Aminobutyraldehyde dehydrogenase

Class of enzymes From Wikipedia, the free encyclopedia

In enzymology, aminobutyraldehyde dehydrogenase (EC 1.2.1.19) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
H2O
H+
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
H2O
H+
 
 

The three substrates of this enzyme are 4-aminobutanal, oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are γ-aminobutyric acid, reduced NADH, and a proton.[1][2][3][4][5]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-aminobutanal:NAD+ 1-oxidoreductase. Other names in common use include gamma-guanidinobutyraldehyde dehydrogenase (ambiguous), ABAL dehydrogenase, 4-aminobutyraldehyde dehydrogenase, 4-aminobutanal dehydrogenase, gamma-aminobutyraldehyde dehydrogenase, 1-pyrroline dehydrogenase, ABALDH, and YdcW. This enzyme participates in the urea cycle and the metabolism of amino groups and beta-alanine.[6]

References

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