Összes fotó(5)
Fontos dokumentumok
A3263
Alcohol Dehydrogenase from Saccharomyces cerevisiae
powder, ≥300 units/mg protein, mol wt ~141,000 (four subunits)
Szinonimák:
ADH1, ADH, Alcohol Dehydrogenase from yeast, Alcohol:NAD+ oxidoreductase
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(5)
About This Item
Javasolt termékek
biológiai forrás
bakers yeast
Minőségi szint
Forma
powder
specifikus aktivitás
≥300 units/mg protein
molekulatömeg
~141,000 (four subunits)
tisztítva
crystallization
tárolási körülmény
(Tightly closed. Dry)
környezetbarátabb alternatív termék tulajdonságai
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
szín
beige
optimális pH
8.6-9.0
alkalmasság
suitable for recycling micro-assay of β-NAD and β-NADH
UniProt elérési szám
környezetbarátabb alternatív kategória
tárolási hőmérséklet
−20°C
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Általános leírás
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.
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.
Alkalmazás
Alcohol Dehydrogenase from Saccharomyces cerevisiae has been used for the determination of NAD+ and NADH concentrations.
Biokémiai/fiziológiai hatások
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)
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.
Specifikációk
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.
Egység definíció
One unit will convert 1.0 μmole of ethanol to acetaldehyde per min at pH 8.8 at 25 °C.
Fizikai forma
Solids containing <2% citrate buffer salts
antitest
Product No.
Leírás
Árazás
Figyelmeztetés
Danger
Figyelmeztető mondatok
Óvintézkedésre vonatkozó mondatok
Veszélyességi osztályok
Resp. Sens. 1
Tárolási osztály kódja
11 - Combustible Solids
WGK
WGK 1
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Egyéni védőeszköz
Eyeshields, Gloves, type N95 (US)
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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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