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A7011

Sigma-Aldrich

Alcohol Dehydrogenase from Saccharomyces cerevisiae

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≥300 units/mg protein, lyophilized powder (contains buffer salts), Mw 141-151 kDa

Synonyme(s) :

ADH1, Adh1p, SCAD, YDAH-1, YIM-1, ADH, Alcohol Dehydrogenase from yeast, Alcohol:NAD+ oxidoreductase

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148,00 $
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7500 UNITS
75,80 $
15000 UNITS
92,70 $
30000 UNITS
148,00 $
75000 UNITS
321,00 $
150000 UNITS
599,00 $
300000 UNITS
919,00 $

About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

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Source biologique

Saccharomyces cerevisiae

Niveau de qualité

Forme

lyophilized powder (contains buffer salts)

Activité spécifique

≥300 units/mg protein

Poids mol.

Mw 141-151 kDa

Produit purifié par

crystallization

Conditions de stockage

(Keep container tightly closed in a dry and well-ventilated place.)

Caractéristiques du produit alternatif plus écologique

Waste Prevention
Design for Energy Efficiency
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Couleur

white to light yellow-brown, Light brown

pH optimal

8.6-9.0

Solubilité

H2O: soluble 1.0 mg/mL, clear to slightly hazy, colorless to faintly yellow
soluble

Numéro d'accès UniProt

Application(s)

diagnostic assay manufacturing

Autre catégorie plus écologique

Conditions d'expédition

dry ice

Température de stockage

−20°C

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Description générale

Research area: Neuroscience

Yeast alcohol dehydrogenase 1 (ADH1) belongs to the family of zinc-containing alcohol dehydrogenases. It is a homotetramer with each subunit containing one catalytic domain and coenzyme-binding domain.[1]

Application

Alcohol dehydrogenase has been used along with lactic dehydrogenase for the enzymatic reduction of acetaldehyde using sodium(R,S)-[2-3H] lactate.[2] It has also been used to study the inhibitory effect of zinc-chelated silymarin flavonolignans on yeast alcohol dehydrogenase.[3]

Ethanol concentration can be determined colorimentrically by monitoring the enzymatic reduction of NAD using alcohol dehydrogenase after preremoval of the aldehyde group.[4]

Actions biochimiques/physiologiques

ADH (alcohol dehydrogenase) is one of the first enzymes to be isolated and purified. NAD+ is its coenzyme. Three isozymes of yeast ADH, that is, yeast alcohol dehydrogenase-1, 2 and 3 (YADH-1, -2, -3) have been identified. YADH-1 is expressed during anaerobic fermentation, YADH-2 is expressed in the cytoplasm and YADH-3 is localized to the mitochondria. A 141kDa tetramer containing 4 equal subunits. The active site of each subunit contains a zinc atom. Each active site also contains 2 reactive sulfhydryl groups and a histidine residue.

Isoelectric point: 5.4-5.8

Optimal pH: 8.6-9.0

Substrates: Yeast ADH is most active with ethanol and its activity decreases as the size of the alcohol increases or decreases. Branched chain alcohols and secondary alcohols also have very low activity.

KM (ethanol) = 2.1 × 10-2 M
KM (methanol = 1.3 × 10-1 M
KM (isopropanol) = 1.4 × 10-1 M

Inhibitors: Compounds that react with free sulfhydryls, including N-alkylmaleimides and iodoacetamide.
Zinc chelator inhibitors, including 1,10-phenanthroline,
8-hydroxyquinoline, 2,2′-dipyridyl, and thiourea.
Substrate analogue inhibitors, including β-NAD analogs, purine and pyrimidine derivatives, chloroethanol, and fluoroethanol.

Extinction Coefficient: E1% = 14.6 (water, 280 nm)
Yeast alcohol dehydrogenase 1 (YADH1) catalyzes the conversion of acetaldehyde to ethanol during glucose fermentation pathway.[5] It is also implicated in the production of alcohol from amino acid breakdown via the Ehrlich pathway.[6]

Attention

Contains bound β-NAD and β-NADH and is not suitable for the recycling microassay of β-NAD and β-NADH. If you require ADH for this purpose, see Catalog No. A3263.

Définition de l'unité

One unit will convert 1.0 μmole of ethanol to acetaldehyde per min at pH 8.8 at 25 °C.

Forme physique

Solids containing ≤ 2% citrate buffer salts

Notes préparatoires

Dissolves in water at a concentration of 1 mg/mL to form a clear to slightly hazy, colorless to faintly yellow colored solution.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Stereospecificity of the oxidation of ethanol by catalase.
R J Corrall et al.
The Journal of biological chemistry, 249(10), 3181-3182 (1974-05-25)
Václav Tvrdý et al.
Nutrients, 13(12) (2021-12-29)
Silymarin is known for its hepatoprotective effects. Although there is solid evidence for its protective effects against Amanita phalloides intoxication, only inconclusive data are available for alcoholic liver damage. Since silymarin flavonolignans have metal-chelating activity, we hypothesized that silymarin may
Savarimuthu Baskar Raj et al.
Biochemistry, 53(36), 5791-5803 (2014-08-27)
Yeast (Saccharomyces cerevisiae) alcohol dehydrogenase I (ADH1) is the constitutive enzyme that reduces acetaldehyde to ethanol during the fermentation of glucose. ADH1 is a homotetramer of subunits with 347 amino acid residues. A structure for ADH1 was determined by X-ray
Mark D Redwood et al.
FEMS microbiology letters, 278(1), 48-55 (2007-11-13)
Escherichia coli can perform at least two modes of anaerobic hydrogen metabolism and expresses at least two types of hydrogenase activity. Respiratory hydrogen oxidation is catalysed by two 'uptake' hydrogenase isoenzymes, hydrogenase -1 and -2 (Hyd-1 and -2), and fermentative
Cheol Woong Ha et al.
Nucleic acids research, 42(13), 8486-8499 (2014-07-02)
In Saccharomyces cerevisiae, the stability of highly repetitive rDNA array is maintained through transcriptional silencing. Recently, a β-1,3-glucanosyltransferase Gas1 has been shown to play a significant role in the regulation of transcriptional silencing in S. cerevisiae. Here, we show that

Protocoles

To measure alcohol dehydrogenase activity, this assay uses β-nicotinamide adenine dinucleotide phosphate and a continuous spectrophotometric rate determination at 340 nm.

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