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Alcohol dehydrogenase


Official Full Name
Alcohol dehydrogenase
Background
Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.
Synonyms
aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1

Catalog
Product Name
EC No.
CAS No.
Source
Price
CatalogNATE-1900
EC No.EC 1.1.1.1
CAS No.9031-72-5
SourceZymomonas mobil...
CatalogNATE-1786
EC No.EC 1.1.1.1
CAS No.9031-72-5
SourceE. coli
CatalogEXWM-0001
EC No.EC 1.1.1.1
CAS No.9031-72-5
Source
CatalogNATE-1584
EC No.EC 1.1.1.1
CAS No.9031-72-5
SourceE. coli
CatalogNATE-1197
EC No.EC 1.1.1.2
CAS No.
SourceHuman
CatalogNATE-0975
EC No.
CAS No.9031-72-5
SourceYeast
CatalogNATE-0034
EC No.EC 1.1.1.1
CAS No.9031-72-5
Source
CatalogNATE-0035
EC No.EC 1.1.1.1
CAS No.9031-72-5
SourceSaccharomyces c...
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CatalogCEI-0398
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EC No.
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Alcohol dehydrogenase, which is abundantly present in human and animal livers, plants and microbial cells, is a key enzyme for the metabolism of short-chain alcohols in organisms. It plays an important role in many physiological processes. It is a zinc-containing metalloenzyme with wide substrate specificity.

Introductions

Alcohol dehydrogenase, abbreviated as ADH, is abundant in human and animal liver, plant and microbial cells. It is a zinc-containing metalloenzyme with wide substrate specificity. Alcohol dehydrogenase can use nicotinamide adenine dinucleotide (NAD) as a coenzyme to catalyze the reversible reaction between primary alcohols and aldehydes: CH3CH2OH+ NAD+→ CH3CHO +NADH+ H+. In humans and mammals, alcohol dehydrogenase and acetaldehyde dehydrogenase (ALDH) constitute the alcohol dehydrogenase system, which participates in the metabolism of alcohol in the body and is an important metabolic enzyme in humans and animals. As a key enzyme for the metabolism of short-chain alcohols in organisms, it plays an important role in many physiological processes. It is a widely specific zinc-containing metalloenzyme. Alcohol dehydrogenase alcohol oxidation system is a major way to metabolize alcohol in the liver. Alcohol dehydrogenase oxidation system includes alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH).

Protein structure of alcohol dehydrogenase Figure 1. Protein structure of alcohol dehydrogenase.

Properties

Alcohol dehydrogenase is a dimer with a mass of 80kDa, including a set of isoenzymes, which can convert ethanol into acetaldehyde. In mammals, this is a redox reaction involving the coenzyme nicotinamide adenine dinucleotide (NAD+). Alcohol dehydrogenase is responsible for catalyzing the oxidation of primary and secondary alcohols into aldehydes and ketones, and can also affect their reverse reactions. But for primary alcohols, this catalytic effect is not strong, while for secondary alcohols and cyclic alcohols, the catalytic effect is strong. The optimal pH value of alcohol dehydrogenase is 7.0-10.0, the enzyme activity reaches the maximum when the pH value is 8.0, and the enzyme activity is relatively stable when the pH value is 7.0; the optimal temperature of ADH is 37℃ and the temperature is 30-40 The enzyme activity is relatively stable at ℃, and the enzyme activity drops sharply after the temperature exceeds 45℃.

Application

Clinical significance

Reference

  1. Gutheil WG.; et al. Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase. Biochemistry. 31 (2): 475–81.

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