NAD+ diphosphatase
| NAD+ diphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.1.22 | ||||||||
| CAS no. | 37289-33-1 | ||||||||
| 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, a NAD+ diphosphatase (EC 3.6.1.22) is an enzyme that catalyzes the chemical reaction
- NAD+ + H2O AMP + NMN
Thus, the two substrates of this enzyme are NAD+ and H2O, whereas its two products are AMP and NMN.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is NAD+ phosphohydrolase. Other names in common use include nicotinamide adenine dinucleotide pyrophosphatase, NADP+ pyrophosphatase, and NADH pyrophosphatase. This enzyme participates in nicotinate and nicotinamide metabolism.
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2GB5.
References
[edit]- Anderson BM, Lang CA (1966). "Nicotinamide-adenine dinucleotide pyrophosphatase in the growing and aging mosquito". Biochem. J. 101 (2): 392–6. doi:10.1042/bj1010392. PMC 1270119. PMID 4381708.
- Nakajima Y, Fukunaga N, Sasaki S, Usami S (1973). "Purification and properties of NADP pyrophosphatase from Proteus vulgaris". Biochim. Biophys. Acta. 293 (1): 242–55. doi:10.1016/0005-2744(73)90397-5. PMID 4405504.
