Alcohol Dehydrogenase Inhibitors

Chemical inhibitors of Alcohol Dehydrogenase can act through various mechanisms to halt the activity of this enzyme.Fomepizole is a competitive inhibitor that directly competes with ethanol for the active site of Alcohol Dehydrogenase, effectively blocking access and preventing the oxidation of alcohol to acetaldehyde. Similarly, Pyrazole and 3-Amino-1,2,4-triazole occupy the substrate-binding site, which directly hinders the enzyme's ability to catalyze its intended reaction. These inhibitors mimic the structure of ethanol, thereby deceiving the enzyme and leading to a decrease in its activity.

Other inhibitors, such as Disulfiram and Calcium carbimide, act by binding to essential components of the active site. Disulfiram interacts with the copper ion, a vital cofactor for the enzymatic action, while Calcium carbimide forms a disulfide bond with a cysteine residue near the active site. This disrupts the normal function and structure of Alcohol Dehydrogenase, rendering it inactive. Iodoacetamide also inactivates the enzyme through a similar mechanism by alkylating the cysteine residues. Metal chelators like 1,10-Phenanthroline and Dimercaprol bind to metal cofactors necessary for the catalytic action of Alcohol Dehydrogenase, which results in the inhibition of the enzyme's activity. Sodium azide affects the metal cofactors in the active site, which are critical for enzyme function. In contrast, Ethanol at high concentrations leads to substrate inhibition, where the active site becomes saturated, and the enzymatic activity is reduced. Acetone competes with alcohols for the active site, thus reducing the rate at which Alcohol Dehydrogenase can metabolize alcohols, despite being a poor substrate itself. Each of these chemicals interacts with Alcohol Dehydrogenase in a specific manner that leads to the inhibition of its enzymatic function, thereby preventing the normal metabolic processing of alcohols within the body.