NAD+ synthase (glutamine-hydrolysing)
| NAD+ synthase (glutamine-hydrolyzing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.3.5.1 | ||||||||
| CAS number | 37318-70-0 | ||||||||
| 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+ synthase (glutamine-hydrolysing) (EC 6.3.5.1) is an enzyme that catalyzes the chemical reaction
- ATP + deamido-NAD+ + L-glutamine + H2O AMP + diphosphate + NAD+ + L-glutamate. In eukaryotes, this enzyme contains a glutaminase domain related to nitrilase.[1]
The substrates of this enzyme are ATP, deamido-NAD+, L-glutamine, and H2O, whereas its 4 products are AMP, diphosphate, NAD+, and glutamate [2]
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is deamido-NAD+:L-glutamine amido-ligase (AMP-forming). Other names in common use include NAD+ synthetase (glutamine-hydrolysing), nicotinamide adenine dinucleotide synthetase (glutamine), desamidonicotinamide adenine dinucleotide amidotransferase, and DPN synthetase. This enzyme participates in glutamate metabolism and nicotinate and nicotinamide metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1EE1, 1FYD, 1IFX, 1IH8, 1KQP, 1NSY, and 2NSY.
References
- ↑ Bieganowski.; et al. (2003). "Eukaryotic NAD+ synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase". J. Biol. Chem. 278: 33049–33055. doi:10.1074/jbc.m302257200.
- ↑ Wojcik; et al. (2006). "Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste". J. Biol. Chem. 281: 33395–33402. doi:10.1074/jbc.m607111200.