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Alcohol Dehydrogenase ( ADH )

Zinc-containing enzyme, this enzyme breaks alcohol down into carbon dioxide, fatty acids, and water. Alcohol Dehydrogenase (ADH), or aldehyde reductase, is an enzyme found in a variety of species ranging from Escherichia coli to Ursus arctos (Brown Bear), from Saccharomyces cerevisiae to, of course, Homo sapiens. ADH is a member of a general classes of enzymes called oxidoreductases.

Dehydrogenases are used as enzymes for the oxidation and reduction of carbonyl groups, respectively alcohols. The enzymes are mostly NAD(P)H-dependent. For the reduction of aldehydes and ketones, baker yeast is often used.Reductions with isolated enzymes: During the reduction of a carbonyl group, the cofactor NAD(P)H - the hydride donor - must be stoichiometrically used, or being regenerated through in situ reduction of NAD(P)+ because of the high costs during the reaction.A possibility for the recycling of NAD(P)H is the use of a second enzyme and a suitable substrate which is oxidized : glucose / glucose dehydrogenases, glucose-6-phosphate / glucose-6-phosphate dehydrogenases and alcohol / alcohol dehydrogenases.


 

 

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