| NAD+ synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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+ synthase (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 synthases). The systematic name of this enzyme class is deamido-NAD+:ammonia ligase (AMP-forming). Other names in common use include NAD+ synthetase, NAD+ synthase, nicotinamide adenine dinucleotide synthetase, and diphosphopyridine nucleotide synthetase. This enzyme participates in nicotinate and nicotinamide metabolism and nitrogen metabolism.
Structural studies
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
- 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. PMID 4290215.