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The inactivating ALDH2*2 mutation is "the most common single point mutation in humans". [14] This mutation is found in very few White people, but about 50% of East Asians are heterozygous for this mutation. The ALDH2*2 allele encodes lysine instead of glutamic acid at amino acid 487, [15] distorting the NAD+ binding site.
These symptoms are indicative of a medical condition known as the alcohol flush reaction, also known as “Asian flush” or “Oriental flushing syndrome”. [8] There is a mutant form of aldehyde dehydrogenase, termed ALDH2*2, wherein a lysine residue replaces a glutamate in the active site at position 487 of ALDH2. [9]
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]
Oxidoreductases, enzymes that catalyze oxidation-reduction reactions, constitute Class EC 1 of the IUBMB classification of enzyme-catalyzed reactions. [2] Any of these may be called dehydrogenases, especially those in which NAD + is the electron acceptor (oxidant), but reductase is also used when the physiological emphasis on reduction of the substrate, and oxidase is used only when O 2 is the ...
Individuals with two copies of the ALDH2*2 allele are known to have high blood acetaldehyde levels and experience “hangover” symptoms such as heart palpitations for longer durations, even with low alcohol consumption. [15] [16] [2] Individuals who work with DMF have shown a dose-related increase in alcohol intolerance complaints. [26]
ALDH1a2 belongs to the aldehyde dehydrogenase family of proteins, and specifically the ALDH1 family. The product of this gene, ALDH1a2, is an enzyme that catalyzes the synthesis of all-trans retinoic acid (RA) from retinaldehyde in a NAD-dependent manner. [7]
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 monomer of ALDH2 tetramer.
Tryptophan for instance is doubly oxidized to generate ROSs such as H 2 O 2, which elicit further oxidation and adduction. [24] Nevertheless, the abundance of ALDH3A1 in the cornea ensures that this suicide response neither impedes with aldehyde metabolism nor leads to the formation of insoluble aggregates that would affect the transparency of ...