Letter of Intent Title: development of a solution for this alcohol poisoning using alcohol dehydrogenase1 Background: alcohol dehydrogenases (ADH) also known as (EC 1.1.1.1)2 are defined as a group of enzymes that catalase the conversion of alcohols into ketones or aldehydes (figure 1)4. There are different types of ADH and they are present in different living organisms. Examples of these types include ADH I, II, III, and IV. Alcohol dehydrogenase I is found in human beings and it is mainly found in the liver, heart, and kidney. In this intent letter, ADH I is addressed. ADH enzyme contains two types of inhibitors that are analogues of alcohol and aldehydes and analogues of coenzyme NAD. For ADH I to function it requires an energy carrier molecule called nicotinamide adenine dinucleotide (NAD+) or 1ADC and a zinc metal. The zinc metal is found at the amino acids (Cysteine-174, Cyst-46 and Histidine-67)2. In this experiment, 1ADC is used instead of NAD. The 1ADC molecule is used as a co-substrate in the oxidation reaction in which the zinc metal is used to correctly place the hydroxyl group of the alcohol in a position that can make the 1ADC to attack hence generating a new molecule. The general reaction is shown below 1 Figure 1: the general oxidation reaction catalyzed by alcohol dehydrogenase 1 This enzyme more effective when the type of alcohol used is of low molecular weight and the rate-limiting step in this reaction is the dissociation of the energy carrier molecule, ...
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