LAB BIO3 - Enzyme Function

LAB BIO3 - Enzyme Function - Victor Cruz Portillo BIO 150...

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Victor Cruz Portillo BIO 150 Enzyme Function 1 Oct. 2010 / 8 Oct. 2010 Estefania Yactayo, Nadile Tousseant, Gisellis Correa, Laetiera Compas
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Introduction Enzymes are proteins produced by living cells. Enzymes are biochemical catalysts that lower the activation energy needed for a biochemical reaction to occur. Because of enzyme activity, cells can carry out complex chemical activities (Illanes, 2008, pp. 1-4). The substrate is the substance acted upon in an enzyme-catalyzed reaction, and the substrate can bind reversibly to the active site of the enzyme. The active site is the portion of the enzyme that interacts with the substrate so that any substrate that blocks or changes the shape of the active site affects the activity of the enzyme (Likhtenshtein, 2002, pp. 139). The result of this temporary union is called the enzyme-substrate complex and reduces the amount of energy required to activate the reaction of the substrate molecule so that products are formed (Illanes, 2008, pp. 8). Inhibitors interact with an enzyme so that the activity of an enzyme is altered. An inhibitor decreases or stops the activity. Inhibitors regulate how fast an enzyme acts. Inhibitors work by unfolding or destabilizing bonds, thus denaturing the enzyme. Some inhibitors block or change the shape of the active site (Schulz, 1994, p. 30). In competitive inhibition, the substrate and inhibitor have both the same shape and cannot bind to the enzyme at the same time, which usually results in the substrate and inhibitor competing for access to the enzyme's active site (Schulz, 1994, p. 35). If the competitive inhibitor reaches the enzymes first, the reaction that is usually caused by the enzyme never occurs (Schulz, 1994, p. 35). Competitive inhibition can be type of inhibition can be overcome by sufficiently high concentrations of substrate; essentially the substrates out compete the inhibitor (Schulz, 1994, p. 35). In non-competitive inhibition, the inhibitor reversibly binds to an allosteric site, a site different than the active site, on the enzyme, preventing the substrate from being able to bind to the active site and the reaction of the enzyme (Illanes, 2008, pp. 116).
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This note was uploaded on 11/18/2010 for the course BIO 150 taught by Professor Gioradano during the Fall '10 term at SUNY Suffolk.

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LAB BIO3 - Enzyme Function - Victor Cruz Portillo BIO 150...

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