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A3263 Sigma

Alcohol Dehydrogenase from Saccharomyces cerevisiae Green Alternative

≥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,
mol wt   mol wt ~141,000 (four subunits)
purified by   crystallization
greener alternative product characteristics   Waste Prevention: Greener alternative product characteristics
Learn more about the Principles of Green Chemistry.
suitability   suitable for recycling micro-assay of β-NAD and β-NADH
greener alternative category   Enabling
storage temp.   −20°C


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 units in poly bottle

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

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)


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.

Price and Availability

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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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