Alcool déhydrogénase, réactif de E. coli, >=500 u/ mL

Non disponible en dehors du Royaume-Uni et de l'Irlande

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)