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A7011 Sigma

Alcohol Dehydrogenase from Saccharomyces cerevisiae Green Alternative

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

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



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)
mol wt   Mw 141-151 kDa
purified by   crystallization
greener alternative product characteristics   Waste Prevention: Greener alternative product characteristics
Learn more about the Principles of Green Chemistry.
solubility   H2O: soluble 1.0 mg/mL clear to slightly hazy, colorless to faintly yellow
  : soluble
Featured Industry   Diagnostic Assay Manufacturing
greener alternative category   Enabling
shipped in   dry ice
storage temp.   −20°C



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.

General description

Sigma Life Science is 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 waste prevention when used in fuel cell research. For more information see the article in biofiles.


7500, 15000, 30000, 75000, 150000, 300000 units in poly bottle

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


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

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.

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

All labs need water

Biomedical Applications
Safety & Documentation

Safety Information

NONH for all modes of transport
WGK Germany 
Protocols & Articles


Enzymatic Assay Of Alcohol Dehydrogenase Attached To Agarose (A2529)

The objective of this procedure is to standardize the enzymatic assay of Alcohol Dehydrogenase attached to Agarose, Sigma Product Number (A2529) , at Sigma-Aldrich St. Louis.
Keywords: Extinction coefficient

Enzymatic Assay of Alcohol Dehydrogenase (EC

This procedure may be used for Alcohol Dehydrogenase products, except for insoluble forms of Alcohol Dehydrogenase (Catalog No. A2529).
Keywords: Extinction coefficient

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers


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06693 Timestrip Plus -20 °C

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