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Key Documents

A8656

Sigma-Aldrich

Alcohol Dehydrogenase from Saccharomyces cerevisiae

Sinônimo(s):

ADH, Alcohol Dehydrogenase from yeast, Alcohol:NAD+ oxidoreductase

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About This Item

Número CAS:
Número da licença da enzima:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.25

fonte biológica

Saccharomyces cerevisiae

Nível de qualidade

forma

powder

peso molecular

~150,000

embalagem

vial of 25 mg

temperatura de armazenamento

−20°C

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Aplicação

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.

Ações bioquímicas/fisiológicas

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.

Pictogramas

Health hazard

Palavra indicadora

Danger

Frases de perigo

Declarações de precaução

Classificações de perigo

Resp. Sens. 1

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


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Visite a Biblioteca de Documentos

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)
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)
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)
Jung-Eun Kim et al.
Frontiers in immunology, 11, 593748-593748 (2021-01-26)
Patients with severe eosinophilic asthma (SEA; characterized by persistent eosinophilia in blood and airway tissues) experience frequent asthma exacerbations with poor clinical outcomes. Interleukin 5 (IL-5) and IL-5 receptor alpha subunit (IL-5α) play key roles in eosinophilia maintenance, and relevant

Protocolos

This procedure may be used for Alcohol Dehydrogenase products.

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