This product is recombinant enzyme produced in e. coli. The original species information is not available.
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Alkoholdehydrogenase, rekombinant aus E. coli
≥500 U/mL
Synonym(e):
Alkohol:NADP+-Oxidoreduktase
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1 ML
€ 212,00
5 ML
€ 826,00
About This Item
CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54
Empfohlene Produkte
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.[1] Binding of NAD+ in the active site [2] causes conformational changes that create the binding site for the alcohol substrate.[3]
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.[1] Binding of NAD+ in the active site [2] causes conformational changes that create the binding site for the alcohol substrate.[3]
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.[4]
Biochem./physiol. Wirkung
Alcohol dehydrogenase catalyzes the oxidative conversion of alcohol into aldehyde.[5] 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.[6]
Einheitendefinition
1 U entspricht der Enzymmenge, die 1μmol Aceton pro Minute bei pH 7.0 und 30°C (NADPH als Cofaktor) reduziert.
Signalwort
Warning
H-Sätze
P-Sätze
Gefahreneinstufungen
Eye Irrit. 2
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves
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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)
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)
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