NAD+ synthase (glutamine-hydrolysing)

From Wikipedia, the free encyclopedia

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 $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 6.3.5.1
BRENDA references for 6.3.5.1 (Recommended.)
PubMed references for 6.3.5.1
PubMed Central references for 6.3.5.1
Google Scholar references for 6.3.5.1
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.