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A7011

Alcohol Dehydrogenase from Saccharomyces cerevisiae

greener alternative

≥300 units/mg protein, lyophilized powder (contains buffer salts), Mw 141-151 kDa

Synonim(y):

ADH1, Adh1p, SCAD, YDAH-1, YIM-1, ADH, Alcohol Dehydrogenase from yeast, Alcohol:NAD+ oxidoreductase

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Do Państwa/SKUDostępnośćCena netto
7500 units
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245,00 zł
15000 units
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265,00 zł
30000 units
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1870,00 zł
300000 units
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2790,00 zł

Informacje o tej pozycji

Numer CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-870-4
MDL number:
Numer WE:
Specific activity:
≥300 units/mg protein
Biological source:
Saccharomyces cerevisiae

245,00 zł


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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

Waste Prevention
Design for Energy Efficiency
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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

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]

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]

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)
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.
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Ta pozycja
A8656A3263A9770
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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Klasa składowania

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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Questions

  1. I am using your product Alcohol dehydrogenase from Saccharomyces cerevisiae (Product No. A7011). I would like to ask about the recommended storage conditions after reconstitution. • What buffer is recommended for dissolving the enzyme?

    1 answer
    1. 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.

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