[HTML][HTML] Eukaryotic NAD+ synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase
P Bieganowski, HC Pace, C Brenner - Journal of Biological Chemistry, 2003 - ASBMB
NAD+ is an essential co-enzyme for redox reactions and is consumed in lysine
deacetylation and poly (ADP-ribosyl) ation. NAD+ synthetase catalyzes the final step in
NAD+ synthesis in the well characterized de novo, salvage, and import pathways. It has
been long known that eukaryotic NAD+ synthetases use glutamine to amidate nicotinic acid
adenine dinucleotide while many purified prokaryotic NAD+ synthetases are ammonia-
dependent. Earlier, we discovered that glutamine-dependent NAD+ synthetases contain N …
deacetylation and poly (ADP-ribosyl) ation. NAD+ synthetase catalyzes the final step in
NAD+ synthesis in the well characterized de novo, salvage, and import pathways. It has
been long known that eukaryotic NAD+ synthetases use glutamine to amidate nicotinic acid
adenine dinucleotide while many purified prokaryotic NAD+ synthetases are ammonia-
dependent. Earlier, we discovered that glutamine-dependent NAD+ synthetases contain N …