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A7011

Sigma-Aldrich

Alcohol Dehydrogenase from Saccharomyces cerevisiae

greener alternative

≥300 units/mg protein, lyophilized powder (contains buffer salts), Mw 141-151 kDa

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Synonym(s):
ADH1, Adh1p, SCAD, YDAH-1, YIM-1, ADH, Alcohol Dehydrogenase from yeast, Alcohol:NAD+ oxidoreductase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

biological source

Saccharomyces cerevisiae

form

lyophilized powder (contains buffer salts)

specific activity

≥300 units/mg protein

mol wt

Mw 141-151 kDa

purified by

crystallization

storage condition

(Keep container tightly closed in a dry and well-ventilated place.)

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

color

white to light yellow-brown, Light brown

optimum pH

8.6-9.0

solubility

H2O: soluble 1.0 mg/mL, clear to slightly hazy, colorless to faintly yellow
soluble

UniProt accession no.

application(s)

diagnostic assay manufacturing

greener alternative category

shipped in

dry ice

storage temp.

−20°C

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This Item
A3263A8656A9770
biological source

Saccharomyces cerevisiae

biological source

bakers yeast

biological source

Saccharomyces cerevisiae

biological source

yeast

UniProt accession no.

A0A3G3NDH9, S5RK20, S5RCH3, S5S176

UniProt accession no.

A0A3G3NDH9, S5RCH3, S5RK20, S5S176

UniProt accession no.

-

UniProt accession no.

A0A3G3NDH9, S5RCH3, S5RK20, S5S176

storage condition

(Keep container tightly closed in a dry and well-ventilated place.)

storage condition

(Tightly closed. Dry)

storage condition

-

storage condition

(Tightly closed. Dry)

shipped in

dry ice

shipped in

-

shipped in

-

shipped in

-

form

lyophilized powder (contains buffer salts)

form

powder

form

powder

form

lyophilized powder

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.

Application

Alcohol dehydrogenase has been used along with lactic dehydrogenase for the enzymatic reduction of acetaldehyde using sodium(R,S)-[2-3H] lactate. It has also been used to study the inhibitory effect of zinc-chelated silymarin flavonolignans on yeast alcohol dehydrogenase.

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)
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.

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.

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

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.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Silymarin is known for its hepatoprotective effects. Although there is solid evidence for its protective effects against Amanita phalloides intoxication, only inconclusive data are available for alcoholic liver damage. Since silymarin flavonolignans have metal-chelating activity, we hypothesized that silymarin may
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Protocols

To measure alcohol dehydrogenase activity, this assay uses β-nicotinamide adenine dinucleotide phosphate and a continuous spectrophotometric rate determination at 340 nm.

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