Lecture 14 Proteins Enzyme regulation

Lecture 14 Proteins Enzyme regulation - or inactivating 2...

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Biol141 Foundations in Modern Biology Cellular Biology and Genetics Lecture 14 – Wednesday, September 28 th , 2011 Proteins – Enzyme regulation and Review of Exam #1 Reading: Freeman, Emory 2 nd Ed. Chapter 3 (pages 54-56)
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Learning objectives At the end of this lecture, you will be able to: 1) Describe the two forms of enzyme regulation, competitive inhibition and allosteric regulation. 2) Explain the saturation kinetics of an enzymatic reaction. 3) Explain the effects of temperature and pH on enzymatic activity.
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From last time: Summary of enzyme catalysis. 1) Do all of the reactions catalyzed by a specific enzyme always occur at the same rate? 2) Think of an example to support your answer for the first question. Why does this phenomenon occur?
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1. Competitive inhibition : One of two forms of enzyme regulation.
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Allosteric regulation : A second form of enzyme regulation which can be activating
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Unformatted text preview: or inactivating . 2. Enzymes are saturable—reaction rate is limited by the amounts of substrate present and available enzyme. 1. The speed of an enzyme-catalyzed reaction increases linearly at low substrate concentrations. 2. The increase slows as substrate concentration increases 3. The reaction rate reaches maximum speed at high substrate concentrations. All enzymes show this type of saturation kinetics. At some point, active sites cannot accept substrates any faster, no matter how large the concentration of substrates gets. 3. Enzymes function best at some particular temperature and pH. Temperature affects the movement of the substrates and enzyme. pH affects the enzyme ` s shape and reactivity. To summarize, the rate of an enzyme-catalyzed reaction depends on: 1. Substrate concentration 2. The enzyme ` s intrinsic affinity for the substrate 3. Temperature 4. pH...
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Lecture 14 Proteins Enzyme regulation - or inactivating 2...

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