InterPro domain: IPR014183

Class III alcohol dehydrogenases (ADH3) ( 1.1.1.1 ) tend to show poor activity for ethanol among their various substrate alcohols. They catalyze the oxidation and reduction of a wide variety of substrates that include S-(hydroxymethyl)glutathione (HMGSH), S-nitrosoglutathione, and long chain primary alcohols and aldehydes [ 1 ]. The enzyme was previously designated as glutathione-dependent formaldehyde dehydrogenase, as it acts as a HMGSH dehydrogenase ( 1.1.1.284 ). ADH3 oxidizes HMGSH to S-formylglutathione, which is then hydrolyzed to glutathione and formate by a hydrolase [ 2 , 3 ]. S-(hydroxymethyl)glutathione can form spontaneously from formaldehyde and glutathione, and constitutes a cellular strategy for sequestering and metabolizing highly toxic formaldehyde [ 4 ].

1. Human liver class III alcohol and glutathione dependent formaldehyde dehydrogenase are the same enzyme. Biochem. Biophys. Res. Commun. 178, 1371-7
2. Expression of formaldehyde dehydrogenase and S-formylglutathione hydrolase activities in different rat tissues. Adv. Exp. Med. Biol. 414, 365-71
3. Purification and characterization of S-formylglutathione hydrolase from human, rat and fish tissues. Adv. Exp. Med. Biol. 372, 427-33
4. Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation. Biochemistry 41, 15189-94