A 100 M B 133 M C 0667 M D 0250 M E 0150 M Ans C The conversion

A 100 m b 133 m c 0667 m d 0250 m e 0150 m ans c the

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A) 1.00 M B) 1.33 M C) 0.667 M D) 0.250 M E) 0.150 M Ans: C Section: 6.3 36 The conversion of glucose-6-phosphate to fructose-6-phosphate is catalyzed by an isomerase enzyme. Glucose-6-phosphate was mixed with the enzyme under standard conditions and the reaction was allowed to come to equilibrium. If the K eq is 0.50, what is the G°′ in kJ/mol? A) +0.99 B) +1.71 C) 0, as defined by equilibrium conditions D) –0.99 5
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Chapter 6 Basic Concepts of Enzyme Action E) –2.27 Ans: B Section: 6.3 37 The conversion of glucose-6-phosphate to fructose-6-phosphate is catalyzed by an isomerase enzyme. Under cellular conditions (37 o C), the glucose-6-phosphate is 6.6 μM and the fructose- 6-phosphate is 1.3 μM. If the K eq ′ is 0.50, what is the ΔG in kJ/mol ? (Hint: Use the G°′ from the previous question.) A) +4.19 B) –1.81 C) –4.03 D) –2.50 Ans: D Section: 6.4 38 That many transition-state analogs bind more tightly than the native substrate reinforces the concept that: A) transition-state analogs are planar structures. B) transition-state analogs are highly charged at physiological pH. C) binding to the transition state is through a lock-and-key-mechanism. D) transition-state analogs are hydrophobic. E) binding to the transition state is through an induced-fit mechanism. Ans: E Section: 6.4 39 How do enzymes facilitate the formation of the transition state? Ans: When enzymes bind substrate, free energy is released by the formation of a large number of weak interactions. Only the correct substrate can participate in the most or all possible interactions with the enzyme. The full complement of interactions occurs when the transition state is achieved. This causes maximal release of free energy. Section: 6.4 40 How is the substrate bound to the active site? Ans: The active site is a small part of the total enzyme structure. It is usually a three- dimensional cleft or crevice, which is formed by amino acid residues from different regions of the polypeptide chain. The substrate is bound by multiple noncovalent attractions such as electrostatic interactions, hydrogen bonds, van der Waals forces, and hydrophobic interactions. The specificity is dependent on the precise arrangement of the various functional groups in the binding site. Section: 6.4 6
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