ABHD10 Human

ABHD10 is a mitochondrially-localized enzyme that acts primarily in liver cells as a hydrolase . The recombinant human ABHD10 protein is typically expressed in Escherichia coli (E. coli) and purified using conventional chromatography techniques . The recombinant form of this protein often includes a His-tag at the N-terminus to facilitate purification and detection .

ABHD10 functions as an acyl-protein thioesterase, which means it hydrolyzes fatty acids from acylated residues in proteins . This activity is crucial for regulating the mitochondrial S-depalmitoylation of peroxiredoxin-5 (PRDX5), a key antioxidant protein. By modulating the mitochondrial antioxidant ability, ABHD10 plays a vital role in maintaining cellular health and protecting against oxidative stress .

Additionally, ABHD10 catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, an active metabolite of the immunosuppressant drug mycophenolate . This function is particularly important in the context of drug metabolism and detoxification.

Mutations or dysregulation of the ABHD10 gene have been associated with various diseases, including epilepsy, familial adult myoclonic epilepsy, and septooptic dysplasia . Understanding the function and regulation of ABHD10 is therefore critical for developing therapeutic strategies for these conditions.

Recombinant human ABHD10 protein is widely used in research to study its biochemical properties and physiological roles. It is also utilized in drug development and screening assays to identify potential inhibitors or modulators of its activity .