06 March 2007 Inhibiting the Action of Catechol Oxidase Biological catalysts also referred to as catalyst increases the rate of production of a particular chemical reaction without being consumed or molecularly altered in the chemical reaction process. The substance, or product in which an enzymes reacts with is defined as a substrate. The result of the enzymes interaction with a substate, endures a reaction that takes place in active site of an enzyme where the catalysis takes place forming an enzyme-substrate complex (product) unlike the enzyme. Most enzymes in their entirety are comprised of proteins. The amount of energy that is required for an new substance or reaction to form or take place is significantly lowered by the presence of an enzyme and in return accelerate or catalyzes the reaction. This process doesn’t define the reactions final equilibrium or in which direction the reaction will proceed. There are multiple factors and or variables that contribute to an enzymes activity such as the cells environment; more specifically the pH level or temperature that dismembers or disassembles an enzymes conformation and directly affects it’s rate of activity. There are other contributing factors that attribute to an enzymes shape and aid the the modification process. Activators are chemicals that bond with enzyme in order for be active. Substance that binds the enzyme in the active site to facilitate the enzymes ability to do work is a cofactor and is comprised of a non-protein substance. Coenzymes are organic cofactors that promote that work of enzymes but may also consist of metal ions. Inhibitors can be defined as chemicals that execute the production of an enzyme activity and can be classified into to categories, competitive or non-competitive. Competitive inhibition takes place as a result of similar structural molecule to that of substrate, competing for a placement of an active site an enzyme. This particular activity limits the availability of an enzyme, resulting in the substrates inability to bond with the enzyme. A constant concentration of high levels of an inhibitor may result in the reversal of competitive ve inhibition if the substrate level is kept relatively high. The binding of an inhibitor to non active site is defined as a noncompetitive inhibition. In this particular binding or bonding process all catalytic properties are lost and takes place in either of these two ways; the active site is restricted by the non-competitive inhibition or the protein undergoes a conformational change in it’s protein which “inactivates the active site.” In the instance of a non competitive inhibition the inhibitor is unbound that reverses the inhibition. IN this particular binding process the competitive inhibition is irreversible In this particular lab experiment we will be analyzing and assessing the inhibition of enzyme activity by the use of phenylthiourea. In order for this substance to become be come readily available to participate in the reaction process it must first bond to activator that is catehol oxidase. Three experimental test tubes will be prepared with water , potato extract next PTU distilled water and Catechol then covered with Parafilm square and mixed. We will then analyze, access and evaluate the affect of the different inhibitors have on the various given substances in addition to developing a hypothesis.
Posted on: Thu, 15 Aug 2013 15:54:44 +0000
Trending Topics
Recently Viewed Topics
© 2015