Alcohol dehydrogenase class-3 (ADH5)

Alcohol dehydrogenase class-3 (ADH5), also known as formaldehyde dehydrogenase and S-nitrosoglutathione reductase, is an enzyme of the medium-chain dehydrogenase/reductase family. It primarily catalyzes the glutathione-dependent oxidation of formaldehyde and the reduction of S-nitrosoglutathione, playing a key role in detoxification of these reactive metabolites[1][3][5]. In humans, the enzyme forms a homodimer with each subunit binding two zinc atoms, essential for structural stability and catalysis. ADH5 is widely expressed and localizes to both the cytoplasm and nucleus. Unlike other alcohol dehydrogenases, it does not efficiently metabolize ethanol or retinoids. Its activity is crucial for cellular defense against formaldehyde-induced DNA damage, maintenance of S-nitrosothiol balance, and nitrogen oxide metabolism[1][5]. Dysfunction or genetic variation in ADH5 has been implicated in increased susceptibility to formaldehyde toxicity, carcinogenesis, and disorders involving redox imbalance[1][3][5].

Other names

Formaldehyde dehydrogenaseS-nitrosoglutathione reductaseClass III alcohol dehydrogenaseGlutathione-dependent formaldehyde dehydrogenase

Inhibition of the enzymatic oxidation of formaldehyde; Blockade of S-nitrosoglutathione reduction