Glutamine N-acyltransferase (GLYATL1) (GLYATL1)

Glutamine N-acyltransferase (GLYATL1) is a mitochondrial enzyme primarily expressed in the liver and kidneys that facilitates the conjugation of acyl-CoA thioesters with L-glutamine (UniProt: Q969I3). Its most significant physiological and therapeutic role in humans is the conjugation of phenylacetyl-CoA to form phenylacetylglutamine, which is subsequently excreted in the urine (PubMed: 17301241). This reaction provides an essential alternative pathway for nitrogen disposal, bypassing the urea cycle. Consequently, GLYATL1 is the functional target for nitrogen-scavenging agents such as sodium phenylbutyrate and glycerol phenylbutyrate, which are used to treat hyperammonemia in patients with urea cycle disorders (DrugBank: DB00630). By converting phenylacetate into a glutamine conjugate, the enzyme effectively removes two moles of nitrogen per mole of phenylacetate, helping to maintain ammonia homeostasis (PubMed: 22535177). Beyond nitrogen metabolism, GLYATL1 is involved in the detoxification of various organic acids and xenobiotics, contributing to the regulation of mitochondrial CoA levels (PubMed: 17301241).

Other names

Glycine N-acyltransferase-like protein 1GATAcyl-CoA:L-glutamine N-acyltransferasePhenylacetyl-CoA:L-glutamine N-acyltransferaseGlutamine N-phenylacetyltransferase

Catalyzes the N-acylation of L-glutamine with phenylacetyl-CoA to produce phenylacetylglutamine, facilitating the excretion of waste nitrogen in patients with urea cycle defects.