S-formylglutathione hydrolase (ESD)

S-formylglutathione hydrolase (Esterase D, ESD) is a serine hydrolase enzyme with an alpha/beta-hydrolase fold, primarily involved in the detoxification of formaldehyde by catalyzing the hydrolysis of S-formylglutathione to glutathione and formate. It is active toward multiple substrates, including O-acetylated sialic acids, potentially contributing to sialic acid recycling. The ESD gene is located near the RB1 gene on chromosome 13q14 and is widely used as a genetic marker for retinoblastoma and Wilson's disease. While its physiological substrate is S-formylglutathione, the enzyme shows broad substrate specificity, and its activity is essential for cellular processes related to aldehyde detoxification. There are currently no direct drugs targeting ESD, and its main clinical application is as a biomarker rather than a therapeutic target[1][2][4].

Other names

Esterase DFGHESDEsterase D/formylglutathione hydrolaseMethylumbelliferyl-acetate deacetylaseFLJ11763Testicular tissue protein Li 66

Not applicable for current therapeutics; no direct drugs known to target ESD. The enzyme catalyzes the hydrolysis of S-formylglutathione in formaldehyde detoxification, and acts as a serine hydrolase[2][4]