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Glycine N-acyltransferase-like protein 2 (GLYATL2) is an enzyme that facilitates the transfer of an acyl group from medium- and long-chain acyl-CoA molecules (especially monounsaturated fatty acids such as oleoyl-CoA and arachidonoyl-CoA) to glycine, leading to the synthesis of bioactive N-acyl glycine lipids. These products are involved in fatty acid metabolism and function as signaling molecules with antinociceptive, anti-inflammatory, and antiproliferative effects, and can activate G-protein-coupled receptors. GLYATL2 is primarily localized in the endoplasmic reticulum, with mRNA expressed in salivary gland, trachea, spinal cord, and skin fibroblasts. Its expression and activity suggest roles in skin and lung barrier function and immune response[1][2][6][4]. GLYATL2 belongs to the family of acyltransferase enzymes, and its paralog GLYATL1 performs similar functions[2][6]. No current drugs, biomarkers, or safety issues linked directly to GLYATL2 have been described in the retrieved literature.
Not specified for existing drugs (the enzyme catalyzes the formation of N-acyl glycines from acyl-CoA and glycine; potential mechanisms for drugs could include enzyme inhibition or modulation, but no clinical drugs are listed)
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