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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:
9031-72-5
Enzyme Commission number:
1.1.1.1 (BRENDA, IUBMB)
EC Number:
232-870-4
MDL number:
MFCD00081305
NACRES:
NA.54

biological source

Saccharomyces cerevisiae

Quality Level

300

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.

A0A3G3NDH9
S5RCH3
S5RK20
S5S176

application(s)

diagnostic assay manufacturing

greener alternative category

, Enabling

shipped in

dry ice

storage temp.

−20°C

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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.

antibody

Product No.
Description
Pricing

WH0000127M1

Monoclonal Anti-ADH4 antibody produced in mouse, clone 3C5, purified immunoglobulin, buffered aqueous solution

WH0000130M1

Monoclonal Anti-ADH6 antibody produced in mouse, clone 4G4, purified immunoglobulin, buffered aqueous solution

AV41787

Anti-ADH1B antibody produced in rabbit, IgG fraction of antiserum

AV43573

Anti-ADH4 antibody produced in rabbit, IgG fraction of antiserum

HPA020525

Anti-ADH4 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

SAB2100059

Anti-ADH1B antibody produced in rabbit, affinity isolated antibody

SAB4500399

Anti-ADH7 antibody produced in rabbit, affinity isolated antibody

HPA039695

Anti-ADH7 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Václav Tvrdý et al.
Nutrients, 13(12) (2021-12-29)
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
Stereospecificity of the oxidation of ethanol by catalase.
R J Corrall et al.
The Journal of biological chemistry, 249(10), 3181-3182 (1974-05-25)
Analysis of genes from Saccharomyces cerevisiae HJ01 participating in aromatic alcohols biosynthesis during huangjiu fermentation
Liu S, et al.
LWT--Food Science and Technology, 154 (2022)
Cheol Woong Ha et al.
Nucleic acids research, 42(13), 8486-8499 (2014-07-02)
In Saccharomyces cerevisiae, the stability of highly repetitive rDNA array is maintained through transcriptional silencing. Recently, a β-1,3-glucanosyltransferase Gas1 has been shown to play a significant role in the regulation of transcriptional silencing in S. cerevisiae. Here, we show that
Cláudio J R Frazão et al.
Scientific reports, 9(1), 11576-11576 (2019-08-11)
In this work, we describe the construction of a synthetic metabolic pathway enabling direct biosynthesis of 1,3-propanediol (PDO) from glucose via the Krebs cycle intermediate malate. This non-natural pathway extends a previously published synthetic pathway for the synthesis of (L)-2,4-dihydroxybutyrate
View All Related Papers

Protocols

Enzymatic Assay of Alcohol Dehydrogenase (EC 1.1.1.1)

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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