Nicotinamide-nucleotide adenylyltransferase
| 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, a nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1) is an enzyme that catalyzes the chemical reaction
- ATP + nicotinamide ribonucleotide diphosphate + NAD+
Thus, the two substrates of this enzyme are ATP and nicotinamide ribonucleotide, whereas its two products are diphosphate and NAD+.
This enzyme participates in nicotinate and nicotinamide metabolism.
The human version of this protein is NMNAT1.
Belongs to
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:nicotinamide-nucleotide adenylyltransferase. Other names in common use include NAD+ pyrophosphorylase, adenosine triphosphate-nicotinamide mononucleotide transadenylase, ATP:NMN adenylyltransferase, diphosphopyridine nucleotide pyrophosphorylase, nicotinamide adenine dinucleotide pyrophosphorylase, nicotinamide mononucleotide adenylyltransferase, and NMN adenylyltransferase.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1EJ2, 1GZU, 1HYB, 1KKU, 1KQN, 1KQO, 1KR2, 1M8F, 1M8G, 1M8J, and 1M8K.
References
- ATKINSON MR, JACKSON JF, MORTON RK (1961). "Nicotinamide mononucleotide adenylyltransferase of pig-liver nuclei. The effects of nicotinamide mononucleotide concentration and pH on dinucleotide synthesis". Biochem. J. 80 (2): 318–23. PMC 1244001. PMID 13684981.
- Dahmen W, Webb B, Preiss J (1967). "The deamido-diphosphopyridine nucleotide and diphosphopyridine nucleotide pyrophosphorylases of Escherichia coli and yeast". Arch. Biochem. Biophys. 120 (2): 440–50. doi:10.1016/0003-9861(67)90262-7. PMID 4291828.
- Kornberg A; Pricer WE (1951). "Enzymatic cleavage of diphosphopyridine nucleotide with radioactive pyrophosphate". J. Biol. Chem. 191 (2): 535–541. PMID 14861199.