Abhydrolase domain-containing protein 10 (ABHD10)

Abhydrolase domain-containing protein 10 (ABHD10) is a mitochondrial serine hydrolase with dual roles in both drug metabolism and regulation of mitochondrial redox homeostasis. In the liver, it catalyzes the hydrolysis (deglucuronidation) of acyl-glucuronide metabolites such as mycophenolic acid acyl-glucuronide and probenecid acyl-glucuronide, thus participating in the detoxification of potentially harmful drug metabolites. ABHD10 also functions as an S-depalmitoylase within mitochondria, removing palmitoyl groups from substrate proteins such as peroxiredoxin-5, thereby modulating their antioxidant capacity and contributing to mitochondrial oxidative stress defense. The enzyme is characterized by a canonical α/β hydrolase fold and a catalytic triad necessary for its activity. Loss or inhibition of ABHD10 results in increased cellular oxidative stress and impaired drug detoxification, which can increase sensitivity to drug-induced toxicity[1][2][3].

Other names

Palmitoyl-protein thioesterase ABHD10, mitochondrialMycophenolic acid acyl-glucuronide esterase, mitochondrialAcyl-protein thioesterase ABHD10Alpha/beta hydrolase domain-containing protein 10FLJ11342Abhydrolase domain containing 10

Enzymatic hydrolysis (deglucuronidation) of drug acyl-glucuronides; Enzymatic S-depalmitoylation of mitochondrial protein targets, modulating their function