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49641

Sigma-Aldrich

Alcohol Dehydrogenase, recombinant from E. coli

≥500 U/mL

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Synonym(s):
Alcohol:NADP+ oxidoreductase
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

form

liquid

specific activity

≥500 U/mL

storage temp.

−20°C

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This Item
A8656L5135L2011
form

liquid

form

powder

form

lyophilized powder

form

ammonium sulfate suspension

specific activity

≥500 U/mL

specific activity

-

specific activity

≥60 units/mg protein

specific activity

≥250 units/mg protein (biuret)

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

Quality Level

100

Quality Level

200

Quality Level

200

Quality Level

200

Biochem/physiol Actions

Alcohol dehydrogenase catalyzes the oxidative conversion of alcohol into aldehyde. It has a homodimeric structure with a co-enzyme binding domain at the C-terminal and an N-terminal catalytic domain. The active site is located at the interdomain cleft. Binding of NAD+ in the active site causes conformational changes which create the binding site for the alcohol substrate.

Unit Definition

1 U corresponds to the amount of enzyme which reduces 1 μmol acetone per minute at pH 7.0 and 30°C (NADPH as cofactor)

Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Precautionary Statements

Hazard Classifications

Eye Irrit. 2

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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H Eklund et al.
Biochemistry, 23(25), 5982-5996 (1984-12-04)
The binding of NAD to liver alcohol dehydrogenase has been studied in four different ternary complexes by using crystallographic methods. These complexes crystallize isomorphously in a triclinic crystal form which contains the whole dimer of the enzyme in the asymmetric
F Colonna-Cesari et al.
The Journal of biological chemistry, 261(32), 15273-15280 (1986-11-15)
A study of the hinge bending mode in the enzyme liver alcohol dehydrogenase is made by use of empirical energy functions. The enzyme is a dimer, with each monomer composed of a coenzyme binding domain and a catalytic domain with
Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution.
H Eklund et al.
Journal of molecular biology, 146(4), 561-587 (1981-03-15)
Steven Hayward et al.
Biophysical journal, 91(5), 1823-1831 (2006-05-23)
Horse liver alcohol dehydrogenase is a homodimer, the protomer having a coenzyme-binding domain and a catalytic domain. Using all available x-ray structures and 50 ns of molecular dynamics simulations, we investigated the mechanism of NAD+-induced domain closure. When the well-known
Tomáš Pluskal et al.
Nature plants, 5(8), 867-878 (2019-07-25)
Kava (Piper methysticum) is an ethnomedicinal shrub native to the Polynesian islands with well-established anxiolytic and analgesic properties. Its main psychoactive principles, kavalactones, form a unique class of polyketides that interact with the human central nervous system through mechanisms distinct

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