Chapter 9 Catalytic Strategies 2 7 A technique that aids in determination of structure/function relationships in enzymes. Ans:c Section:9.1 8 The metal ion frequently found at active sites containing phosphate groups. Ans:g Section:9.3 9 A technique that can be used to determine mechanisms when chiral molecules are involved in reactions. Ans:f Section:9.3 10 Inverted repeats in double-stranded DNA create this type of symmetry. Ans:h Section:9.3 Fill in the Blank Questions 1 For a protease inhibitor to be effective,it must be for one enzyme. Ans:specific Section:9.1 2 The catalytic mechanism of adenylate kinase,in which the substrates are oriented to stabilize the transition state,is called Ans:catalysis by approximation Section:9.4 3 A-T base pairs are easily interrupted,as they contain only hydrogen bonds versus hydrogen bonds found in G-C base pairs. Ans:two,three Section:9.3 4 The mechanism of chymotrypsin involves the formation of an unstable shaped intermediate that is stabilized by the oxyanion hole. Ans:tetrahetral Section:9.1 5 In trypsin,the specificity pocket contains a/an residue that binds to the positive charge of the K or R residue of the substrate. Ans:aspartyl,aspartic,or D Section:9.1 6 The reaction center of most carbonic anhydrases is a zinc ion bound to water and residues of the enzyme. Ans:histidine Section:9.2Chapter 9 Catalytic Strategies 2 7 ____________ A technique that aids in determination of structure/function relationships in enzymes. Ans: c Section: 9.1 8 ____________ The metal ion frequently found at active sites containing phosphate groups. Ans: g Section: 9.3 9 ____________ A technique that can be used to determine mechanisms when chiral molecules are involved in reactions. Ans: f Section: 9.3 10 ____________ Inverted repeats in double-stranded DNA create this type of symmetry. Ans: h Section: 9.3 Fill in the Blank Questions 1 For a protease inhibitor to be effective, it must be _________________ for one enzyme. Ans: specific Section: 9.1 2 The catalytic mechanism of adenylate kinase, in which the substrates are oriented to stabilize the transition state, is called ___________________. Ans: catalysis by approximation Section: 9.4 3 A-T base pairs are easily interrupted, as they contain only _____ hydrogen bonds versus _______ hydrogen bonds found in G-C base pairs. Ans: two, three Section: 9.3 4 The mechanism of chymotrypsin involves the formation of an unstable __________________ - shaped intermediate that is stabilized by the oxyanion hole. Ans: tetrahetral Section: 9.1 5 In trypsin, the specificity pocket contains a/an ______________ residue that binds to the positive charge of the K or R residue of the substrate. Ans: aspartyl, aspartic, or D Section: 9.1 6 The reaction center of most carbonic anhydrases is a zinc ion bound to water and _______________ residues of the enzyme. Ans: histidine Section: 9.2