A3263
Alcohol Dehydrogenase from Saccharomyces cerevisiae
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
Produits recommandés
Source biologique
bakers yeast
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
Waste Prevention
Design for Energy Efficiency
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sustainability
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Couleur
beige
pH optimal
8.6-9.0
Adéquation
suitable for recycling micro-assay of β-NAD and β-NADH
Numéro d'accès UniProt
Autre catégorie plus écologique
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.
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in fuel cell research. For more information see the article in biofiles.
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.
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in fuel cell research. For more information see the article in biofiles.
Application
Alcohol Dehydrogenase from Saccharomyces cerevisiae has been used for the determination of NAD+ and NADH concentrations.
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)
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. It is also implicated in the production of alcohol from amino acid breakdown via the Ehrlich pathway.
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
Anticorps
Réf. du produit
Description
Tarif
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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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)
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
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
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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