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49641

Sigma-Aldrich

Alkoholdehydrogenase, rekombinant aus E. coli

≥500 U/mL

Synonym(e):

Alkohol:NADP+-Oxidoreduktase

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About This Item

CAS-Nummer:
9028-12-0
EC-Nummer:
1.1.1.2 (BRENDA, IUBMB)
MDL-Nummer:
MFCD00130451
UNSPSC-Code:
12352204
NACRES:
NA.54

Rekombinant

expressed in E. coli

Form

liquid

Spezifische Aktivität

≥500 U/mL

Methode(n)

cell based assay: suitable

Farbe

light brownish-yellow to brown-green

Eignung

suitable for molecular biology

Anwendung(en)

life science and biopharma

Lagertemp.

−20°C

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Allgemeine Beschreibung

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.

Anwendung

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. Wirkung

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.

Einheitendefinition

1 U entspricht der Enzymmenge, die 1μmol Aceton pro Minute bei pH 7.0 und 30°C (NADPH als Cofaktor) reduziert.

Piktogramme

Exclamation mark
GHS07

Signalwort

Warning

H-Sätze

H319

Gefahreneinstufungen

Eye Irrit. 2

Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves

Analysenzertifikate (COA)

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Ethanol-Assay-Kit sufficient for 100 colorimetric or fluorometric tests

Sigma-Aldrich

MAK076

Ethanol-Assay-Kit

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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