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A7011 Sigma

Alcohol Dehydrogenase from Saccharomyces cerevisiae

lyophilized powder (contains buffer salts), ≥300 units/mg protein

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

Properties

Related Categories 1.1.x.x Acting on hydroxyl groups, 1.x.x.x Oxidoreductases, Alcohol Metabolism, Application Index, Biochemicals and Reagents,
Quality Level   PREMIUM
form   lyophilized powder (contains buffer salts)
purified by   crystallization
composition   Protein, ≥90% E1%/280
solubility   H2O: soluble1.0 mg/mL, clear to slightly hazy, colorless to faintly yellow
suitability   suitable for conventional determination of β-NAD, β-NADH, ethanol and acetaldehyde
Featured Industry   Diagnostic Assay Manufacturing
shipped in   dry ice
storage temp.   −20°C

Description

Caution

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.

Preparation Note

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

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

Application

Alcohol dehydrogenase has been used along with lactic dehydrogenase for the enzymatic reduction of acetaldehyde using sodium(R,S)-[2-3H] lactate.1 Ethanol concentration can be determined colorimentrically by monitoring the enzymatic reduction of NAD using alcohol dehydrogenase after preremoval of the aldehyde group.2

Biochem/physiol Actions

A 141 kDa 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)

Price and Availability


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