The protein encoded by this gene is a member of the alcohol dehydrogenase family.

Alcohol dehydrogenase is a dimer with a mass of 80 kDa.

This is related to an average higher body mass, but also to the prevalence of high levels of alcohol dehydrogenase in the population.

The latter reaction is again catalyzed by an alcohol dehydrogenase, now operating in the opposite direction.

The removal of ethanol through oxidation by alcohol dehydrogenase in the liver from the human body is limited.

Vennesland had developed a project involving the fate of hydrogen atoms in alcohol dehydrogenase.

Germanium can interfere with such enzymes as lactate and alcohol dehydrogenase.

Alcohol dehydrogenase was first discovered in the mid-1960s in 'Drosophila melanogaster'.

It is metabolised primarily through alcohol dehydrogenase or glucuronyl transferase.

Members of the iron-containing alcohol dehydrogenase family include:

In a recent study Lewis et al., looked at alcohol dehydrogenase genes and their mutations, which humans can have between 0 and 10.

This enzyme is also called perillyl alcohol dehydrogenase.

A periplasmic quinoprotein alcohol dehydrogenase is only present in methylotrophic bacteria.

An enzyme in the liver called alcohol dehydrogenase strips electrons from ethanol to form acetaldehyde.

The main alcohol dehydrogenase in yeast is larger than the human one, consisting of four rather than just two subunits.

Alcohol is metabolized mainly by the group of six enzymes collectively called alcohol dehydrogenase.

Other names in common use include cinnamyl alcohol dehydrogenase, and CAD.

High level of alcohol dehydrogenase activity results in fast transformation of ethanol to more toxic acetaldehyde.

Yeast have low levels of fatty alcohol dehydrogenase.)

These ions can inhibit oxidative enzymes such as yeast alcohol dehydrogenase.

In the brain, alcohol dehydrogenase has a minor role in the oxidation of ethanol to acetaldehyde.

"Nucleotide polymorphism at the alcohol dehydrogenase locus of Drosophila melanogaster".

Alcohol dehydrogenase activity varies between men and women, between young and old, and among populations from different areas of the world.

Isopropyl alcohol is oxidized to form acetone by alcohol dehydrogenase in the liver.

Alcohol dehydrogenase has a higher affinity for ethanol, thus preventing methanol from binding and acting as a substrate.

This protein belongs to the aldehyde dehydrogenase family of proteins.

It inhibits aldehyde dehydrogenase, an enzyme required for breaking down alcohol.

Therefore, it is the first known aldehyde dehydrogenase to show a preference for 9-cis-retinal relative to all-trans-retinal.

There are more genes in the family of alcohol and aldehyde dehydrogenase genes.

It is also an allosteric inhibitor of human liver aldehyde dehydrogenase.

Antiquitin is a member of subfamily 7 in the aldehyde dehydrogenase gene family.

This enzyme is also called aldehyde dehydrogenase (acceptor).

Lactaldehyde is then oxidized to lactic acid by aldehyde dehydrogenase.

Furthermore, the researchers needed a dehydrogenase to replace the aldehyde dehydrogenase capacity of AdhE2.

Aldehyde dehydrogenase is the second enzyme of the major oxidative pathway of alcohol metabolism.

It is not a substrate of that enzyme, and is metabolized by aldehyde dehydrogenase into isovanillic acid.

Pristanal is oxidized by aldehyde dehydrogenase to form pristanic acid (which can then undergo beta-oxidation).

Antiquitin functions as an aldehyde dehydrogenase in the pipecolic acid pathway of lysine catabolism.

The reaction is primarily due to an inherited lack of an enzyme called aldehyde dehydrogenase 2 (ALDH2).

ALDH1L2 is an aldehyde dehydrogenase.

Aldehyde dehydrogenase 2 family (mitochondrial), also known as ALDH2, is a human gene found on chromosome 12.

The levels of alcohol dehydrogenase and aldehyde dehydrogenase in the liver increase in response to long-term alcohol exposure.

Human ALDH1A1 aldehyde dehydrogenase is capable of oxidizing malondialdehyde.

Another enzyme, called aldehyde dehydrogenase, converts the acetaldehyde, in the presence of oxygen, to acetic acid, the main component in vinegar.

Methylglyoxal reductase and aldehyde dehydrogenase convert methylglyoxal into lactaldehyde and, eventually, L-lactate.

The enzyme associated with the chemical transformation from acetaldehyde to acetic acid is aldehyde dehydrogenase 2 family (ALDH2).

Most of the aldophosphamide is oxidised by the enzyme aldehyde dehydrogenase (ALDH) to make carboxyphosphamide.

It turns out that an eye-specific form of a housekeeping enzyme known as aldehyde dehydrogenase was one of the major crystallins filling the squid eye's lens.

Aldehyde dehydrogenase (ALDH) is the only enzyme that catalyses the oxidation of acetaldehyde to acetate.

This is followed by oxidation by aldehyde dehydrogenase to 5-HIAA, the indole acetic acid derivative.