45) How do the intermediate steps in multisubstrate enzyme mechanisms differ? Section: 8.448) How are the types of inhibition kinetically distinguishable? .Section: 8.550) What are transition-state analogs? Section: 8.5Chapter 9 Catalytic StrategiesMultiple-Choice Questions2)
What type of reaction is catalyzed by proteases?
DSection: 9.13)What metal ion is required by carbonic anhydrase for activity?A)Zn2+B)Mg2+C)Cu2+D)Fe2+E)Ni2+Answer: ASection: 9.28)What metal ion is frequently found in enzyme active sites that act on phosphate-containing substrates?BSection: 9.3Fill-in-the-Blank Questions11. 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: 9.113. In trypsin, the specificity pocket contains a/an ______________ residue that binds to thepositive charge of the K or R residue of the substrate.Section: 9.114. The reaction center of most carbonic anhydrases is a zinc ion bound to water and _______________ residues of the enzyme.Section: 9.215. In chymotrypsin, the tetrahedral intermediate transition state is stabilized by a structural feature referred to as the “___________________” hole.Section: 9.2