Introduction to Enzyme and Coenzyme Chemistry - E-Library Home

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R OPP HO R' OH HO O (1) Via carbanion equivalents O O − O O O − H + − R R R' R R' R (2) Via carbonium ions + + + R R OPP R OPP H H (3) Via radical intermediates O O O O O Figure 7.1 Formation of carbon–carbon bonds.
158 Chapter 7 O H − OH O − O H OH O O − O OH Figure 7.2 Aldol reaction. Carbon–carbon bond formation via carbanion equivalents 7.2 Aldolases The aldol reaction involves the condensation of two carbonyl compounds via an enolate intermediate. The reaction is illustrated in Figure 7.2 for the case of the self-condensation of acetone in alkaline aqueous solution. A wide range of aldol reactions occur in biological systems that are used for the formation of carbon–carbon bonds. Cleavage of carbon–carbon bonds by the reverse reaction is also found. The enzymes which catalyse these aldol reactions are known as aldolases, and they are divided into two families based on their mechanism of action. The class I aldolases function by formation of an imine linkage between one carbonyl reagent and the e-amino group of an active site lysine residue, followed by deprotonation of the adjacent carbon to generate an enamine intermediate. Enamines are well-known enolate equivalents in synthetic organic chemistry: they can be formed under mild conditions by condensation of the carbonyl compound with a primary or secondary amine, and they react with carbonyl compounds also under mild conditions. The class II aldolases do not proceed through enamine intermediates but instead use a metal ion to assist catalysis. The metal ion is usually a divalent metal ion such as Mg 2þ ,Mn 2þ or Zn 2þ . The two classes are exempliWed by the enzyme fructose-1,6-bisphosphate aldolase, which is found in mammals as a class I enzyme, and in bacteria as a class II enzyme. CASE STUDY: Fructose-1,6-bisphosphate aldolase Fructose-1,6-bisphosphate aldolase catalyses the reversible reaction of dihydroxyacetone phosphate (DHAP) with glyceraldehyde 3-phosphate (G3P) to give fructose-1,6-bisphosphate, shown in Figure 7.3. O OH fructose-1,6-bisphosphate O 2− aldolase O 3 PO 2− O 3 PO 2− OPO + 3 OH OH OH fructose-1,6-bisphosphate dihydroxyacetone-1-phosphate Figure 7.3 Reaction catalysed by fructose-1,6-bisphosphate aldolase. O 2− OPO 3 OH glyceraldehyde-3-phosphate
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Introduction to Enzyme and Coenzyme
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Introduction to Enzyme and Coenzyme
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Contents Preface Representation of
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Contents vii 8 Enzymatic Addition/E
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Representation of Protein Three-Dim
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2 Chapter 1 H 2 N O NH 2 + H 2 O Ja
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4 Chapter 1 Table 1.1 The vitamins.
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6 Chapter 1 has very diVerent biolo
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2 All Enzymes are Proteins 2.1 Intr
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10 Chapter 2 (Gln). There are three
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12 Chapter 2 AAA Lys ACA Thr AGA Ar
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14 Chapter 2 H N O H N O Figure 2.8
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16 Chapter 2 (a) (b) Figure 2.12 St
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18 Chapter 2 Figure 2.14 Structure
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20 Chapter 2 (a) X Y Enzyme + Subst
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22 Chapter 2 maintaining protein te
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24 Chapter 2 surface glycoprotein g
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26 Chapter 2 O-linked glycosylation
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28 Chapter 2 Metalloproteins I. Ber
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30 Chapter 3 O N H R CO 2 H acylase
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32 Chapter 3 (a) Free energy uncata
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34 Chapter 3 Ester k rel Effective
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36 Chapter 3 3.4 The importance of
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38 Chapter 3 pKa Tyrosine CH 2 O H
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40 Chapter 3 glycoside hydrolysis (
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42 Chapter 3 O O Glu 143 O − R H
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44 Chapter 3 the hydroxyl groups of
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46 Chapter 3 E + S E + S ES' ES ‘
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48 Chapter 3 Examination of protein
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50 Chapter 3 (Note: Similar results
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52 Chapter 4 (1) Direct UV (2) Radi
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54 Chapter 4 Figure 4.3 PuriWcation
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56 Chapter 4 The two kinetic consta
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58 Chapter 4 Lineweaver−Burk Plot
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60 Chapter 4 E + S K i EI+ I ES E +
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62 Chapter 4 (2) by treatment with
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64 Chapter 4 In general the stereoc
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H D T CO 2 H CO − 2 T HO D H −
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68 Chapter 4 4.5 The existence of i
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70 Chapter 4 18O 18O 18 O O P O −
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72 Chapter 4 If a reaction involves
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74 Chapter 4 O D H ketosteroid isom
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76 Chapter 4 Table 4.3 Group speciW
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78 Chapter 4 [S] (mM) Rate of produ
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80 Chapter 4 Enzyme kinetics I.H. S
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82 Chapter 5 O = C NHR peptidase H
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84 Chapter 5 non-speciWc protease c
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86 Chapter 5 His 57 His 57 Asp 102
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88 Chapter 5 Other serine proteases
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90 Chapter 5 Figure 5.8 Structure o
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92 Chapter 5 now predominate Perhap
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OH R O Zn 2+ O O O Ph Glu 270 H 2 N
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96 Chapter 5 CASE STUDY: HIV-1 prot
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98 Chapter 5 HO Transition state pe
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100 Chapter 5 The aminoacyl group o
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102 Chapter 5 5.5 Enzymatic phospho
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104 Chapter 5 Figure 5.29 Structure
Page 117 and 118: 106 Chapter 5 Figure 5.32 Structure
Page 119 and 120: 108 Chapter 5 Adenosine 5 0 -tripho
Page 121 and 122: 110 Chapter 5 functional group. Gly
Page 123 and 124: 112 Chapter 5 CH 2 OH O RO HO OH O
Page 125 and 126: 114 Chapter 5 to these atoms that t
Page 127 and 128: 116 Chapter 5 Problems (1) Using pa
Page 129 and 130: 118 Chapter 5 (6) Retaining glycosi
Page 131 and 132: 120 Chapter 5 J.R. Knowles (1980) E
Page 133 and 134: 122 Chapter 6 +1.0 Redox potential
Page 135 and 136: Table 6.1 Classes of redox enzymes.
Page 137 and 138: 126 Chapter 6 An important point is
Page 139 and 140: 128 Chapter 6 O H − OH − O OH H
Page 141 and 142: 130 Chapter 6 one-electron transfer
Page 143 and 144: 132 Chapter 6 (a) R N H + N O R N H
Page 145 and 146: 134 Chapter 6 Inactivation by trany
Page 149 and 150: 138 Chapter 6 (a) (b) Figure 6.23 S
Page 151 and 152: 140 Chapter 6 glutathione called tr
Page 153 and 154: 142 Chapter 6 neither has a stable
Page 155 and 156: 144 Chapter 6 of the haem cofactor
Page 157 and 158: 146 Chapter 6 Figure 6.33 Active si
Page 159 and 160: 148 Chapter 6 HO H N N O O H N prol
Page 161 and 162: 150 Chapter 6 R R R O 2 , Fe 2+ O O
Page 163 and 164: 152 Chapter 6 CoA. Explain these re
Page 165 and 166: 154 Chapter 6 NADH models O. Almars
Page 167: 7 Enzymatic Carbon-Carbon Bond Form
Page 173 and 174: 162 Chapter 7 Figure 7.6 Active sit
Page 175 and 176: 164 Chapter 7 7.3 Claisen enzymes I
Page 177 and 178: 166 Chapter 7 CoAS O EnzB − H D T
Page 179 and 180: 168 Chapter 7 onto the acetyl-thioe
Page 181 and 182: 170 Chapter 7 In the case of erythr
Page 183 and 184: 172 Chapter 7 O HO O − O ATP ADP
Page 185 and 186: 174 Chapter 7 CO 2 − vitamin K-de
Page 187 and 188: 176 Chapter 7 7.8 Thiamine pyrophos
Page 189 and 190: 178 Chapter 7 HN N + N H NH S O OPP
Page 191 and 192: 180 Chapter 7 O OH OH camphor geran
Page 193 and 194: 182 Chapter 7 CH 3 * OPP (−)pinen
Page 197 and 198: 186 Chapter 7 C C C C C O OCH 3 C H
Page 199 and 200: 188 Chapter 7 AcO HO HO NHAc O OH +
Page 201 and 202: 190 Chapter 7 (9) Usnic acid is a n
Page 203 and 204: 192 Chapter 7 Radical couplings W.M
Page 205 and 206: 194 Chapter 8 C-O cleavage H E1 H C
Page 207 and 208: 196 Chapter 8 leads to the formatio
Page 209 and 210: 198 Chapter 8 aconitase citrate cis
Page 211 and 212: 200 Chapter 8 *H R H H CO 2 − NH
Page 213 and 214: 202 Chapter 8 EnzB − 2 H − O 2
Page 215 and 216: 204 Chapter 8 involves no change in
Page 217 and 218: 206 Chapter 8 Glyphosate H H N CO
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208 Chapter 8 (5) Chorismic acid (s
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9 Enzymatic Transformations of Amin
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CO − − 2 CO 2 H H CO 2 − N +
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214 Chapter 9 - BEnz CO − 2 Cl H
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216 Chapter 9 Arg 292 Arg 292 Lys 2
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218 Chapter 9 Arg 292 Asp 292 HN H
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220 Chapter 9 S − B 1 Enz H − C
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222 Chapter 9 9.6 N-Pyruvoyl-depend
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224 Chapter 9 The biosyntheses of n
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226 Chapter 9 Further reading Gener
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228 Chapter 10 B 1 - H + NH 3 CO
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230 Chapter 10 ‘low-barrier’ +
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232 Chapter 10 H S C 6 H 13 HN His
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234 Chapter 10 O H NH 3 CO 2 − CO
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236 Chapter 10 sub-units. Each sub-
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238 Chapter 10 Further reading Gene
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11 Radicals in Enzyme Catalysis 11.
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242 Chapter 11 CH 2 Co III Ad H OH
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244 Chapter 11 − O 2 C − O CO
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246 Chapter 11 H N H O 734 H N H PF
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248 Chapter 11 H H* + H + H 3 N CO
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250 Chapter 11 O HN NH + H 3 N H 3
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252 Chapter 11 cofactor is involved
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254 Chapter 11 Protein Radicals J.
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256 Chapter 12 self-splicing reacti
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258 Chapter 12 Figure 12.2 Structur
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260 Chapter 12 antigen combining si
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262 Chapter 12 R O OR' OH − R O
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264 Chapter 12 CO 2 − − O 2 C O
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266 Chapter 12 (1) Selective substr
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268 Chapter 12 HO O HO OH HO OH O O
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270 Chapter 12 Problems (1) How rev
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Appendix 1: Cahn-Ingold-Prelog Rule
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Appendix 2: Amino Acid Abbreviation
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276 Appendix 3 Preparation of orang
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278 Appendix 4 (2) Intramolecular a
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280 Appendix 4 from water at a-posi
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282 Appendix 4 Chapter 8 (1) Treat
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284 Appendix 4 (b) Formation of rad
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286 Index b-hydroxydecanoyl thioest
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288 Index glycosylation 26-7 glysop
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290 Index phenylalanine ammonia lya
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292 Index transition states 31-2 an
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