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The stereospecificity of the acetaldehyde reduction with alcohol dehydrogenase (AlDH) has been rationalized in terms of the interaction of the coenzyme, the side-chains attached to the carbonyl group and finally in terms of the hydrophilic and hydrophobic regions near the active site of the enzyme. However, no structural information is available concerning the substrate recognition site. This report is concerned with the site-specific labeling of the substrate-binding site of horse liver AlDH by means of the following substrate analogs, bromo-acetaldehyde and bromo-cyclohexanone. The results presented strongly suggest that the acetaldehyde and cyclohexanone groups are covalently attached to the substrate-binding site …
