alcohol dehydrogenase

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Related to alcohol dehydrogenase: Aldehyde dehydrogenase

al·co·hol de·hy·dro·gen·ase (ADH),

(al'kŏ-hol dē-hi-droj'e-nās),
An oxidoreductase that reversibly converts an alcohol to an aldehyde (or ketone) with NAD+ as the hydride acceptor; for example, ethanol + NAD+ ⇄ acetaldehyde + NADH.
See also: alcohol dehydrogenase (acceptor), alcohol dehydrogenase (NADP+).

alcohol dehydrogenase

/al·co·hol de·hy·dro·gen·ase/ (ADH) (de-hi´dro-jen-ās) an enzyme that catalyzes the reversible oxidation of primary or secondary alcohols to aldehydes; the reaction is the first step in the metabolism of alcohols by the liver.

alcohol dehydrogenase

Any of a class of enzymes that catalyze the oxidation of alcohols to aldehydes or ketones.

al·co·hol de·hy·dro·gen·ase

(ADH) (al'kŏ-hol dē-hī-droj'en-ās)
An oxidoreductase that reversibly converts an alcohol to an aldehyde (or ketone) with NAD+ as the H acceptor. For example, ethanol + NAD+↔ acetaldehyde+ NADH. Plays an important role in alcoholism.


an enzyme that mobilizes the hydrogen of a substrate so that it can pass to a hydrogen acceptor, such as NAD+ or FAD+.

alcohol dehydrogenase
dimeric enzyme protein of the liver catalyzing the NAD+-linked dehydrogenation of ethanol to acetaldehyde.
glucose-6-phosphate dehydrogenase
see glucose-6-phosphate dehydrogenase.
glutamate dehydrogenase (GD), glutamic dehydrogenase
an enzyme that catalyzes the reversible reaction of glutamic acid into 2-oxoglutaric acid and ammonia. High concentrations occur in the liver of sheep, cattle, horses and dogs. Serum levels are useful in detecting hepatocellular damage in ruminants.
l-iditol dehydrogenase (ID)
a liver specific enzyme; serum determinations have been used in the horse to detect hepatocellular damage. Called also sorbitol dehydrogenase, SDH.
isocitrate dehydrogenase (ICD)
an enzyme found in high concentrations in many tissues. Two major forms of the enzyme, an NAD+-dependent ICD associated with the mitochondrial TCA cycle and a NADP+-dependent ICD associated with fat synthesis in adipose tissue and lactating mammary gland of ruminants or with steroidogenesis in endocrine tissues. Serum levels have been used to detect hepatocellular damage, but it is not highly specific.
lactate dehydrogenase (LDH), lactic acid dehydrogenase
an enzyme that catalyzes the interconversion of lactate and pyruvate. It is widespread in tissues and is particularly abundant in kidney, skeletal muscle, liver and myocardium. It appears in elevated concentrations when these tissues are injured. See also mouse lactic dehydrogenase elevating virus.
lactate dehydrogenase agent
polyol dehydrogenase
sorbitol dehydrogenase (SDH)
References in periodicals archive ?
Alcohol metabolism in American Indians and whites: Lack of racial differences in metabolic rate and liver alcohol dehydrogenase.
Alcohol dehydrogenases make up one of the important enzyme classes in this field and can be used for the cost efficient synthesis of chiral alcohols from ketones with extraordinary purities.
Hepatic alcohol dehydrogenase and acetaldehyde dehydrogenase enzyme activities: Twenty four male rats weighing between 250-275 g were divided into 3 groups of 8 each.
One would predict that any new amino acid sequence derived from a genome sequence project that exhibits high sequence identity and similarity to these alcohol dehydrogenase sequences will exhibit the same structure and function.
KEY WORDS: alcohol dehydrogenase, aldehyde dehydrogenase, chloral hydrate, genetic variability, human hepatocytes, metabolism, risk assessment, trichloroacetate, trichloroethylene.
Ethanol conversion to acetaldehyde in the red blood cell has been shown to occur in the presence of oxyhemoglobin acting as an alcohol dehydrogenase.
TOKYO - Japanese researchers said Tuesday that men who have an alcohol dehydrogenase genotype that decomposes alcohol more slowly and who tend to drink more are twice as likely to suffer a cerebral infarction.
According to the Harvard Women's Health Watch (December 2003), women become more intoxicated while consuming lesser amounts of alcohol due to higher proportion of fat to water ratio and the lower secretions of alcohol dehydrogenase, an enzyme that breaks down the alcohol.
The gene variant codes for a slow-acting form of alcohol dehydrogenase, an alcohol-metabolizing enzyme.
Approximately 80% of ethanol is oxidized through alcohol dehydrogenase into acetaldehyde, a carcinogen.
Of the enzyme systems initially assayed, alcohol dehydrogenase (ADH); lactate dehydrogenase (LDH); malate dehydrogenase (MDH); phosphohexose isomerase (PHI/PGI); and 6-phosphogluconate dehydrogenase (6-PGD) resolved consistently.
Syngenta Participations AG (Basle, Switzerland) has patented a DNA construct comprising an expression cassette having a constitutive promoter which functions in plant cells operably linked to a maize alcohol dehydrogenase intron, a DNA sequence of a gene encoding a Cry 1Ab protein, and a terminator functional in plants and optionally further comprising a second cassette including a promoter which functions in plants operably linked to a maize alcohol dehydrogenase intron, a DNA sequence of a gene encoding for phosphinothricin acetyl transferase, and a terminator functional in plants wherein the two cassettes are transcribed in the same direction.

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