Ryan McGrath
Bio 111L-C
24 September 2008
The Effect of Enzyme-Substrate Specificity on the Activity of Enzymes with Various Substrates
In any given instant within one’s body, millions of processes and reactions are subconsciously taking place to maintain a state of homeostasis and produce energy for general function. Seeing as many of these processes are extremely complicated and lengthy procedures, yet millions of these actions take place at any given moment, something must be driving the efficiency human bodies exhibit. This is where various specialized proteins found throughout the body, called enzymes, come into play (Dusheck 2005). Enzymes are catalysts within biological systems which lower the activation energy of chemical reactions and biological processes yet are not consumed or altered within the reaction itself (Dusheck 2005). There is a plethora of enzymes within the body, each with a very specific function or reaction to catalyze (Johnson 2008). Yet, with so many enzymes present, is it really possible that the activity of a given enzyme is relegated to catalyzing a singular biological or chemical reaction? As a result, this experiment was derived in order to exhibit the extent in which enzymes display specificity to a singular reaction within their activity. Thus, pertaining to this study, it is predicted that one enzyme will cleave only one substrate when combined with many different substrates. Therefore, it is believed that if an enzyme is mixed with different substrates in order to catalyze different reactions, then the enzyme will display a significantly increased activity with one substrate than any other substrate as a result of enzyme-substrate specificity.
In order to test the hypothesis stated it was quite clear that the various enzyme-substrate combinations must be isolated from one another in order to standardize a single enzyme-substrate reaction and to also establish a means of comparison between the calculated enzyme...