aminobutyraldehyde dehydrogenase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: 4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+. [EC:1.2.1.19]

Aminobutyraldehyde dehydrogenase (ALDH) activity catalyzes the oxidation of 4-aminobutyraldehyde (4-ABAL) to gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the central nervous system. This reaction involves the transfer of a hydride ion from 4-ABAL to the nicotinamide adenine dinucleotide (NAD+) cofactor, resulting in the formation of NADH and GABA. ALDH enzymes are typically tetrameric proteins containing a Rossmann fold, which is a common structural motif in nucleotide-binding proteins. The active site of ALDH enzymes contains a catalytic cysteine residue that is essential for the oxidation reaction. The mechanism of the reaction involves the formation of a covalent intermediate between the cysteine residue and 4-ABAL, followed by the transfer of a hydride ion from the intermediate to NAD+. The reaction is highly specific for 4-ABAL, and ALDH enzymes are not known to act on other aldehydes. The activity of ALDH enzymes is important for maintaining the balance of GABA in the brain, and mutations in ALDH genes have been linked to neurodevelopmental disorders.'
"

Proteins (1)

Compounds (12)