ABHD10 is a mitochondrial acyl-protein thioesterase that functions as an S-depalmitoylase with critical roles in redox homeostasis and drug metabolism 1. Its primary enzymatic function involves hydrolyzing palmitate and other fatty acids from protein substrates, regulating the post-translational lipid modification status of target proteins 1. Mechanistically, ABHD10 catalyzes S-depalmitoylation of peroxiredoxin-5 (PRDX5), a key mitochondrial antioxidant protein, thereby modulating mitochondrial antioxidant capacity 1. Beyond redox regulation, ABHD10 catalyzes deglucuronidation of acyl-glucuronides, including mycophenolic acid acyl-glucuronide and probenecid acyl-glucuronide, functioning as a detoxification enzyme for immunosuppressant and uricosuric drug metabolites 23. Disease relevance spans multiple contexts: In alcoholic liver disease, ABHD10 downregulation via ELK-3 signaling increases PRDX5 palmitoylation, driving oxidative stress and hepatocyte dysfunction; ABHD10 overexpression ameliorates liver damage in animal models 4. Additionally, ABHD10 is essential for male fertility, with knockout mice exhibiting sperm motility defects and malformed mitochondrial sheaths due to hyper-palmitoylation of sheath formation factors 5. Clinically, ABHD10 represents a therapeutic target for hepatotoxicity and potential biomarker for cardiac conduction through associations with PR interval 6.