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{{enzyme
| Name = NAD<sup>+</sup> diphosphatase
| EC_number = 3.6.1.22
| CAS_number = 37289-33-1
| IUBMB_EC_number = 3/6/1/22
| GO_code = 0000210
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''NAD<sup>+</sup> diphosphatase''' ({{EC number|3.6.1.22}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:NAD<sup>+</sup> + H<sub>2</sub>O <math>\rightleftharpoons</math> AMP + NMN

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[nicotinamide adenine dinucleotide|NAD<sup>+</sup>]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[adenosine monophosphate|AMP]] and [[Nicotinamide MononNucleoside|NMN]].

This enzyme belongs to the family of [[hydrolase]]s, specifically those acting on acid anhydrides in phosphorus-containing anhydrides.  The systematic name of this enzyme class is '''NAD<sup>+</sup> 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 [[tertiary structure|structure]] has been solved for this class of enzymes, with the [[Protein Data Bank|PDB]] accession code {{PDB link|2GB5}}.

==References==
{{reflist|1}}
* {{cite journal | author = Anderson BM, Lang CA | date = 1966 | title = Nicotinamide-adenine dinucleotide pyrophosphatase in the growing and aging mosquito | journal = Biochem. J.  | volume = 101 | pages = 392&ndash;6  | pmid = 4381708 | issue = 2 | pmc = 1270119 }}
* {{cite journal | author = Nakajima Y, Fukunaga N, Sasaki S, Usami S | date = 1973 | title = Purification and properties of NADP pyrophosphatase from Proteus vulgaris | journal = Biochim. Biophys. Acta.  | volume = 293 | pages = 242&ndash;55  | pmid = 4405504 | issue = 1 }}

{{hydrolase-stub}}

[[Category:EC 3.6.1]]
[[Category:NADH-dependent enzymes]]
[[Category:Enzymes of known structure]]