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49641

Sigma-Aldrich

Alcohol Dehydrogenase, recombinant from E. coli

≥500 U/mL

Synonym(s):

Alcohol:NADP+ oxidoreductase

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About This Item

CAS Number:
9028-12-0
Enzyme Commission number:
1.1.1.2 (BRENDA, IUBMB)
MDL number:
MFCD00130451
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

form

liquid

specific activity

≥500 U/mL

technique(s)

cell based assay: suitable

color

light brownish-yellow to brown-green

suitability

suitable for molecular biology

application(s)

life science and biopharma

storage temp.

−20°C

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General description

Research area: Neuroscience

Alcohol dehydrogenase 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 that create the binding site for the alcohol substrate.

Application

Alcohol dehydrogenase (ADH) has been used for the reversal of deficient 3-[4,5-dimethylthiazol-2-yl]-2,5 diphenyl tetrazolium bromide (MTT) assay reduction in the disrupted schizophrenia 1 (DISC1-FL) and DB7 cell lysate.

Biochem/physiol Actions

Alcohol dehydrogenase catalyzes the oxidative conversion of alcohol into aldehyde. The metabolism of ethanol catalyzed by alcohol dehydrogenase (ADH) results in the generation of reactive oxygen species (ROS) and nitric oxide (NO) leading to oxidative damage to mitochondria and cellular proteins and is further associated with the onset of neuroinflammation and neurological disorders.

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
GHS07

Signal Word

Warning

Hazard Statements

H319

Precautionary Statements

P305 + P351 + P338

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Inhibition of protein translation by the DISC1-Boymaw fusion gene from a Scottish family with major psychiatric disorders
Ji B, et al.
Human Molecular Genetics, 23(21), 5683?5705-5683?5705 (2014)
Mechanism of alcohol-induced oxidative stress and neuronal injury
Haorah J, et al.
Free Radical Biology & Medicine, 45(11), 1542?1550-1542?1550 (2008)
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)
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
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
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