A8656
Alcohol Dehydrogenase from Saccharomyces cerevisiae
Sinonimo/i:
ADH, Alcohol Dehydrogenase from yeast, Alcohol:NAD+ oxidoreductase
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About This Item
Prodotti consigliati
Origine biologica
Saccharomyces cerevisiae
Livello qualitativo
Forma fisica
powder
PM
~150,000
Confezionamento
vial of 25 mg
Temperatura di conservazione
−20°C
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Applicazioni
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.
Azioni biochim/fisiol
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)
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.
Avvertenze
Danger
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Resp. Sens. 1
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
Certificati d'analisi (COA)
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
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)
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