How do the intermediate steps in multisubstrate

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45) How do the intermediate steps in multisubstrate enzyme mechanisms differ? Section: 8.4 48) How are the types of inhibition kinetically distinguishable? . Section: 8.5 50) What are transition-state analogs? Section: 8.5 Chapter 9 Catalytic Strategies Multiple-Choice Questions 2) What type of reaction is catalyzed by proteases?
D Section: 9.1 3)What metal ion is required by carbonic anhydrase for activity? A)Zn2+B)Mg2+C)Cu2+D)Fe2+E)Ni2+Answer: A Section: 9.2 8)What metal ion is frequently found in enzyme active sites that act on phosphate-containing substrates? B Section: 9.3 Fill-in-the-Blank Questions 11. The catalytic mechanism of carbonic anhydrase, in which the substrates are simply oriented to stabilize the transition state, is called ___________________. Section: Introduction
12. The mechanism of chymotrypsin involves the formation of an unstable __________________ -shaped intermediate that is stabilized by the oxyanion hole. Section: 9.1 13. In trypsin, the specificity pocket contains a/an ______________ residue that binds to thepositive charge of the K or R residue of the substrate. Section: 9.1 14. The reaction center of most carbonic anhydrases is a zinc ion bound to water and _______________ residues of the enzyme. Section: 9.2 15. In chymotrypsin, the tetrahedral intermediate transition state is stabilized by a structural feature referred to as the “___________________” hole. Section: 9.2

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