Alcohol Dehydrogenase, recombinant from E. coli, >=500 U/mL
Biochem/physiol Actions
Alcohol dehydrogenase catalyzes the oxidative conversion of alcohol into aldehyde. It 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 which create the binding site for the alcohol substrate.
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)
| Quality Level | 100 |
|---|---|
| Manufacturer | SIGMA-ALDRICH |
| Storage Temp. | −20°C |
| Form | liquid |
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