NAD+ synthase
| NAD+ synthetase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.1.5 | ||||||||
| CAS no. | 9032-69-3 | ||||||||
| 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+ synthetase (EC 6.3.1.5) is an enzyme that catalyzes the chemical reaction
- ATP + deamido-NAD+ + NH3 AMP + diphosphate + NAD+
The 3 substrates of this enzyme are ATP, deamido-NAD+, and NH3, whereas its 3 products are AMP, diphosphate, and NAD+.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthetase). The systematic name of this enzyme class is deamido-NAD+:ammonia ligase (AMP-forming). Other names in common use include NAD+ synthetase, NAD+ synthetase, nicotinamide adenine dinucleotide synthetase, and diphosphopyridine nucleotide synthetase. This enzyme participates in nicotinate and nicotinamide metabolism and nitrogen metabolism.
Structural studies
[edit]As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1WXE, 1WXF, 1WXG, 1WXH, 1WXI, 1XNG, 1XNH, 2E18, 2PZ8, 2PZA, and 2PZB.
References
[edit]- Spencer RL, Preiss J (1967). "Biosynthesis of diphosphopyridine nucleotide. The purification and the properties of diphospyridine nucleotide synthetase from Escherichia coli b". J. Biol. Chem. 242 (3): 385–92. doi:10.1016/S0021-9258(18)96282-4. PMID 4290215.
