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A3263

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Alcohol Dehydrogenase from Saccharomyces cerevisiae

greener alternative

powder, ≥300 units/mg protein, mol wt ~141,000 (four subunits)

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

biological source

bakers yeast

form

powder

specific activity

≥300 units/mg protein

mol wt

~141,000 (four subunits)

purified by

crystallization

storage condition

(Tightly closed. Dry)

greener alternative product characteristics

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

color

beige

optimum pH

8.6-9.0

suitability

suitable for recycling micro-assay of β-NAD and β-NADH

UniProt accession no.

greener alternative category

storage temp.

−20°C

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A7011A865674931
vibrant-m

74931

Alcohol Dehydrogenase

biological source

bakers yeast

biological source

Saccharomyces cerevisiae

biological source

Saccharomyces cerevisiae

biological source

-

mol wt

~141,000 (four subunits)

mol wt

Mw 141-151 kDa

mol wt

~150,000

mol wt

-

color

beige

color

white to light yellow-brown, Light brown

color

-

color

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

optimum pH

8.6-9.0

optimum pH

8.6-9.0

optimum pH

-

optimum pH

-

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.

We are 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 energy efficiency and waste prevention when used in fuel cell research. For more information see the article in biofiles.

Application

Alcohol Dehydrogenase from Saccharomyces cerevisiae has been used for the determination of NAD+ and NADH concentrations.

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.

Specifications

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.

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

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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N C Jerez et al.
Journal of animal science, 81(4), 997-1003 (2003-05-02)
The objective of this experiment was to determine the effect of prerigor injection of several glycolytic inhibitors on pH, color, tenderness, and related traits of low-value beef cuts. The semimembranosus, triceps brachii, and supraspinatus muscles from each of 10 steer
Sexual dimorphism in acute myocardial infarction-induced acute kidney injury: cardiorenal deteriorating effects of ovariectomy in premenopausal female mice
Nada J Habeichi, et al.
Clinical Science (London, England : 1979), 137(1), 47-63 (2023)
The role of zinc in alcohol dehydrogenase. V. The effect of metal-binding agents on thestructure of the yeast alcohol dehydrogenase molecule.
J H KAGI et al.
The Journal of biological chemistry, 235, 3188-3192 (1960-11-01)
Savarimuthu Baskar Raj et al.
Biochemistry, 53(36), 5791-5803 (2014-08-27)
Yeast (Saccharomyces cerevisiae) alcohol dehydrogenase I (ADH1) is the constitutive enzyme that reduces acetaldehyde to ethanol during the fermentation of glucose. ADH1 is a homotetramer of subunits with 347 amino acid residues. A structure for ADH1 was determined by X-ray
L Tretter et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 20(24), 8972-8979 (2000-01-11)
In this study we addressed the function of the Krebs cycle to determine which enzyme(s) limits the availability of reduced nicotinamide adenine dinucleotide (NADH) for the respiratory chain under H(2)O(2)-induced oxidative stress, in intact isolated nerve terminals. The enzyme that

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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