388704	Isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases Ziegler, M, Agledal, L, Gossmann, TI, Lau, C, Dölle, C, Niere, M	J Biol Chem	2010
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