This product is recombinant enzyme produced in e. coli. The original species information is not available.
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Informazioni su questo articolo
Numero CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥500 U/mL
Recombinant:
expressed in E. coli
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
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.
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.
Other Notes
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)
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From what organism is this alcohol dehydrogenase from
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