GLYAT (glycine-N-acyltransferase) is a mitochondrial acyltransferase that catalyzes the conjugation of acyl groups from acyl-CoA substrates to glycine, with preference for benzoyl-CoA as an acyl donor 1. The enzyme functions as a phase II detoxification enzyme, conjugating both xenobiotics (benzoic acid, salicylic acid) and endogenous organic acids (isovaleric acid) to form N-acylglycines 2. Mechanistically, GLYAT employs a catalytic mechanism wherein a critical glutamate residue deprotonates glycine to facilitate nucleophilic attack on the acyl-CoA substrate 1. Clinically, GLYAT has multiple disease associations. Genetic variants in GLYAT, particularly p.(Gln61Leu), show decreased enzymatic activity with potential pharmacogenetic implications 3. In preeclampsia, placental GLYAT upregulation reduces the bioavailability of salicylic acid, contributing to aspirin nonresponsiveness despite adequate drug metabolism 4. In cancer, decreased GLYAT expression correlates with poor prognosis in both breast cancer and hepatocellular carcinoma, where GLYAT downregulation promotes tumor growth, metastasis, and epithelial-mesenchymal transition via the PI3K/AKT/Snail pathway 56. Genome-wide association studies identified GLYAT variants associated with bone size phenotypes and lean muscle mass, suggesting roles in glucose and energy metabolism 7.