NAD+ synthase (glutamine-hydrolysing) explained

NAD^+ synthase (glutamine-hydrolyzing)
Ec Number:	6.3.5.1
Cas Number:	37318-70-0
Go Code:	0003952
Width:	270

In enzymology, a NAD⁺ synthase (glutamine-hydrolysing) is an enzyme that catalyzes the chemical reaction

ATP + deamido-NAD⁺ + L-glutamine + H₂O

\rightleftharpoons 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 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).

Notes and References

1. Bieganowski P, Pace HC, Brenner C . 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 . August 2003 . 12771147 . 10.1074/jbc.m302257200 . free .
2. Wojcik M, Seidle HF, Bieganowski P, Brenner C . Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste . The Journal of Biological Chemistry . 281 . 44 . 33395–402 . November 2006 . 16954203 . 10.1074/jbc.m607111200 . free.