Alcohol Dehydrogenase.ppt

Alcohol Dehydrogenase The Hang-Over Enzyme Pat Baron Outline Why the Hang-Over enzyme? Forms, Functions, and a little Fiction A closer look into the active site of ADH Conclusions Why the Hang-Over Enzyme?- General Information on ADH and questions answered! Alcohol Dehydrogenase belongs to the oxidoreductase family of enzymes ADH is found in high concentrations within the human liver and kidney The primary and most common role of ADH in humans is to detoxify incoming ethanol by converting it into acetaldehyde The resulting acetaldehyde, a more toxic molecule than ethanol, is quickly converted into acetate and other molecules easily utilized by the cell But Why the Hang-Over?- Partially explained by the chemistry Incoming ethanol is converted to acetaldehyde by the mechanism below: Ethanol + NAD+ ----------? Acetaldehyde + NADH Ethanol is oxidized by ADH into acetaldehyde and NADH is formed The highly toxic acetaldehyde is then further modified into foodstuffs for the cell Throughout these processes, water molecules are lost and dehydration could set in after prolonged imbibing. There you have it! Dehydration is the Culprit “….then dying of thirst must be one of the worst hang-overs to experience.” A Beautiful Mind Forms, Functions, and a little fiction- structure and function of ADH and associated isoenzymes Humans have at least nine known forms of ADH ADH exists as a homo or heterodimer due to the fact there are two different types of monomer The two types are E and S for ethanol active and steroid active respectively. Although they have different specificities, both are nearly identical at 374 aa’s long Therefore, possible types of ADH are: EE, SS, and ES hybrid ADH. EE is the most commonly found at 40-60% Characteristics of EE ADH EE ADH has a molecular weight of about 80 000 There are 8 chains, 60 helices, and 74 beta strands in ADH Each monomer of the dimer has 2 subunits Each of the two subu