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Published byDoris Henry Modified over 9 years ago
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Figure 6.1 The complexity of metabolism
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Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change
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Figure 6.6 Energy changes in exergonic and endergonic reactions
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Figure 6.7 Disequilibrium and work in closed and open systems
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Figure 6.8 The structure and hydrolysis of ATP
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Figure 6.9 Energy coupling by phosphate transfer
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Figure 6.10 The ATP cycle
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Figure 6.11 Example of an enzyme-catalyzed reaction: Hydrolysis of sucrose
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Figure 6.12 Energy profile of an exergonic reaction http://www.stolaf.edu/people/giannini/flashanimat/enzymes/transition%20state.swf
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Figure 6.13 Enzymes lower the barrier of activation energy
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Figure 6.14 The induced fit between an enzyme and its substrate
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Figure 6.15 The catalytic cycle of an enzyme
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Figure 6.16 Environmental factors affecting enzyme activity
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Characterizing enzymes V max - rate when enzyme is saturated with substrate K M – substrate concentration that allows reaction to proceed at 1/2 V max K M – useful as a measure of how tightly an enzyme binds its substrate –Low K M means tight binding, high K M means weak binding Enzyme kinetics
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Characterizing enzymes Turnover number: V max /enzyme concen. – typically about 1000 substrate molecules processed per second per enzyme molecule, but can be much higher
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EnzymeTurnover number (per second) Carbonic anhydrase600,000 Acetycholinesterase25,000 Amylase18,000 Penicillinase2,000 DNA Polymerase15
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Measuring enzyme activity One unit of an enzyme is defined as the amount that will catalyze a defined amount of substrate in one minute under specified conditions. For catalase: one unit decomposes 1 mole H 2 O 2 at 25 0 C at pH 7.
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What to measure for rate? Amount of substrate used over a specified time. OR Amount of product accumulated over a specified time. Which to use???
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Figure 6.17 Inhibition of enzyme activity
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Figure 6.18 Allosteric regulation of enzyme activity
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Figure 6.19 Feedback inhibition
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Figure 6.20 Cooperativity
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