NAD synthase (glutamine-hydrolyzing) | |||||||||
---|---|---|---|---|---|---|---|---|---|
Glutamine-dependent NAD+ synthetase homooctamer, Human | |||||||||
Identifiers | |||||||||
EC no. | 6.3.5.1 | ||||||||
CAS no. | 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 / QuickGO | ||||||||
|
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.
The substrates of this enzyme are ATP, deamido-NAD+, L-glutamine, and H2O, whereas its 4 products are AMP, diphosphate, NAD, and glutamate
This enzyme participates in glutamate metabolism and nicotinate and nicotinamide metabolism.
Nomenclature
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).
References
- Bieganowski P, Pace HC, Brenner C (August 2003). "Eukaryotic NAD+ synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase". The Journal of Biological Chemistry. 278 (35): 33049–55. doi:10.1074/jbc.m302257200. PMID 12771147.
- Wojcik M, Seidle HF, Bieganowski P, Brenner C (November 2006). "Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste". The Journal of Biological Chemistry. 281 (44): 33395–402. doi:10.1074/jbc.m607111200. PMID 16954203.
Enzymes: CO CS and CN ligases (EC 6.1-6.3) | |
---|---|
6.1: Carbon-Oxygen | |
6.2: Carbon-Sulfur | |
6.3: Carbon-Nitrogen |
Enzymes | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|
This EC 6.3 enzyme-related article is a stub. You can help Misplaced Pages by expanding it. |