Herbicide classes in development : mode of action, targets, genetic engineering, chemistry /

1 Acetolactate Synthase Inhibitors Tsutomu Shimizu and Ishizue Nakayama and Kozo Nagayama and Takeshige Miyazawa and Yukio Nezu
1.1 Introduction p. 1
1.2 Acetolactate Synthase-Inhibiting Herbicides Actively Developed in the Late 1990s p. 2
1.3 Discovery of Pyrimidinyl Carboxy Herbicides (Pyrimidinylsalicylate Class Herbicides) p. 5
1.3.1 Discovery of the Lead Structures p. 5
1.3.2 Discovery and Optimizations of the Secondary Lead Structure p. 7
1.3.3 Further Optimizations of the Pyrimidinyl Carboxy Herbicides p. 9
1.4 Herbicidal Activity of Pyrimidinyl Carboxy Herbicides p. 10
1.4.1 Pyrithiobac-Sodium for Use in Cotton p. 10
1.4.2 Bispyribac-Sodium for Use in Rice p. 10
1.4.3 Bispyribac-Sodium for Vegetation Management p. 11
1.4.4 Pyriminobac-Methyl for Use in Rice p. 11
1.5 Physiological Plant Response to Pyrimidinyl Carboxy Herbicides p. 12
1.6 Mode of Action and Selectivity of Pyrimidinyl Carboxy Herbicides p. 13
1.6.1 Primary Target p. 13
1.6.2 Inhibition of Bacterial Acetolactate Synthase p. 14
1.6.3 Selectivity p. 15
1.7 Biological Characteristics of the Target Enzyme p. 16
1.7.1 Kinetic Studies of Plant Acetolactate Synthase p. 16
1.7.2 Subunit Compositions of Plant Acetolactate Synthase p. 17
1.7.3 Recombinant Systems p. 18
1.8 Inhibition Mechanism of the Target Enzyme by Pyrimidinyl Carboxy Herbicides p. 19
1.8.1 Inhibition Kinetics with Plant Acetolactate Synthase p. 19
1.8.2 Inhibition Kinetics with Bacterial Acetolactate Synthase p. 22
1.9 Molecular Genetics of Target Enzyme p. 22
1.9.1 Acetolactate Synthase Genes of Plants p. 22
1.9.2 Acetolactate Synthase-Inhibiting Herbicide-Resistant Crops (Including Arabidopsis thaliana) and Their Acetolactate Synthase Genes p. 24
1.9.3 Acetolactate Synthase-Inhibiting Herbicide-Resistant Weeds and Their Acetolactate Synthase Genes p. 28
1.9.4 Genetic Engineering p. 31
References p. 32
2 Bleaching Herbicides: Action Mechanism in Carotenoid Biosynthesis, Structural Requirements and Engineering of Resistance Gerhard Sandmann
2.1 Herbicidal Effect and Mode of Action p. 43
2.2 Interaction of Inhibitors with Carotene Desaturation p. 44
2.3 Structural Requirements for an Inhibitor of Phytoene Desaturase p. 47
2.4 Strategies for Genetic Engineering of Herbicide Resistance by Modification of the Carotenogenic Pathway p. 50
2.4.1 Overexpression of a Susceptible Lycopene Cyclase in Synechococcus p. 50
2.4.2 Selection of Mutants with Resistant Phytoene Desaturase and Gene Transfer into Tobacco p. 51
2.4.3 Naturally Resistant Phytoene Desaturase from Bacteria and Genetic Engineering of a Resistant Tobacco p. 52
2.5 Conclusion and Perspectives p. 54
References p. 55
3 Inhibitors of Aromatic Amino Acid Biosynthesis (Glyphosate) Donald R. Geiger and Mark A. Fuchs
3.1 Introduction p. 59
3.2 Symptoms of Herbicidal Activity p. 60
3.3 Mode of Action of Glyphosate p. 62
3.3.1 Overview of the Mode of Action p. 62
3.3.2 Primary Mode of Action p. 64
3.3.2.1 Biochemical Characteristics of the Target Enzyme p. 64
3.3.2.2 Structural Characteristics of the Target Enzyme p. 65
3.3.2.3 Interaction Between 5-Enolpyruvylshikimate 3-Phosphate Synthase and Glyphosate p. 66
3.3.2.4 Molecular Requirements for Herbicidal Activity of Glyphosate p. 69
3.3.3 Secondary Physiological Consequences of Inhibition of 5-Enolpyruvylshikimate 3-Phosphate Synthase p. 70
3.3.3.1 Inhibition of Chorismate Synthesis p. 70
3.3.3.2 Depletion of Photosynthetic Carbon Reduction Cycle Intermediate Metabolites p. 71
3.3.3.3 Development of Secondary Damage Symptoms p. 72
3.3.3.4 Bases of Development of Lethal Symptoms Among Species p. 72
3.4 Mechanisms for Resistance and Tolerance to Glyphosate p. 75
3.4.1 Development of Commercially Valuable Glyphosate-Resistant Plants p. 75
3.4.2 Tolerance to Field Doses of Glyphosate in Field-Grown Plants p. 77
3.5 Summary p. 79
References p. 80
4 Inhibitors of Glutamine Synthetase Guenter Donn and Helmut Kocher
4.1 Introduction p. 87
4.2 Plant Glutamine Synthetase Isoforms and Their Function p. 87
4.3 Glutamine Synthetase Inhibitors p. 90
4.4 Discovery of the Herbicidal Activity of Phosphinothricin and Bialaphos p. 91
4.5 Mode of Glutamine Synthetase Inhibition p. 92
4.6 Effects of Glutamine Synthetase Inhibitors in Plants p. 94
4.6.1 Visible Symptoms of Herbicidal Action p. 94
4.6.2 Physiological Effects of Glutamine Synthetase Inhibition in Plants by Phosphinothricin p. 94
4.7 Attempts to Generate Selectivity for Glufosinate p. 96
4.7.1 Attempts to Select Glufosinate Tolerant Mutants p. 97
4.7.2 Metabolic Inactivation of Glufosinate by Bar and Pat Enzymes p. 98
References p. 99
5 Acetyl-CoA Carboxylase Inhibitors Malcolm D. Devine
5.1 Introduction p. 103
5.2 Symptoms of Herbicidal Activity p. 103
5.3 Biochemical Characteristics of the Target Enzyme p. 104
5.4 Mode of Action of Cyclohexanedione and Aryloxyphenoxypropanoate Herbicides p. 105
5.5 Assays for Acetyl-CoA Carboxylase Activity p. 106
5.6 Molecular Genetics of Resistance to Acetyl-CoA Carboxylase Inhibitors p. 107
References p. 110
6 Inhibitors of Biosynthesis of Very-Long-Chain Fatty Acids Peter Boger and Bernd Matthes
6.1 Introduction p. 115
6.2 The Model System p. 119
6.3 Very Long-Chain Fatty Acid Biosynthesis Inhibition in Intact Leaves p. 123
6.4 The Cell-Free Elongase System p. 127
6.5 Assumptions of the Reaction Mechanism p. 131
6.6 Considerations on Resistance p. 133
References p. 135
7 Cellulose Biosynthesis Inhibitor Herbicides Kevin C. Vaughn
7.1 Introduction p. 139
7.2 Mode of Action Studies p. 140
7.2.1 Cell Plates p. 140
7.2.2 Developing Cotton Fibers p. 142
7.2.3 Azido-Dichlobenil Derivatives p. 144
7.3 Resistant Biotypes p. 145
7.4 Habituation p. 146
7.5 The Unusual Case of Quinclorac p. 148
7.6 Conspectus p. 148
References p. 148
8 Inhibitors of Protoporphyrinogen Oxidase: A Brief Update Hiroshi Matsumoto
8.1 Introduction p. 151
8.2 Protoporphyrinogen Oxidase Inhibitors and Their Mode of Action p. 152
8.3 Biochemical Characterization of Protoporphyrinogen Oxidase p. 154
8.4 Protoporphyrinogen Oxidase Genes and Transgenic Herbicide-Resistant Plants p. 154
8.5 Recent Advances in QSAR Studies p. 156
8.6 Antioxidative Stress Responses of Plants to Protoporphyrinogen Oxidase Inhibitors p. 157
References p. 158
9 Genetic Engineering of Herbicide-Resistant Plants Mamoru Horikoshi
9.1 Introduction p. 163
9.2 Strategy p. 164
9.2.1 The Gene Encoding the Herbicide-Inactivating Enzyme p. 164
9.2.2 Mutant or Foreign Gene Encoding the Target Enzyme with Low Affinity to the Herbicide p. 165
9.3 Cloning of the Genes p. 166
9.3.1 Genetic Resource p. 166
9.3.1.1 Microorganism p. 167
9.3.1.2 Plant Tissue Culture p. 167
9.3.1.3 Mutant Plants p. 168
9.3.2 Cloning Methods p. 168
9.3.2.1 The Information of Protein p. 168
9.3.2.2 The Information of Nucleic Acid p. 169
9.3.2.3 Bacterial Genetics p. 169
9.4 Gene Transfer p. 169
9.4.1 PEG-Mediated Gene Transfer and Electroporation p. 170
9.4.2 Particle Bombardment p. 170
9.4.3 Agrobacterium-Mediated Gene Transfer p. 170
9.5 Vector Constructs p. 171
9.5.1 Expression Cassettes p. 171
9.5.1.1 Promoter and Terminator p. 171
9.5.1.2 Selection Marker Gene p. 172
9.5.1.3 Enhancer Sequence p. 172
9.5.1.4 Transit Peptide Sequence p. 172
9.5.2 Type of Vectors p. 172
9.5.2.1 Vector for Direct Gene Transfer p. 172
9.5.2.2 Vectors for Agrobacterium-Mediated Gene Transfer p. 173
9.5.2.3 Other Vectors p. 173
9.6 Conclusions p. 173
References p. 174
10 Major Synthetic Routes for Modern Herbicide Classes and Agrochemical Characteristics Kenji Hirai and Atsushi Uchida and Ryuta Ohno
10.1 Introduction p. 179
10.2 Acetolactate Synthase Inhibitors p. 179
10.2.1 Sulfonylurea Acetolactate Synthase Inhibitors p. 180
10.2.1.1 Practical Sulfonylurea Acetolactate Synthase Inhibitors p. 180
10.2.1.2 Structural Evolution of Sulfonylurea Acetolactate Synthase Inhibitors p. 186
10.2.1.3 Major Synthetic Routes for Sulfonylureas p. 193
10.2.2 Triazolinone Acetolactate Synthase Inhibitors p. 196
10.2.2.1 Practical Triazolinone Acetolactate Synthase Inhibitors p. 196
10.2.2.2 Structural Evolution of Triazolinone Acetolactate Synthase Inhibitors p. 197
10.2.2.3 Major Synthetic Routes for Triazolinone Acetolactate Synthase Inhibitors p. 197
10.2.3 Triazolopyrimidine Acetolactate Synthase Inhibitors p. 197
10.2.3.1 Practical Triazolopyrimidine Acetolactate Synthase Inhibitors p. 199
10.2.3.2 Structural Evolution of Triazolopyrimidine Acetolactate Synthase Inhibitors p. 201
10.2.3.3 Major Synthetic Routes for Triazolopyrimidine Acetolactate Synthase Inhibitors p. 202
10.2.4 Acetolactate Synthase Inhibitor-Like Miscellaneous Pyrimidines and Related Compounds p. 202
10.2.5 Pyrimidyl(thio)oxybenzoate Acetolactate Synthase Inhibitors p. 202
10.2.5.1 Practical Pyrimidyl(thio)oxybenzoate Acetolactate Synthase Inhibitors p. 202
10.2.5.2 Structural Evolution of Pyrimidyl(thio)oxybenzoate Acetolactate Synthase Inhibitors p. 204
10.2.5.3 Major Synthetic Routes for Pyrimidyl(thio)oxybenzoate Acetolactate Synthase Inhibitors p. 209
10.2.6 Imidazolinone Acetolactate Synthase Inhibitors p. 210
10.2.6.1 Practical Imidazolinone Acetolactate Synthase Inhibitors p. 210
10.2.6.2 Structural Evolution of Imidazolinone ALS Inhibitors p. 212
10.2.6.3 Major Synthetic Routes for Imidazolinone Acetolactate Synthase Inhibitors p. 212
10.3 Carotenogenesis Inhibitors p. 213
10.3.1 Phytoene Desaturase Inhibitors p. 213
10.3.1.1 Practical Phytoene Desaturase Inhibitors p. 213
10.3.1.2 Structural Evolution of Phytoene Desaturase Inhibitors p. 216
10.3.1.3 Major Synthetic Routes for Phytoene Desaturase Inhibitors p. 218
10.3.2 4-Hydroxyphenylpyruvate Dioxygenase Inhibitors p. 221
10.3.2.1 Practical 4-Hydroxyphenylpyruvate Dioxygenase Inhibitors p. 221
10.3.2.2 Structural Evolution of 4-Hydroxyphenylpyruvate Dioxygenase Inhibitors p. 223
10.3.2.3 Major Synthetic Routes for 4-Hydroxyphenylpyruvate Dioxygenase Inhibitors p. 229
10.3.3 Other Carotenogenesis Inhibitors p. 229
10.4 Aromatic Amino Acid Biosynthesis Inhibitors p. 232
10.5 Glutamine Synthetase Inhibitors p. 234
10.6 Acetyl CoA Carboxylase (ACCase) Inhibitors p. 234
10.6.1 Practical Acetyl CoA Carboxylase Inhibitors p. 235
10.6.2 Structural Evolution of Acetyl CoA Carboxylase Inhibitors p. 238
10.6.3 Major Synthetic Routes for Acetyl CoA Carboxylase Inhibitors p. 238
10.7 Very Long-Chain Fatty Acids Biosynthesis Inhibitors p. 243
10.7.1 Practical Chloroacetamide Very Long-Chain Fatty Acids Biosynthesis Inhibitors p. 244
10.7.2 Other Very Long-Chain Fatty Acids Biosynthesis Inhibitors p. 246
10.8 Cellulose Biosynthesis Inhibitors p. 249
10.8.1 Practical Cellulose Biosynthesis Inhibitors p. 249
10.8.2 Structural Evolution of Cellulose Biosynthesis Inhibitors p. 253
10.8.3 Major Synthetic Routes for Cellulose Biosynthesis Inhibitors p. 253
10.9 Protoporphyrinogen-IX Oxidase Inhibitors p. 255
10.9.1 Heterocycle Protoporphyrinogen-IX Oxidase Inhibitors p. 256
10.9.1.1 First-Generation Heterocycle Protoporphyrinogen-IX Oxidase Inhibitors p. 259
10.9.1.2 Second-Generation Heterocycle Protoporphyrinogen-IX Oxidase Inhibitors p. 260
10.9.2 Structural Evolution of Protoporphyrinogen-IX Oxidase Inhibitors Since 1995 p. 262
10.9.2.1 Structural Evolution of First-Generation Heterocycle Protoporphyrinogen-IX Oxidase Inhibitors p. 263
10.9.2.2 Structural Evolution of Second-Generation Heterocycle Protoporphyrinogen-IX Oxidase Inhibitors p. 263
10.9.2.3 Next-Generation Heterocycle Protoporphyrinogen-IX Oxidase Inhibitors p. 271
10.9.3 Major Synthetic Routes for Protoporphyrinogen-IX Oxidase Inhibitors p. 274
10.10 Notes p. 278
Patent Literature p. 280
11 Diverse Response of Plants Towards Chiral Phytotoxic Chemicals Hiroyoshi Omokawa
11.1 Introduction p. 291
11.2 Diverse Response of Optically Active Herbicides p. 292
11.2.1 Qualitatively Similar Enantioselective Action p. 294
11.2.2 Enantiomeric Metabolism p. 295
11.2.3 Chiral Inversion p. 296
11.3 Diverse Response of Plants Through Chirality p. 297
11.3.1 Chiral s-Triazines p. 298
11.3.1.1 Light-Dependent and Light-Independent Growth Inhibition p. 298
11.3.1.2 Cytokinin-Like Activity p. 300
11.3.2 Chiral Ureas p. 302
11.3.2.1 Enantioselective Phytotoxicity p. 302
11.3.2.2 Stress-Relieving Activity p. 304
11.3.2.3 Cross Intergenus Selective Phytotoxicity Among Gramineae p. 306
11.4 Chirality and Activity Relationship p. 307
11.4.1 Binding Direction of s-Triazines at the Photosystem II Reaction Center p. 308
11.4.2 Eudismic Analysis p. 311
11.4.2.1 Photosystem II Inhibition p. 311
11.4.2.2 Light-Independent Inhibition p. 313
11.4.2.3 Stress Relief p. 313
References p. 314
12 Transcuticular Penetration of Foliar-Applied Pesticides - Its Analysis by a Logistic-Kinetic Penetration Model Tadakazu Watanabe
12.1 Introduction p. 319
12.2 Overview p. 320
12.3 Logistic-Kinetic Transcuticular Penetration Model of Foliar-Applied Pesticides p. 323
12.3.1 Scenario p. 323
12.3.2 Transcuticular Penetration-Measuring Cell p. 326
12.4 Parameters and Factors Governing Transcuticular Penetration Kinetics of Foliar-Applied Pesticides p. 327
12.4.1 Adaptability of the Logistic-Kinetic Penetration Model p. 327
12.4.2 Factors Influencing Transcuticular Penetration Kinetics p. 328
12.4.3 Effect of Molecular Parameters of Pesticides on Transcuticular Penetration Kinetics p. 328
12.5 Effects of Adjuvants on Transcuticular Penetration Kinetics of Foliar-Applied Pesticides p. 330
12.5.1 Analysis of Adjuvant Action (Adjuvancy) p. 330
12.5.2 Effect of Triton Surfactants p. 331
12.5.3 Effect of Emulsifiable Oils p. 332
12.5.4 Effect of Humectants p. 332
12.5.5 Effect of Amine Surfactants on Glyphosate Penetration p. 333
12.6 Discussion and Conclusions p. 334
References p. 337
13 Structure-Activity Correlation of Very Long-Chain Fatty Acid Biosynthesis Inhibitors Ko Wakabayashi and Peter Boger
13.1 Introduction p. 341
13.2 Very Long-Chain Fatty Acid Biosynthesis Inhibition by Herbicides p. 341
13.3 Very Long-Chain Fatty Acid Biosynthesis Inhibition by Thenylchlor and Its Analogs p. 345
13.4 Action of Cafenstrole and its Analogs p. 349
13.5 Action of Indanofan and its Analogs p. 351
13.6 Outlook p. 353
References p. 356
Index p. 359