- 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 Search PMC articles PubMed articles 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
The 4 substrates of this enzyme are ATP, deamido-NAD+, L-glutamine, and H2O, whereas its 4 products are AMP, diphosphate, NAD+, and L-glutamate.
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
- IMSANDE J (1961). "Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia coli". J. Biol. Chem. 236: 1494–7. PMID 13717628.
- IMSANDE J, HANDLER P (1961). "Biosynthesis of diphosphopyridine nucleotide. III. Nicotinic acid mononucleotide pyrophos-phorylase". J. Biol. Chem. 236: 525–30. PMID 13717627.
This ligase article is a stub. You can help Wikipedia by expanding it.