| nicotinamide-nucleotide adenylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Nicotinamide-nucleotide adenylyltransferase (nuclear) hexamer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.7.1 | ||||||||
| CAS no. | 9032-70-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, nicotinamide-nucleotide adenylyltransferase (NMNAT) (EC 2.7.7.1) are enzymes that catalyzes the chemical reaction
- ATP + nicotinamide mononucleotide diphosphate + NAD+
Thus, the two substrates of this enzyme are ATP and nicotinamide mononucleotide (NMN), whereas its two products are diphosphate and NAD+.
This enzyme participates in nicotinate and nicotinamide metabolism.
Humans have three protein isoforms: NMNAT1 (widespread), NMNAT2 (predominantly in brain), and NMNAT3 (highest in liver, heart, skeletal muscle, and erythrocytes).[1] Mutations in the NMNAT1 gene lead to the LCA9 form of Leber congenital amaurosis.[1] Mutations in NMNAT2 or NMNAT3 genes are not known to cause any human disease.[1] NMNAT2 is critical for neurons: loss of NMNAT2 is associated with neurodegeneration.[1] All NMNAT isoforms reportedly decline with age.[2]
- ^ a b c d Brazill JM, Li C, Zhu Y, Zhai RG (2017). "NMNAT: It's an NAD + Synthase… It's a Chaperone… It's a Neuroprotector". Current Opinion in Genetics & Development. 44: 156–162. doi:10.1016/j.gde.2017.03.014. PMC 5515290. PMID 28445802.
- ^ McReynolds MR, Chellappa L, Baur JA (2020). "Age-related NAD + Decline". Experimental Gerontology. 134: 110888. doi:10.1016/j.exger.2020.110888. PMC 7442590. PMID 32097708. S2CID 211237873.