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

n.
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.

dehydrogenase

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 dehydrogenase F allele frequencies Accelerated Control Parental Accelerated p = 1.
High blood alcohol lev(,is in women; the role of decreased gastric alcohol dehydrogenase and first pass metabolism.
Genetic polymorphism of alcohol dehydrogenase in Europeans: The ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1.
Evidence of a competitive effect of narezode on EG metabolism by alcohol dehydrogenase comes from the work of Proctor and Schlesser (18), who showed that, in healthy volunteers, oral narezode significantly reduced the rate of elimination of moderate doses of ethanol, which is also metabolized through alcohol dehydrogenase.
18) This region contains a cluster of 7 genes encoding for alcohol dehydrogenases (ADH), including 3 Class I genes--ADH1A, ADH1B, and ADH1C--coding for the corresponding proteins that play a major role in alcohol metabolism.
Hines' team examined the alcohol dehydrogenase genes of 396 men in that study who had suffered a heart attack and 770 others who hadn't.
Ethanol adaptation and alcohol dehydrogenase polymorphism in Drosophila: from phenotypic function to genetic structure.
For example, the genes that code for the alcohol-metabolizing enzyme alcohol dehydrogenase are of the same size and base sequence in most individuals.
The primary enzymes involved in alcohol metabolism are alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH).
This present study investigated whether pharmacokinetic interactions between kava constituents and alcohol via alcohol dehydrogenase (ADH) inhibition by individual kavalactones might explain its claimed hepatotoxic effects.
In addition, functional polymorphisms of alcohol dehydrogenase (ADH2) and aldehyde dehydrogenase (ALDH2) genes have been shown to have a significant impact on alcohol metabolism in the liver, and thus, may contribute to vulnerability to alcohol abuse and dependence, alcohol-related liver diseases and cancers.
The rate-limiting step in alcohol metabolism is controlled by alcohol dehydrogenase.

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