C irreversible Ans D How is specificity determined by

C irreversible ans d how is specificity determined by

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C) irreversible Ans: D Section: 8.2 23 How is specificity determined by chymotrypsin? A) interaction of the active site amino acids with the substrate B) binding of the N-terminus amino acid at the active site C) covalent binding of a his residue to the substrate D) conformational change upon binding of substrate E) binding of the proper amino acid into a deep pocket on the enzyme Ans: E Section: 8.3 24 An enzyme is optimally active at neutral pH , but activity drops off sharply if the pH is changed , This enzyme is likely to have what in the active site ? A) the side chains of aspartate and glutamate B) two histidine amino acid side chains C) a glycine amino acid D) polar side chains E) nonpolar side chains Ans: A Section: 8.2 25 In this catalytic strategy, a cofactor serves as an electrophile to stabilize a negative charge on a reaction intermediate. A) covalent catalysis B) general acid–base catalysis C) metal ion catalysis D) catalysis by approximation and orientation 3
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Chapter 8 Mechanisms and Inhibitors E) irreversible catalysis Ans: C Section: 8.2 26 In designing a drug to inhibit an enzyme specific to a new strain of E. coli , would you choose a group-specific inhibitor or a mechanism-based inhibitor? Why? A) Mechanism-based because it mimics the transition-state intermediate. B) Mechanism-based because it modifies a catalytically active group on the enzyme. C) Group-specific because it will react to specific R-groups in the enzyme. D) Group-specific because its activity can be enhanced with an allosteric inhibitor. E) Group-specific because they are structurally similar to the enzyme’s substrate. Ans: B Section: 8.2 27 What two biochemical principles explain the enzyme activity versus temperature curve? A) The rising portion of the curve is due to increase in Brownian motion of the molecules, and the decrease is due to activation of inhibitor molecules.
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