A8656

Sigma-Aldrich

Alcohol Dehydrogenase from Saccharomyces cerevisiae

Sinónimos:
Alcohol:NAD+ oxidoreductase, ADH, Alcohol Dehydrogenase from yeast
Número de CAS:
Comisión internacional de enzimas:
Número de EC:
Número MDL:
NACRES:
NA.25

formulario

powder

Nivel de calidad

200

mol peso

~150,000

envase

vial of 25 mg

temp. de almacenamiento

−20°C

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Aplicación

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.

Acciones bioquímicas o 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.

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)

RIDADR

NONH for all modes of transport

WGK Alemania

WGK 3

Punto de inflamabilidad F

Not applicable

Punto de inflamabilidad C

Not applicable

The alcohol dehydrogenases of Saccharomyces cerevisiae: a comprehensive review
De Smidt O, et al.
FEMS Yeast Research, 8(7), 967-978 (2008)
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)
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)
Protocolos
Gel filtration chromatography is an established method for determining the size and molecular mass of proteins.
Más información
This procedure may be used for Alcohol Dehydrogenase products.
Más información

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