NAD+ diphosphatase
| NAD+ diphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.1.22 | ||||||||
| CAS number | 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 / EGO | ||||||||
| |||||||||
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
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2GB5.
References
- Anderson BM, Lang CA (1966). "Nicotinamide-adenine dinucleotide pyrophosphatase in the growing and aging mosquito". Biochem. J. 101 (2): 392–6. 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.
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