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Essay #1 I. pH and allosteric regulation are both determining factors in the control of enzymes II. Allosteric control A. Allosteric site - site that regulatory molecules on enzymes bind to 1. Two kinds of allosteric molecules a) Activator - stabilizes the active form of the enzyme b) Inhibitor - stabilizes the inactive form of the enzyme 2. Enzymes can easily move from the active to inactive state and back a) One activator or inhibitor can bond to an allosteric site and change all subunits of an enzyme b) Some activators and inhibitors are similar in structure and compete for allosteric sites 3. Allosteric inhibition prevents or slows the enzyme's metabolic function, while activation speeds it up a) In this case phosphofructokinase controls the rates of certain metabolic reactions III. pH control A. Optimal pH 1. Certain enzymes are most active at a specific pH 2. This pH usually ranges from 6 to8 B. pH can control the activity of enzymes 1. Increase in pH can reduce activity of enzymes that normally have an acidic environment 2. Increase in pH increases activity of enzymes that are more basic 3.
Approximate Word count = 716
Approximate Pages = 2.9
(250 words per page double spaced)
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