Wheat, alcohol dehydrogenase

The crystal structure of the HNL isolated from S. bicolor (SbHNL) was determined in a complex with the inhibitor benzoic acid." The folding pattern of SbHNL is similar to that of wheat serine carboxypeptidase (CP-WII)" and alcohol dehydrogenase." A unique two-amino acid deletion in SbHNL, however, is forcing the putative active site residues away from the hydrolase binding site toward a small hydrophobic cleft, thereby defining a completely different active site architecture where the triad of a carboxypeptidase is missing. 

Mitchell, H.J., Hall, J.L., and Barber, M S., 1994, Elicitor-induced cinnamyl alcohol dehydrogenase activity in lignifying wheat (Triticum aestivum L.) leaves, Plant Physiol. 104 551-556. 

Althoi h green leaves appear to have lost the ability to form acetaldehyde from pymvic acid, they still retain some of the alcohol dehydrogenase which is present in considerable amounts in seeds (340). Stafford et al. (328) have reported slight alcohol dehydrogenase activity in parsley leaves. Small amounts of alcohol de-hydri enase have also been found in tobacco and spinach leaves (I. Zelitch and W. Vishniac, unpublished observations). These alcohol dehydrogenases react with DPN. Wheat germ alcohol dehydrogenase was found by Stafford and Vennesland (329) to react with both DPN and TPN. 

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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