This product is recombinant enzyme produced in e. coli. The original species information is not available.
49641
Alcohol Dehydrogenase, recombinant
≥500 U/mL
Sinónimos:
Alcohol:NADP+ oxidoreductase
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1 ML
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5 ML
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About This Item
Número de CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Productos recomendados
recombinant
expressed in E. coli
Quality Level
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.[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]
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.[4]
Biochem/physiol Actions
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]
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)
signalword
Warning
hcodes
pcodes
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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Mechanism of alcohol-induced oxidative stress and neuronal injury
Haorah J, et al.
Free Radical Biology & Medicine, 45(11), 1542?1550-1542?1550 (2008)
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)
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)
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
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From what organism is this alcohol dehydrogenase from
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