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A3263

Sigma-Aldrich

Alcohol Dehydrogenase from Saccharomyces cerevisiae

greener alternative

powder, ≥300 units/mg protein, mol wt ~141,000 (four subunits)

Synonyme(s) :

ADH1, ADH, Alcohol Dehydrogenase from yeast, Alcohol:NAD+ oxidoreductase

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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

bakers yeast

Niveau de qualité

Forme

powder

Activité spécifique

≥300 units/mg protein

Poids mol.

~141,000 (four subunits)

Produit purifié par

crystallization

Conditions de stockage

(Tightly closed. Dry)

Caractéristiques du produit alternatif plus écologique

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Couleur

beige

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Cet article
A7011G5003A8656
specific activity

≥300 units/mg protein

specific activity

≥300 units/mg protein

specific activity

≥10 units/mg protein (using p-nitrophenyl α-D-glucoside as substrate.)

specific activity

-

suitability

suitable for recycling micro-assay of β-NAD and β-NADH

suitability

-

suitability

-

suitability

-

form

powder

form

lyophilized powder (contains buffer salts)

form

lyophilized powder

form

powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage condition

(Tightly closed. Dry)

storage condition

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

storage condition

-

storage condition

-

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]

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Application

Alcohol Dehydrogenase from Saccharomyces cerevisiae has been used for the determination of NAD+ and NADH concentrations.[2][3][4][5]

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.[6] It is also implicated in the production of alcohol from amino acid breakdown via the Ehrlich pathway.[7]

Caractéristiques

The dried enzyme has been stored for several weeks in a vacuum desiccator with little loss in activity. According to experiments described by A. Kornberg,3 the enzyme can be stored in the frozen state and can be thawed repeatedly without marked loss of activity.

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

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Sexual dimorphism in acute myocardial infarction-induced acute kidney injury: cardiorenal deteriorating effects of ovariectomy in premenopausal female mice
Nada J Habeichi, et al.
Clinical Science (London, England : 1979), 137(1), 47-63 (2023)
N C Jerez et al.
Journal of animal science, 81(4), 997-1003 (2003-05-02)
The objective of this experiment was to determine the effect of prerigor injection of several glycolytic inhibitors on pH, color, tenderness, and related traits of low-value beef cuts. The semimembranosus, triceps brachii, and supraspinatus muscles from each of 10 steer
L Tretter et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 20(24), 8972-8979 (2000-01-11)
In this study we addressed the function of the Krebs cycle to determine which enzyme(s) limits the availability of reduced nicotinamide adenine dinucleotide (NADH) for the respiratory chain under H(2)O(2)-induced oxidative stress, in intact isolated nerve terminals. The enzyme that
Nada J Habeichi et al.
Bioscience reports, 40(6) (2020-06-11)
The impact of cigarette smoking (CS) on kidney homeostasis in the presence of myocardial infarction (MI) in both males and females remains poorly elucidated. C57BL6/J mice were exposed to 2 weeks of CS prior to MI induction followed by 1
The role of zinc in alcohol dehydrogenase. V. The effect of metal-binding agents on thestructure of the yeast alcohol dehydrogenase molecule.
J H KAGI et al.
The Journal of biological chemistry, 235, 3188-3192 (1960-11-01)

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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