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Alcohol dehydrogenases (EC 22.214.171.124) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones. In humans and many other animals, they serve to break down alcohols which could otherwise be toxic; in yeast and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation.
The CAS number for this type of the enzyme is [9031-72-5].
In humans[edit | edit source]
- CH3CH2OH + NAD+ → CH3CHO + NADH + H+
Alcohol dehydrogenase is also involved in the toxicity of other types of alcohol: for instance, it oxidizes methanol to produce formaldehyde, and ethylene glycol to ultimately yield glycolic and oxalic acids. Humans have at least six slightly different alcohol dehydrogenases. All of them are dimers (consist of two polypeptides), with each dimer containing two zinc ions Zn2+. One of those ions is crucial for the operation of the enzyme: it is located at the catalytic site and holds the hydroxyl group of the alcohol in place.
Most people of East Asian descent have a mutation in their alcohol dehydrogenase gene that makes this enzyme unusually effective at converting ethanol to acetaldehyde, and about half of such people also have a form of acetaldehyde dehydrogenase which is less effective at converting acetaldehyde to acetic acid . This combination causes them to suffer from the alcohol flush reaction, in which acetaldehyde accumulates after drinking, leading to severe and immediate hangover symptoms. These people are therefore less likely to become alcoholics. The drug Antabuse (disulfiram) also prevents the oxidation of acetaldehyde to acetic acid, with the same unpleasant effects for drinkers. It has been used in the treatment of alcoholism.
In yeast and bacteria[edit | edit source]
In yeast and many bacteria, alcohol dehydrogenase plays an important part in fermentation: pyruvate resulting from glycolysis is converted to acetaldehyde and carbon dioxide, and the acetaldehyde is then reduced to ethanol by an alcohol dehydrogenase called ADH1. The purpose of this latter step is the regeneration of NAD+, so that the energy-generating glycolysis can continue. Humans exploit this process to produce alcoholic beverages, by letting yeast ferment various fruits or grains.
The main alcohol dehydrogenase in yeast is larger than the human one, consisting of four rather than just two subunits. It also contains zinc at its catalytic site.
Together with the zinc-containing alcohol dehydrogenases of animals and humans, these enzymes from yeasts and many bacteria form the family of "long-chain"-alcohol dehydrogenases.
Brewer's yeast also has another alcohol dehydrogenase, ADH2, which evolved out of a duplicate version of the chromosome containing the ADH1 gene. ADH2 is used by the yeast to convert ethanol back into acetaldehyde, and it is only expressed when sugar concentration is low. Having these two enzymes allows yeast to produce alcohol when sugar is plentiful (and this alcohol then kills off competing microbes), and then continue with the oxidation of the alcohol once the sugar, and competition, is gone.
Iron-containing alcohol dehydrogenases[edit | edit source]
A third family of alcohol dehydrogenases, unrelated to the above two, are iron-containing ones. They occur in bacteria, and an (apparently inactive) form has also been found in yeast. In comparison to enzymes the above families, these enzymes are oxygen-sensitive.
Other alcohol dehydrogenase types[edit | edit source]
A further class of alcohol dehydrogenases belongs to quinoenzymes and requires quinoid cofactors (e. g. pyrroloquinoline quinone, PQQ) as enzyme-bound electron acceptors. A typical example for this type of enzyme is methanol dehydrogenase of methylotrophic bacteria.
Applications[edit | edit source]
In biotransformation: Alcohol dehydrogenases are often used for the synthesis of enantiomerically pure stereoisomers of chiral alcohols. In contrast to the chemical process, the enzymes yield directly the desired enatiomer of the alcohol by reduction of the corresponding ketone.
See also[edit | edit source]
[edit | edit source]
- PDBsum has links to three-dimensional structures of various alcohol dehydrogenases contained in the Protein Data Bank
- ExPASy contains links to the alcohol dehydrogenase sequences in Swiss-Prot, to a Medline literature search about the enzyme, and to entries in other databases.
- BRENDA most comprehensive compilation of information and literature references about the enzyme; requires payment for commercial users
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- Xiao Q, Weiner H, Crabb DW (1996). The mutation in the mitochondrial aldehyde dehydrogenase (ALDH2) gene responsible for alcohol-induced flushing increases turnover of the enzyme tetramers in a dominant fashion. J. Clin. Invest. 98 (9): 2027-32.