Page last updated: 2024-10-24

S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity

Definition

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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Proteins (1)

ProteinDefinitionTaxonomy
Alcohol dehydrogenase class-3An alcohol dehydrogenase class-3 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P11766]Homo sapiens (human)

Compounds (3)

CompoundDefinitionClassesRoles
tetramethylene sulfoxidetetrahydrothiophenes
isovaleramideisovaleramide: inhibits liver alcohol dehydrogenases
n6022N6022: inhibits S-nitrosoglutathione reductase; structure in first source