ch06.3 - The active site of an enzyme is most complimentary...

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The active site of an enzyme is most complimentary to A. the substrate. B. the transition state. C. the product. D. the enzyme itself.
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Recall the extraordinary enhancements of rate which enzymes produce: generally a factor of 10 6 to 10 17 . How do they do this? By lowering the activation energy of the reaction Factors which contribute to catalytic efficiency of enzymes: 1. Binding energy 2. General acid-base catalysis 3. Covalent catalysis 4. Metal ion catalysis
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6-6 Binding energy ( G B )
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2. General Acid-Base catalysis 6-9 Which of these are most likely to be involved in an enzyme that functions around pH 7? His (pK a ~ 6-7) Cys (pK a ~ 7-8)
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3. Covalent catalysis Covalent E-S intermediate
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4. Metal ion catalysis 6-23 enolase
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6-22 Hexokinase exhibits induced fit inactive active
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Which of the following is true about allosteric enzymes? A. Allosteric enzymes are always multimeric. B. Regulatory sites (allosteric sites) on an allosteric enzyme are always different from the catalytic site. C. Allosteric enzymes always change the conformation of the active site in response to binding of an allosteric modulator. D. Suicide inactivators are examples of allosteric modulators.
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Enzymes (Ch. 6) 3. Regulation (Modulation of activity of pre- existing pool of enzyme)
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cooperativity What can we say about the structure of an enzyme that exhibits sigmoidal kinetics? Multi-subunit
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ch06.3 - The active site of an enzyme is most complimentary...

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