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The ALDH2 gene is about 44 kbp in length and contains at least 13 exons which encode 517 amino acid residues. Except for the signal NH2-terminal peptide, which is absent in the mature enzyme, the amino acid sequence deduced from the exons coincided with the reported primary structure of human liver ALDH2.
Aldehyde dehydrogenase is a polymorphic enzyme [3] responsible for the oxidation of aldehydes to carboxylic acids. [3] There are three different classes of these enzymes in mammals: class 1 (low K m, cytosolic), class 2 (low K m, mitochondrial), and class 3 (high K m, such as those expressed in tumors, stomach, and cornea).
ALDH2, which has a lower K M for acetaldehydes than ALDH1 and acts predominantly in the mitochondrial matrix, is the main enzyme in acetaldehyde metabolism and has three genotypes. A single point mutation (G → A) at exon 12 of the ALDH2 gene causes a replacement of glutamate with lysine at residue 487, resulting in the ALDH2K enzyme. [8]
Aldehyde dehydrogenase 1 family, member A2, also known as ALDH1A2 or retinaldehyde dehydrogenase 2 (RALDH2), is an enzyme that in humans is encoded by the ALDH1A2 gene. [ 5 ] [ 6 ] Function
People have various ALDH2 alleles. ALDH2*1 is a common allele , but about 40% of people of East Asian ethnicity have one or two copies of the dominant ALDH2*2 instead, which causes ALDH2 deficiency. If deficient people drink ethanol, they suffer from alcohol flush reaction due to acetaldehyde accumulation. [3] Four Alda-1 molecules bind to each ...
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This protein belongs to the aldehyde dehydrogenases family of proteins and is a member of the ALDH1 subfamily (including ALDH1A2, ALDH1A3, ALDH1B1, ALDH2). Aldehyde dehydrogenase isozymes are NAD(P)-dependent dehydrogenases that catalyze the oxidation of an aldehyde into the corresponding carboxylic acid while reducing NAD+ or NADP+.
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