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Key Documents

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49641

Sigma-Aldrich

Alcohol Dehydrogenase, recombinant

≥500 U/mL

Sinónimos:

Alcohol:NADP+ oxidoreductase

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About This Item

Número de CAS:
9028-12-0
Comisión internacional de enzimas:
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

signalword

Warning

hcodes

H319

Hazard Classifications

Eye Irrit. 2

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves

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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
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
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
Albert Rosell et al.
Journal of molecular biology, 330(1), 75-85 (2003-06-24)
The amphibian enzyme ADH8, previously named class IV-like, is the only known vertebrate alcohol dehydrogenase (ADH) with specificity towards NADP(H). The three-dimensional structures of ADH8 and of the binary complex ADH8-NADP(+) have been now determined and refined to resolutions of
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