aldehyde dehydrogenase (NAD+) activity

Definition

Target type: molecularfunction

Catalysis of the reaction: an aldehyde + NAD+ + H2O = an acid + NADH + H+. [EC:1.2.1.3]

Aldehyde dehydrogenase (NAD+) activity is a critical enzyme-catalyzed process involved in the oxidation of aldehydes to their corresponding carboxylic acids, utilizing nicotinamide adenine dinucleotide (NAD+) as a cofactor. This enzymatic activity plays a central role in various metabolic pathways, including the detoxification of harmful aldehydes, the biosynthesis of essential molecules like fatty acids and steroids, and the regulation of cellular redox balance. The catalytic mechanism involves the formation of a covalent intermediate between the enzyme and the aldehyde substrate, followed by the transfer of hydride ions from the aldehyde to NAD+. The resulting carboxylic acid product is then released from the enzyme, leaving NADH, the reduced form of NAD+, as a byproduct. Aldehyde dehydrogenase (NAD+) activity exhibits broad substrate specificity, catalyzing the oxidation of a wide range of aldehydes, including those derived from lipid metabolism, alcohol consumption, and drug metabolism. The activity of this enzyme is tightly regulated by various factors, including substrate availability, cofactor concentration, and cellular redox status. Its dysregulation can lead to the accumulation of toxic aldehydes, contributing to various diseases, including alcoholic liver disease, cancer, and neurodegenerative disorders. Therefore, understanding the molecular function of aldehyde dehydrogenase (NAD+) activity is crucial for developing therapeutic strategies targeting these diseases.'
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Proteins (7)

Compounds (20)