49641
Alcohol Dehydrogenase, recombinant
≥500 U/mL
Sinónimos:
Alcohol:NADP+ oxidoreductase
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About This Item
Número de CAS:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
Productos recomendados
recombinante
expressed in E. coli
Nivel de calidad
Formulario
liquid
actividad específica
≥500 U/mL
técnicas
cell based assay: suitable
color
light brownish-yellow to brown-green
idoneidad
suitable for molecular biology
aplicaciones
life science and biopharma
temp. de almacenamiento
−20°C
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Descripción general
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.
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.
Aplicación
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.
Acciones bioquímicas o fisiológicas
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.
Definición de unidad
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)
Palabra de señalización
Warning
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Eye Irrit. 2
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
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)
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
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