Yeast alcohol dehydrogenase source

Sources Yeast alcohol dehydrogenase. Drosophila alcohol dehydrogenase. 

Enzymes from various sources have been used for asymmetric reductions in organic synthesis. Microorganisms are the most important sources. There are a huge number of species (mostly in soil), containing a variety of enzymes. Commercially available microbial dehydrogenases are alcohol dehydrogenases from yeast, Ther-moanaerobium brockii (TBADH), and the hydroxysteroid dehydrogenase from Pseudomonas testosteroni. 

The importance of obstruction (steric hindrance) in determining the stereochemical course of enzymic reactions is further illustrated by a comparison of the stereospecificities of the alcohol dehydrogenases from yeast and from horse liver. The enzymes from both sources are A-side (re face) specific dehydrogenases wherein the pro-(R) hydrogen at C-l of the alcohol is in the transferring position Eq. (2)] ... 

Strict specificity toward a coenzyme regardless of the source material. Alcohol dehydrogenase isolated from yeast and horse liver reacts with DPN but not at all with TPN. Triosephosphate dehydrogenase might have been cited as another example of strict DPN specificity except that current... 

Pyruvate decarboxylase (EC 4.1.1.1) has been characterized in different sources including yeast, bacteria, wheat, maize, sweet potato, and plants [8]. This is the first enzyme of the branch of the glycolytic pathway, which under anaerobic conditions leads to nonoxidative decarboxylation of pyruvate to reduced end-products [9]. In the case of yeast, pyruvate decarboxylase together with alcohol dehydrogenase (EC 1.1.1.1) converts pyruvate to ethanol. 

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