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Alcohol dehydrogenase mechanism elucidation

Alcohol dehydrogenases are enzymes that are well known from physiological and biochemical studies on the primary metabolism of cells. Several ADHs are commercially available and for some of them such as the ADH from yeast or liver details concerning the structure and reaction mechanism have been elucidated. For preparative applications however they seldom meet the requirements and new enzymes are needed for this field. [Pg.148]

Other Zinc Enzymes. Studies aimed at elucidating the mechanism of dimeric alcohol dehydrogenase enzymes have also been reported. Cobalt(n) can replace zinc(ii) at the two catalytic and non-catalytic sites in the liver enzyme, LADH. Reduction of pyridinealdehyde derivatives by the yeast enzyme has been examined. In acetonitrile solution, reduction by NADH analogues is catalysed by metal ions and mechanistic studies of the reaction have been carried out. Biomimetic studies of zinc-catalysed carbonyl reduction have also been reported. ... [Pg.362]


See other pages where Alcohol dehydrogenase mechanism elucidation is mentioned: [Pg.170]    [Pg.659]    [Pg.231]    [Pg.357]    [Pg.182]    [Pg.143]    [Pg.170]    [Pg.159]   
See also in sourсe #XX -- [ Pg.191 , Pg.193 ]




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