A3263

Alcohol Dehydrogenase from Saccharomyces cerevisiae

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

• Synonym(s): ADH1, ADH, Alcohol Dehydrogenase from yeast, Alcohol:NAD⁺ oxidoreductase
• CAS Number: 9031-72-5
• Enzyme Commission number: 1.1.1.1 (BRENDA, IUBMB)
• EC Number: 232-870-4
• MDL number: MFCD00081305
• UNSPSC Code: 12352204
• NACRES: NA.54

Properties

• biological source: bakers yeast
• form: powder
• specific activity: ≥300 units/mg protein
• mol wt: ~141,000 (four subunits)
• purified by: crystallization
• storage condition: (Tightly closed. Dry)
• greener alternative product characteristics: Waste Prevention; Design for Energy Efficiency; Learn more about the Principles of Green Chemistry.
• sustainability: Greener Alternative Product
• color: beige
• optimum pH: 8.6-9.0
• suitability: suitable for recycling micro-assay of β-NAD and β-NADH
• UniProt accession no.: A0A3G3NDH9; S5RCH3; S5RK20; S5S176
• greener alternative category: Enabling,
• storage temp.: −20°C

Description

General description

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.

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Application

Alcohol Dehydrogenase from Saccharomyces cerevisiae has been used for the determination of NAD⁺ and NADH concentrations.

Biochem/physiol Actions

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.

K_M (ethanol) = 2.1 × 10^-2 M
K_M (methanol = 1.3 × 10^-1 M
K_M (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: E^1% = 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.

Specifications

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.

Unit Definition

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

Physical form

Solids containing <2% citrate buffer salts

Safety Information

• pictograms: GHS08
• signalword: Danger
• hcodes: H334
• pcodes: P261 - P284 - P501
• Hazard Classifications: Resp. Sens. 1
• Storage Class: 11 - Combustible Solids
• wgk_germany: WGK 1
• flash_point_f: Not applicable
• flash_point_c: Not applicable
• ppe: Eyeshields, Gloves, type N95 (US)