Glutamine Amidotransferase (None)

Glutamine amidotransferases (GATases) are a family of enzymes that catalyze the removal of the amide nitrogen from glutamine and transfer it to a specific substrate, forming a new carbon-nitrogen bond on that substrate. This reaction is central to the biosynthesis of nucleotides, amino acids, glycoproteins, and enzyme cofactors, making GATases key metabolic enzymes essential for cell proliferation. They hydrolyze glutamine to generate ammonia (NH₃), which is then transferred to an acceptor molecule via two half-reactions. Many GATases use a catalytic triad composed of cysteine, histidine, and glutamate residues in their active site. Examples of enzymes containing GAT domains include anthranilate synthase component II, CTP synthetase, GMP synthetase, and carbamoyl-phosphate synthetases.

Inhibition of glutamine utilization for nucleotide/amino acid biosynthesis