Alcohol Dehydrogenase from Saccharomyces cerevisiae 

Contains bound β-NAD and β-NADH and is not suitable for the recycling microassay of β-NAD and NADH. If you require ADH for this purpose, see Catalog No. A3263.

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

Solids containing ≤ 2% citrate buffer salts

A 141k Da 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^-3 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)

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lyophilized powder (contains buffer salts)

crystallization

Protein, ≥90% E1%/280

suitable for conventional determination of β-NAD, β-NADH, ethanol and acetaldehyde

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dry ice

−20°C

Buhner, M. and Sund, H. Eur. J. Biochem. 11, 73, (1969) abstract

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