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A8656

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Alcohol Dehydrogenase from Saccharomyces cerevisiae

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Synonym(s):
ADH, Alcohol Dehydrogenase from yeast, Alcohol:NAD+ oxidoreductase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.25

biological source

Saccharomyces cerevisiae

Quality Level

form

powder

mol wt

~150,000

packaging

vial of 25 mg

storage temp.

−20°C

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This Item
A7011A326374931
Sigma-Aldrich

Sigma-Aldrich

74931

Alcohol Dehydrogenase

form

powder

form

lyophilized powder (contains buffer salts)

form

powder

form

powder

mol wt

~150,000

mol wt

Mw 141-151 kDa

mol wt

~141,000 (four subunits)

mol wt

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

300

Quality Level

200

Quality Level

-

packaging

vial of 25 mg

packaging

-

packaging

-

packaging

-

Application

Alcohol Dehydrogenase from Saccharomyces cerevisiae has been used as a gel filtration molecular weight marker/ It has also been used as a component of nine protein mixture for mass spectroscopy analysis.

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)
Alcohol Dehydrogenase (ADH) is an oxidoreductase and also a pyridine nucleotide-dependent dehydrogenase. It catalyzes the generation of aldehydes or ketones by reversible oxidation of alcohols. ADH in parallel also mediates the reduction of the nicotinamide adenine dinucleotide (NAD+) or nicotinamide adenine dinucleotide phosphate (NADP+). ADH from yeast is more active than mammalian ADHs.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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The alcohol dehydrogenases of Saccharomyces cerevisiae: a comprehensive review
De Smidt O, et al.
FEMS Yeast Research, 8(7), 967-978 (2008)
Yeast alcohol dehydrogenase structure and catalysis
Raj S, et al.
Biochemistry, 53(36), 5791-5803 (2014)
Determination of hydrodynamic radius of proteins by size exclusion chromatography
La Verde V, et al.
Bio-protocol, 7(8), 1-14 (2017)
Study of Reduction Properties of Enzyme Alcohol Dehydrogenase from Saccharomyces cerevisiae Meyen ex. Hansen on Some Selected Compounds
Khan SYN
International journal of language & communication disorders, 3(4), 1218-1222 (2017)
Application of de novo sequencing to large-scale complex proteomics data sets
Devabhaktuni A and Elias JE
Journal of Proteome Research, 15(3), 732-742 (2016)

Protocols

Gel filtration chromatography is an established method for determining the size and molecular mass of proteins.

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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