The lyophilized powder is soluble in water at a concentration of 1 mg/ml, yielding a clear to slightly hazy solution. In solutions of ≥1 mg/ml, alcohol dehydrogenase retains all activity after 90 minutes when stored at 0 °C or at room temperature. More dilute solutions of alcohol dehydrogenase are quite unstable. Freezing and thawing of alcohol dehydrogenase solutions is not recommended. For long-term storage, the lyophilized powder should be kept at –20 °C.
A7011
Alcohol Dehydrogenase from Saccharomyces cerevisiae
≥300 units/mg protein, lyophilized powder (contains buffer salts), Mw 141-151 kDa
Synonym(s):
ADH1, Adh1p, SCAD, YDAH-1, YIM-1, ADH, Alcohol Dehydrogenase from yeast, Alcohol:NAD+ oxidoreductase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-870-4
MDL number:
Specific activity:
≥300 units/mg protein
Biological source:
Saccharomyces cerevisiae
Pricing and availability is not currently available.
biological source
Saccharomyces cerevisiae
Quality Segment
form
lyophilized powder (contains buffer salts)
specific activity
≥300 units/mg protein
mol wt
Mw 141-151 kDa
purified by
crystallization
storage condition
(Keep container tightly closed in a dry and well-ventilated place.)
greener alternative product characteristics
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sustainability
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color
white to light yellow-brown, Light brown
optimum pH
8.6-9.0
solubility
H2O: soluble 1.0 mg/mL, clear to slightly hazy, colorless to faintly yellow, soluble
UniProt accession no.
application(s)
diagnostic assay manufacturing
greener alternative category
, Enabling
shipped in
dry ice
storage temp.
−20°C
General description
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.[1]
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.[1]
Application
Alcohol dehydrogenase has been used along with lactic dehydrogenase for the enzymatic reduction of acetaldehyde using sodium(R,S)-[2-3H] lactate.[2] It has also been used to study the inhibitory effect of zinc-chelated silymarin flavonolignans on yeast alcohol dehydrogenase.[3]
Ethanol concentration can be determined colorimentrically by monitoring the enzymatic reduction of NAD using alcohol dehydrogenase after preremoval of the aldehyde group.[4]
Ethanol concentration can be determined colorimentrically by monitoring the enzymatic reduction of NAD using alcohol dehydrogenase after preremoval of the aldehyde group.[4]
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)
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.[5] It is also implicated in the production of alcohol from amino acid breakdown via the Ehrlich pathway.
Physical form
Solids containing ≤ 2% citrate buffer salts
Preparation Note
Dissolves in water at a concentration of 1 mg/mL to form a clear to slightly hazy, colorless to faintly yellow colored solution.
Other Notes
One unit will convert 1.0 μmole of ethanol to acetaldehyde per min at pH 8.8 at 25 °C.
Disclaimer
Contains bound β-NAD and β-NADH and is not suitable for the recycling microassay of β-NAD and β-NADH. If you require ADH for this purpose, see Catalog No. A3263.
1 of 1
This Item | |||
|---|---|---|---|
| biological source Saccharomyces cerevisiae | biological source Saccharomyces cerevisiae | biological source bakers yeast | biological source yeast |
| specific activity ≥300 units/mg protein | specific activity - | specific activity ≥300 units/mg protein | specific activity ≥10 units/mg protein |
| application(s) diagnostic assay manufacturing | application(s) - | application(s) - | application(s) - |
| form lyophilized powder (contains buffer salts) | form powder | form powder | form lyophilized powder |
| optimum pH 8.6-9.0 | optimum pH - | optimum pH 8.6-9.0 | optimum pH - |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. 2-8°C |
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flash_point_c
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