Target type: molecularfunction
Catalysis of the reaction: S-(hydroxymethyl)glutathione + NAD+ = S-formylglutathione + NADH + H+. [RHEA:19985]
S-(hydroxymethyl)glutathione dehydrogenase (NAD+) is an enzyme that catalyzes the oxidation of S-(hydroxymethyl)glutathione to formaldehyde and glutathione. This reaction is important in the detoxification of formaldehyde, a toxic compound that is produced as a byproduct of many metabolic processes. The enzyme uses NAD+ as a cofactor, which is reduced to NADH during the reaction. The enzyme is found in a variety of organisms, including bacteria, fungi, and mammals. It is thought to play a role in protecting cells from oxidative stress and in maintaining cellular redox homeostasis. The reaction mechanism of the enzyme involves the formation of a covalent intermediate between the enzyme and the substrate. This intermediate is then hydrolyzed to release formaldehyde and glutathione. The enzyme is highly specific for S-(hydroxymethyl)glutathione and does not catalyze the oxidation of other glutathione derivatives. The enzyme is inhibited by formaldehyde, glutathione, and NADH. S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity is regulated by a variety of factors, including the concentration of substrates, cofactors, and inhibitors. The enzyme is also regulated by post-translational modifications, such as phosphorylation.'
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Protein | Definition | Taxonomy |
---|---|---|
Alcohol dehydrogenase class-3 | An alcohol dehydrogenase class-3 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P11766] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
tetramethylene sulfoxide | tetrahydrothiophenes | ||
isovaleramide | isovaleramide: inhibits liver alcohol dehydrogenases | ||
n6022 | N6022: inhibits S-nitrosoglutathione reductase; structure in first source |