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El. knyga: Amino Acids in Higher Plants [CABI E-books]

Contributions by (Monsanto), Contributions by (San Francisco State University), Contributions by (New Mexico State University), Contributions by (Monsanto), Contributions by , Edited by (formerly Scottish Agricultural College, UK), Contributions by , Contributions by (Universidad de Malaga-;), Contributions by (Texas A&M University System, USA), Contributions by (Rochester Institute of Technology)
  • Formatas: 632 pages
  • Išleidimo metai: 10-Apr-2015
  • Leidėjas: CABI Publishing
  • ISBN-13: 9781780642635
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  • CABI E-books
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Amino Acids in Higher PlantsDidesnis paveikslėlis
  • Formatas: 632 pages
  • Išleidimo metai: 10-Apr-2015
  • Leidėjas: CABI Publishing
  • ISBN-13: 9781780642635
Kitos knygos pagal šią temą:
Wiley OnlineMore info about CABI e-books
Amino acids play a role in the defence mechanisms and stress responses of plants, as well as in food quality and safety for humans and animals. Recent advances in the field make a comprehensive overview of the information a necessity; this book collates chapters on plant enzymes and metabolism, modulation, molecular aspects and secondary products. Also including information on ecology, the environment and mammalian nutrition and toxicology, it provides an authoritative resource.
Contributors xix
Preface xxiii
Glossary xxvii
PART I ENZYMES AND METABOLISM
1 Glutamate Dehydrogenase
1(29)
G.O. Osuji
W.C. Madu
1.1 Abstract
1(1)
1.2 Introduction
2(1)
1.3 Glutamate Dehydrogenase Structure and Localization
2(1)
1.4 Control Plants and Control Glutamate Dehydrogenase
3(1)
1.5 Availability of Ammonium Ions
4(1)
1.5.1 Ammonium ion contents of experimental tissues and plants
4(1)
1.5.2 Glutamate deamination in mitochondria
5(1)
1.6 Glutamate Dehydrogenase-Linked Schiff Base Amination Complex
5(2)
1.6.1 Pesticide treatment and ammonium ion fertilization
5(1)
1.6.2 Pesticide treatment, ammonium ion fertilization and protein contents
6(1)
1.7 Protect the Glutamine Synthetase-Glutamate Synthase Cycle in Glutamate Dehydrogenase Research
7(1)
1.8 Molecular Biology of Glutamate Dehydrogenase
8(12)
1.8.1 The supply of α-ketoglutarate from the citric acid cycle to glutamate dehydrogenase and glutamate synthase
8(8)
1.8.2 Aminating and deaminating activities
16(3)
1.8.3 Amination-based crop yield doubling biotechnology
19(1)
1.8.4 The aminating cassette of glutamate dehydrogenase isoenzymes
19(1)
1.9 Food Security
20(3)
1.10 Conclusions
23(7)
Acknowledgements
24(1)
References
24(6)
2 Alanine Aminotransferase: Amino Acid Metabolism in Higher Plants
30(27)
A. Raychaudhuri
2.1 Abstract
30(1)
2.2 Introduction
30(1)
2.3 Structure and Functions of Alanine
31(1)
2.3.1 Structure of alanine
31(1)
2.3.2 Functions of alanine
31(1)
2.4 Alanine Metabolism
32(1)
2.4.1 Alanine metabolism by alanine aminotransferase
33(1)
2.5 Specific Cellular and Sub-Cellular Functions of Alanine Aminotransferase
33(2)
2.5.1 Homologues and tissue localization
34(1)
2.5.2 Sub-cellular localization
35(1)
2.6 A Phylogenetic Analysis of Alanine Aminotransferase
35(1)
2.7 Purification of Alanine Aminotransferase
36(1)
2.8 Protein Characterization of Alanine Aminotransferase
36(9)
2.8.1 Subunits and substrate specificities
36(2)
2.8.2 Kinetics and reaction mechanism
38(5)
2.8.3 Inhibitors of the enzyme
43(1)
2.8.4 Crystal structure
44(1)
2.9 Diverse Roles of Alanine Aminotransferase in Plants
45(5)
2.9.1 Roles in metabolism
45(1)
2.9.1.1 Roles in carbon metabolism
45(2)
2.9.1.2 Roles in photorespiration
47(1)
2.9.1.3 Role in nitrogen use efficiency
48(1)
2.9.2 Role in stress biology
48(1)
2.9.2.1 Roles in hypoxia
49(1)
2.9.2.2 Other abiotic and biotic stresses
50(1)
2.10 Conclusions
50(7)
References
52(5)
3 Aspartate Aminotransferase
57(11)
C.D. Leasure
Z-H. He
3.1 Abstract
57(1)
3.2 Introduction
57(1)
3.3 The Vitamin Cofactor
58(1)
3.4 Enzyme Function
58(3)
3.4.1 The reaction mechanism
60(1)
3.4.2 Enzyme properties
61(1)
3.5 Enzyme Structure
61(1)
3.5.1 K258
61(1)
3.5.2 R292*
61(1)
3.5.3 R386
61(1)
3.5.4 D222
62(1)
3.5.5 Y225
62(1)
3.6 Enzyme Genetics
62(1)
3.7 The Enzyme during Plant Development
63(1)
3.8 The Role of Aspartate in Plants
63(1)
3.8.1 C4 metabolism
64(1)
3.9 Other Roles of Aspartate Aminotransferase
64(1)
3.9.1 Moonlighting
64(1)
3.9.2 Genetic engineering with aspartate aminotransferases
64(1)
3.10 Future Research
65(1)
3.11 Conclusions
65(3)
References
65(3)
4 Tyrosine Aminotransferase
68(14)
A.O. Hudson
4.1 Abstract
68(1)
4.2 Introduction
68(2)
4.2.1 Aminotransferases: a brief introduction
68(1)
4.2.2 A brief history of aminotransferase activity in plants
69(1)
4.2.3 Oligomeric state, cofactor requirement and mechanism of action of action of aminotransferases
69(1)
4.3 Aminotransferases from the Model Organism Arabidopsis thaliana
70(1)
4.4 The Anabolism of Tyrosine and Phenylalanine in Plants and Bacteria
71(3)
4.4.1 The anabolism of tyrosine and phenylalanine in bacteria
71(2)
4.4.2 A second pathway for the synthesis of tyrosine and phenylalanine in plants
73(1)
4.5 Properties of Tyrosine Aminotransferase Annotated by the Locus Tag At5g36160 from Arabidopsis thaliana
74(3)
4.5.1 Kinetic and physical properties
74(2)
4.5.2 Substrate specificity
76(1)
4.5.3 In vivo analysis of tyrosine aminotransferase
76(1)
4.6 The Role of Tyrosine Aminotransferase in Plants
77(2)
4.7 Conclusions
79(3)
Acknowledgement
79(1)
References
79(3)
5 An insight Into the Role and Regulation of Glutamine Synthetase in Plants
82(18)
C. Sengupta-Gopalan
J.L. Ortega
5.1 Abstract
82(1)
5.2 Introduction
82(1)
5.3 Classification of Glutamine Synthetase
83(1)
5.4 Glutamine Synthetase in Plants
83(3)
5.4.1 Chloroplastic glutamine synthetase
84(1)
5.4.2 Cytosolic glutamine synthetase
84(2)
5.5 Modulation of Glutamine Synthetase Expression in Transgenic Plants
86(2)
5.6 Regulation of Glutamine Synthetase Gene Expression in Plants
88(5)
5.6.1 Transcriptional regulation
88(1)
5.6.2 Post-transcriptional regulation
89(2)
5.6.3 Translational regulation
91(1)
5.6.4 Post-translational regulation
91(2)
5.7 Concluding Remarks
93(7)
Acknowledgements
94(1)
References
94(6)
6 Asparagine Synthetase
100(29)
S.M.G. Duff
6.1 Abstract
100(1)
6.2 Introduction: the Role of Asparagine and Asparagine Synthetase in Nitrogen Metabolism
100(1)
6.3 Asparagine: History, Chemical Properties and Role in Plants
101(1)
6.4 Asparagine Synthetase: an Early History of Research in Humans, Microbes and Plants
102(2)
6.5 The Occurrence of Asparagine Synthetase in Nature
104(1)
6.6 The Expression and Function of Asparagine Synthetase in Plants
105(5)
6.6.1 Nutritional and mineral deficiency
105(1)
6.6.2 Seed germination
105(1)
6.6.3 Light signalling
106(1)
6.6.4 Developmental stage and tissue specificity
106(1)
6.6.5 Environmental stress and carbohydrate depletion
107(1)
6.6.6 Senescence and nitrogen remobilization
108(1)
6.6.7 Seed maturation
108(1)
6.6.8 Photorespiration
109(1)
6.6.9 Nitrogen signalling and glutamine: asparagine ratio
109(1)
6.6.10 Asparagine: a nitrogen carrier, storage compound, detoxification mechanism and signal
110(1)
6.7 Phylogeny, Subunit Structure and Enzymatic Activity of Asparagine Synthetase
110(2)
6.7.1 Phylogeny
110(2)
6.7.2 Subunit structure
112(1)
6.7.3 The enzymatic activities of asparagine synthesis
112(1)
6.8 Kinetics, Reaction Mechanism and Crystal Structure of B-type Asparagine Synthetases
112(4)
6.8.1 Kinetics of plant asparagine synthetase
112(2)
6.8.2 The crystal structure and reaction mechanism of asparagine synthetase
114(2)
6.9 Other Routes of Asparagine Synthesis in Plants
116(1)
6.10 Asparagine Catabolism
116(1)
6.11 Asparagine Synthetase and Agriculture
117(3)
6.11.1 Seed protein content and crop yield
117(1)
6.11.2 The impact of plant nutrition
118(1)
6.11.3 Metabolic engineering and transgenic studies
118(2)
6.12 Conclusions
120(9)
Acknowledgements
120(1)
References
120(9)
7 Glutamate Decarboxylase
129(13)
J.J. Molina-Rueda
A. Garrido-Aranda
F. Gallardo
7.1 Abstract
129(1)
7.2 Introduction
129(1)
7.3 Characteristics of Glutamate Decarboxylase in Plants
130(1)
7.4 Glutamate Decarboxylase Gene Family
131(1)
7.5 Expression of Glutamate Decarboxylase Genes
131(4)
7.6 γ-Aminobutyric Acid Synthesis and its Metabolic Context
135(2)
7.6.1 The γ-aminobutyric acid shunt pathway and stress
135(2)
7.6.2 Alternative sources of γ-aminobutyric acid in plant tissues and transport
137(1)
7.7 Classical and Recent Evidence Supporting the Functions of Glutamate Decarboxylase and γ-Aminobutyric Acid
137(2)
7.8 Future Research
139(3)
Acknowledgement
139(1)
References
139(3)
8 L-Arginine-Dependent Nitric Oxide Synthase Activity
142(14)
F.J. Corpas
L.A. del Rio
J.M. Palma
J.B. Barroso
8.1 Abstract
142(1)
8.2 Introduction
142(1)
8.3 Arginine Catabolism in Plants: Urea, Polyamines and Nitric Oxide
143(4)
8.3.1 Urea metabolism
144(1)
8.3.2 L-Arginine modulates polyamine and nitric oxide biosynthesis
144(1)
8.3.3 Arginine and nitric oxide synthesis in higher plants
145(2)
8.4 Modulation of L-Arginine-Dependent Nitric Oxide Synthase Activity During Plant Development and Under Stress Conditions
147(3)
8.4.1 Nitric oxide synthase activity during plant development
147(2)
8.4.2 Nitric oxide synthase activity in plants under stress conditions
149(1)
8.5 A Genetic Engineering Approach to Study of the Relevance of Nitric Oxide Synthase Activity in Plants
150(1)
8.6 Conclusions
150(6)
Acknowledgements
151(1)
References
151(5)
9 Ornithine: At the Crossroads of Multiple Paths to Amino Acids and Polyamines
156(21)
R. Majumdar
R. Minocha
S.C. Minocha
9.1 Abstract
156(1)
9.2 Introduction
156(2)
9.3 Ornithine Biosynthesis and Utilization
158(1)
9.4 Cellular Contents
159(1)
9.5 Mutants of Ornithine Biosynthesis
160(4)
9.6 Genetic Manipulation of Ornithine Metabolism and its Impact on Amino Acids and Other Related Compounds
164(4)
9.7 Ornithine Biosynthesis and Functions in Animals
168(1)
9.8 Exogenous Supply of D- and L-Ornithine
169(1)
9.9 Modelling of Ornithine Metabolism and Associated Flux: Ornithine as a Regulatory Molecule
170(1)
9.10 Conclusions
171(6)
Acknowledgements
172(1)
References
172(5)
10 Polyamines in Plants: Biosynthesis From Arginine, and Metabolic, Physiological and Stress-Response Roles
177(18)
A.K. Mattoo
T. Fatima
R.K. Upadhyay
A.K. Handa
10.1 Abstract
177(1)
10.2 Introduction
177(1)
10.3 Substrates and Enzymes Catalysing Polyamine Biosynthesis
178(4)
10.3.1 The route to the diamine putrescine
178(2)
10.3.2 The route to higher polyamines, spermidine and spermine/thermospermine
180(1)
10.3.3 S-Adenosylmethionine decarboxylase
180(1)
10.3.4 Spermidine synthase
181(1)
10.3.5 Spermine/thermospermine synthases
181(1)
10.4 Substrate Flux into the Polyamine Versus Ethylene Pathway
182(1)
10.5 Back Conversion of Polyamines and Reactive Oxygen Species Signalling
183(1)
10.6 Polyamines have an Impact on Metabolism
184(1)
10.7 Polyamines and Plant Growth Processes
185(1)
10.8 Polyamines in Plant Responses to Abiotic Stress
186(1)
10.9 Conclusions
186(9)
References
188(7)
11 Serine Acetyltransferase
195(24)
M. Watanabe
H-M. Hubberten
K. Saito
R. Hoefgen
11.1 Abstract
195(1)
11.2 Introduction
195(2)
11.3 Biochemical Properties and Sub-cellular Localization of Serine Acetyltransferases
197(2)
11.4 The Serine Acetyltransferase-0-Acetylserine(Thiol)Lyase Complex
199(3)
11.5 Expression Patterns of Serine Acetyltransferase Genes
202(2)
11.6 In Vivo Functions of Serine Acetyltransferases
204(2)
11.7 Serine Acetyltransferase Overexpressors
206(1)
11.8 O-Acetylserine Signalling
207(4)
11.8.1 Identification of O-acetylserine cluster genes
207(2)
11.8.2 Regulation of O-acetylserine cluster genes
209(1)
11.8.3 Functions of O-acetylserine cluster genes
210(1)
11.9 Conclusions
211(8)
References
212(7)
12 Cysteine Homeostasis
219(15)
I. Garcia
L.C. Romero
C. Gotor
12.1 Abstract
219(1)
12.2 Introduction
219(1)
12.3 Photosynthetic Assimilation of Sulfate in Plants
220(2)
12.3.1 Sulfate transport
220(1)
12.3.2 Sulfate reduction
221(1)
12.3.3 Cysteine biosynthesis
222(1)
12.4 The Cysteine Synthase Complex: Regulation of Cysteine Biosynthesis
222(2)
12.5 Cysteine Synthesis in Cellular Compartments
224(1)
12.6 Other Members of the 0-Acetylserine(Thiol)Lyase Gene Family
224(5)
12.6.1 CS26
225(1)
12.6.2 CYS-C1
226(1)
12.6.3 DES1
227(2)
12.7 Conclusions
229(5)
Acknowledgements
229(1)
References
229(5)
13 Lysine Metabolism
234(17)
L.O. Medici
A.C. Nazareno
S.A. Gaziola
D. Schmidt
R.A. Azevedo
13.1 Abstract
234(1)
13.2 Introduction
234(2)
13.3 Aspartate Kinase and Homoserine Dehydrogenase
236(1)
13.4 Aspartate Semialdehyde Dehydrogenase
237(1)
13.5 Homoserine Kinase
237(1)
13.6 Dihydrodipicolinate Synthase
238(2)
13.7 Lysine Catabolism
240(3)
13.8 What Next?
243(2)
13.9 Conclusions
245(6)
References
245(6)
14 Histidine
251(11)
R.A. Ingle
14.1 Abstract
251(1)
14.2 Introduction
251(1)
14.3 Histidine Biosynthesis in Plants
252(4)
14.4 Links Between Histidine Biosynthesis and Other Metabolic Pathways in Plants
256(1)
14.5 Sub-Cellular Localization and Evolution of Plant Histidine Biosynthetic Enzymes
256(1)
14.6 Regulation of Histidine Biosynthesis in Plants
256(2)
14.7 Role of Histidine in Nickel Hyperaccumulation in Plants
258(1)
14.8 Conclusions
258(4)
References
258(4)
15 Amino Acid Synthesis Under Abiotic Stress
262(15)
E. Planchet
A.M. Limami
15.1 Abstract
262(1)
15.2 Introduction
262(2)
15.3 The Glutamate Family Pathway
264(3)
15.3.1 Proline accumulation and adaptive responses to stress
264(2)
15.3.2 The regulation of proline metabolism during stress
266(1)
15.3.3 Accumulation of γ-aminobutyric acid (GABA) in response to plant stresses
267(1)
15.4 The Pyruvate Family Pathway
267(3)
15.4.1 Alanine accumulation: a universal phenomenon under stress
268(2)
15.4.2 Leucine and valine: the importance of branched-chain amino acid accumulation in response to stress
270(1)
15.5 The Aspartate Family Pathway
270(2)
15.5.1 Stress-induced asparagine accumulation
271(1)
15.5.2 Aspartate-derived amino acids in response to stress
272(1)
15.6 Conclusions
272(5)
References
273(4)
16 The Central Role of Glutamate and Aspartate in the Post-translational Control of Respiration and Nitrogen Assimilation in Plant Cells
277(21)
B. O'Leary
W.C. Plaxton
16.1 Abstract
277(1)
16.2 Introduction: The Metabolic Organization of N Assimilation
277(5)
16.2.1 The pivotal role of phospoenolpyruvate metabolism in the control of plant glycolysis and respiration
280(2)
16.3 Metabolic Effects of N Resupply in Unicellular Green Algae and Vascular Plants
282(2)
16.3.1 The response of primary C metabolism to N resupply in N-starved green microalgae
282(1)
16.3.2 The response of primary C metabolism to N resupply in vascular plants
283(1)
16.4 The Post-translational Control of Plant Phosphoenolpyruvate Carboxylase and Cytosolic Pyruvate Kinase is Often Geared to NH+4 Assimilation
284(6)
16.4.1 The functional diversity of plant phosphoenolpyruvate carboxylase isoenzymes reflects their complex mechanisms of post-translational control
284(4)
16.4.2 The allosteric features of plant cytosolic pyruvate kinase isoenzymes help to synchronize C/N interactions in different tissues
288(1)
16.4.3 Glutamate and aspartate play a central role in the coordinate allosteric control of phosphoenolpyruvate carboxylase and cytosolic pyruvate kinase during NH+4 assimilation
289(1)
16.5 Transgenic Plants with Altered Phospoenolpyruvate or Glutamate Metabolism Display an Altered C/N Balance
290(2)
16.5.1 Mutants with phosphoenolpyruvate metabolism perturbed by cytosolic pyruvate kinase or phosphoenolpyruvate carboxylase
290(1)
16.5.2 Effect of mutations that perturb glutamate levels
291(1)
16.6 Conclusions and Future Directions
292(6)
Acknowledgements
292(1)
References
293(5)
PART II DYNAMICS
17 Amino Acid Export in Plants
298(17)
M.B. Price
S. Okumoto
17.1 Abstract
298(1)
17.2 Introduction
298(1)
17.3 Physiology of Amino Acid Export
299(3)
17.3.1 Amino acid export from the seed coat
300(1)
17.3.2 Amino acid export into the xylem
300(1)
17.3.3 Amino acid exchange with the rhizosphere
301(1)
17.3.4 Vascular amino acid transport
302(1)
17.4 Amino Acid Export Proteins in Plants and Other Systems
302(3)
17.4.1 The drug/metabolite transporter (DMT) superfamily
302(1)
17.4.2 The amino acid-polyamine-organocation (APC) superfamily
303(1)
17.4.3 The ATP-binding cassette (ABC) transporter superfamily
304(1)
17.4.4 The major facilitator superfamily (MFS)
305(1)
17.5 Regulation of Amino Acid Export
305(1)
17.6 Amino Acids in Inter-Organism Interactions
306(1)
17.6.1 Amino acid secretion into the rhizosphere
306(1)
17.6.2 Amino acid transport during nodulation
306(1)
17.6.3 Amino acids in plant--pathogen interactions
307(1)
17.7 Conclusions
307(8)
References
307(8)
18 Uptake, Transport and Redistribution of Amino Nitrogen in Woody Plants
315(25)
S. Pfautsch
T.L. Bell
A. Gessler
18.1 Abstract
315(1)
18.2 Introduction
315(2)
18.3 Uptake of Amino-N by Plant Roots
317(8)
18.3.1 Principles of N uptake
317(2)
18.3.2 Capacity and importance of uptake of amino-N
319(2)
18.3.3 Uptake involving mycorrhizal associations
321(2)
18.3.4 `Uptake' involving an N2-fixing association
323(1)
18.3.5 `Double-dipping' or how root hemiparasites access amino-N
324(1)
18.4 Transporting Amino-N in the Xylem
325(3)
18.4.1 Transpiration -- the upward `conveyor belt' for amino-N
325(1)
18.4.2 Loading amino-N into the xylem
326(1)
18.4.3 Amino-N composition of xylem sap
326(2)
18.5 Exchange of Amino Acids Between Xylem and Phloem and Integration of N Transport and Plant N Metabolism
328(1)
18.6 Future Research Directions
329(1)
18.7 Conclusions
330(10)
References
331(9)
PART III CHEMICAL ECOLOGY
19 Auxin Biosynthesis
340(22)
J. W. Chandler
19.1 Abstract
340(1)
19.2 Introduction
341(1)
19.3 Sites of Auxin Synthesis in Plants and Cells
342(1)
19.4 Pathways of Auxin Synthesis
342(6)
19.4.1 The indole-3-pyruvate (IPA) pathway
343(2)
19.4.2 Alternative biosynthetic routes
345(1)
19.4.3 The indole-3-acetaldoxime (IAOx) pathway
346(1)
19.4.4 The indole-3-acetamide (IAM) pathway
346(1)
19.4.5 The tryptamine (TAM) pathway
347(1)
19.5 Endogenous Auxins
348(1)
19.6 Auxin Synthesis via the IPA Pathway is Transcriptionally and Spatio-temporally Regulated
349(1)
19.7 Environmental Regulation of Auxin Synthesis
350(1)
19.8 Hormonal Regulation of Auxin Biosynthesis
351(1)
19.9 Conjugation Contributes to Auxin Homeostasis
352(1)
19.10 The Evolution of Auxin Synthesis in Plants
352(2)
19.11 Conclusions
354(8)
Acknowledgement
354(1)
References
354(8)
20 Involvement of Tryptophan-Pathway-Derived Secondary Metabolism in the Defence Responses of Grasses
362(28)
A. Ishihara
T. Matsukawa
I. Nomura
M. Sue
A. Oikawa
Y. Okazaki
S. Tebayashi
20.1 Abstract
362(1)
20.2 General Introduction to Secondary Metabolism Derived From the Tryptophan Pathway
362(2)
20.3 The Biosynthesis and Functions of Benzoxazinones in Wheat, Rye and Maize
364
20.3.1 Molecular genetics of the benzoxazinone pathway
364(4)
20.3.2 Detoxification and reactivation of benzoxazinones
368(3)
20.3.3 Inducible defence response associated with benzoxazinones
371(1)
20.4 Significance of the Metabolic Processes of Avenanthramides in the Defence Response of Oats
372(1)
20.4.1 Biosynthesis of avenanthramide phytoalexins in oats
372(2)
20.4.2 Metabolism of avenanthramides in elicitor-treated oat leaves
374(1)
20.5 Accumulation of Serotonin in Rice in Response to Biological Stimuli
375(5)
20.5.1 Occurrence of serotonin and its putative ecological roles in plants
375(2)
20.5.2 Critical role of serotonin accumulation in the interaction between rice and its pathogens
377(3)
20.6 Concluding Remarks
380(10)
References
381(9)
21 Melatonin: Synthesis From Tryptophan and its Role in Higher Plants
390(46)
M. B. Arnao
J. Hernandez-Ruiz
21.1 Abstract
390(1)
21.2 Introduction
390(6)
21.2.1 Discovery of melatonin
391(1)
21.2.2 Physiological roles of melatonin
391(4)
21.2.3 1995: a critical year for plants
395(1)
21.3 Biosynthesis of Melatonin
396(11)
21.3.1 Melatonin-related enzymes and their regulation
396(1)
21.3.1.1 Tryptophan 5-hydroxylase (T 5 H)
396(5)
21.3.1.2 Tryptophan decarboxylase (TDC)
401(1)
21.3.1.3 Serotonin N-acetyltransferase (SNAT)
402(1)
21.3.1.4 Hydroxyindole O-methyltransferase (HIOMT)
403(1)
21.3.2 Characteristic features of melatonin-related enzymes in plants
404(1)
21.3.2.1 Tryptophan 5-hydroxylase (T5H)
404(1)
21.3.2.2 Tryptophan decarboxylase (TDC)
405(1)
21.3.2.3 Serotonin N-acetyltransferase (SNAT)
406(1)
21.3.2.4 Hydroxyindole O-methyltransferase (HIOMT)
407(1)
21.4 Catabolism of Melatonin: Enzymatic and Non-enzymatic Pathways
407(2)
21.5 Physiological Actions of Melatonin in Plants
409(6)
21.5.1 Searching for roles of melatonin in plants similar to those observed in animals
410(3)
21.5.2 Searching for specific roles of melatonin in plants
413(2)
21.6 Future Perspectives and Concluding Remarks
415(21)
References
416(20)
22 Glucosinolate Biosynthesis From Amino Acids
436(12)
H.U. Stotz
ED. Brown
J. Tokuhisa
22.1 Abstract
436(1)
22.2 Introduction: Evolution of Glucosinolate Biosynthesis
436(2)
22.3 Cellular and Tissue Distribution of Glucosinolate Metabolism
438(2)
22.4 Connections of Glucosinolate Metabolism to Amino Acid Biosynthesis
440(1)
22.5 Regulation of Glucosinolate Biosynthesis
441(1)
22.6 Biological Activities of Glucosinolate Metabolites
441(2)
22.7 Conclusions
443(5)
References
444(4)
23 Natural Toxins that Affect Plant Amino Acid Metabolism
448(13)
S.O. Duke
F.E. Dayan
23.1 Abstract
448(1)
23.2 Introduction
448(1)
23.3 Approaches to the Discovery of Phytotoxin Mode of Action
449(1)
23.4 Inhibitors of Aminotransferases
449(1)
23.5 An Inhibitor of β-Cystathionase (Cystathionine β-lyase)
450(1)
23.6 Inhibitors of Glutamate Synthase and Asparagine Synthetase
450(1)
23.7 Inhibitors of Glutamine Synthetase
451(2)
23.8 Inhibitors of Ornithine Transcarbamoylase
453(1)
23.9 Inhibitor of Dihydrodipicolinate Synthase
453(1)
23.10 Potential Inhibitors of Amino Acid Metabolism
454(1)
23.11 Ascaulitoxin Aglycone -- A Potential Aminotransferase Inhibitor
454(1)
23.12 Enhanced Photodegradation of L-Phenylalanine
454(1)
23.13 Final Thoughts
454(7)
References
456(5)
24 Glyphosate: The Fate and Toxicology of a Herbicidal Amino Acid Derivative
461(20)
D.A. Saltmiras
D.R. Farmer
A. Mehrsheikh
M.S. Bleeke
24.1 Abstract
461(1)
24.2 Introduction
461(1)
24.3 History of Glyphosate
462(1)
24.4 Herbicidal Mode of Action of Glyphosate
462(1)
24.5 Physico-Chemical Properties of Glyphosate
462(1)
24.6 Glyphosate in the Environment
463(6)
24.6.1 Uptake and metabolism in plants
463(3)
24.6.2 Environmental fate
466(3)
24.7 Glyphosate in Mammals
469(7)
24.7.1 Mammalian absorption, distribution, metabolism and excretion (ADME) studies
470(1)
24.7.2 Toxicology
470(1)
24.7.2.1 Acute toxicity
471(1)
24.7.2.2 Repeat dose toxicity
471(1)
24.7.2.3 Genotoxicity
472(1)
24.7.2.4 Carcinogenicity
472(1)
24.7.2.5 Developmental and reproductive toxicity
473(1)
24.7.2.6 Endocrine disruption
474(1)
24.7.2.7 Neurotoxicity
474(1)
24.7.3 Human dietary exposures to glyphosate
474(1)
24.7.4 Human health risk assessments
475(1)
24.8 Conclusions
476(5)
References
476(5)
PART IV PLANT PRODUCTS: QUALITY AND SAFETY
25 Amino Acid Analysis of Plant Products
481(16)
S.M. Rutherfurd
25.1 Abstract
481(1)
25.2 Introduction
481(1)
25.3 Sample Preparation
482(1)
25.4 Amino Acid Analysis
482(6)
25.4.1 The hydrolysis step
482(2)
25.4.2 Least-squares non-linear regression
484(2)
25.4.3 The chromatography step
486(1)
25.4.4 Mass spectrometry and nuclear magnetic resonance
486(1)
25.4.5 Determination of free amino acids
487(1)
25.4.6 Presentation of amino acid composition data
488(1)
25.4.7 Internal and external standards
488(1)
25.5 Determination of the Amino Acid Composition of Processed Plant Products
488(4)
25.5.1 Lysine
489(1)
25.5.2 Methionine and cysteine
490(1)
25.5.3 Threonine and serine
491(1)
25.5.4 Amino acid racemization
491(1)
25.6 Conclusions
492(5)
References
492(5)
26 Metabolic Amino Acid Availability in Foods of Plant Origin: Implications for Human and Livestock Nutrition
497(10)
C.L. Levesque
26.1 Abstract
497(1)
26.2 Introduction
497(1)
26.3 Amino Acid Digestibility and its Limitations
498(1)
26.4 Metabolic Availability of Amino Acids
499(4)
26.4.1 Metabolic availability in protein sources
501(1)
26.4.2 Advantages of the metabolic availability method
502(1)
26.5 Future Research and Conclusions
503(4)
References
503(4)
27 Toxicology of Non-Protein Amino Acids
507(31)
J.P.F. D'Mello
27.1 Abstract
507(1)
27.2 Introduction
508(1)
27.3 Classification
509(2)
27.4 Distribution
511(1)
27.5 Metabolic Fate
512(2)
27.5.1 Canavanine
512(1)
27.5.2 Analogues of sulfur amino acids
513(1)
27.5.3 Mimosine
513(1)
27.6 Adverse Effects
514(8)
27.6.1 Anti-microbial activity
515(1)
27.6.2 Phytotoxicity
515(2)
27.6.3 Insecticidal activity
517(1)
27.6.4 Manifestations in higher animals
518(2)
27.6.5 Human health risks
520(2)
27.7 Mechanisms
522(5)
27.7.1 Biochemical basis of toxicity
522(3)
27.7.2 Stress-resistance mechanisms
525(2)
27.8 Detoxification
527(1)
27.9 Potential Applications
528(1)
27.10 Conclusions
529(9)
References
531(7)
PART V CONCLUSIONS
28 Delivering Innovative Solutions and Paradigms for a Changing Environment
538(47)
J.P.F. D'Mello
28.1 Abstract
538(1)
28.2 Background
539(1)
28.3 Approach
540(1)
28.4 Glutamate
541(1)
28.5 Proline
541(1)
28.6 Arginine
542(1)
28.7 Ornithine
542(1)
28.8 Citrulline
542(1)
28.9 Glycine
543(1)
28.10 Sulfur Amino Acids
544(1)
28.11 Branched-Chain Amino Acids
545(2)
28.12 Aromatic Amino Acids
547(2)
28.13 Secondary Metabolism
549(1)
28.14 Comparative Metabolism
550(3)
28.15 Signal Transduction
553(1)
28.16 Molecular Interactions
554(5)
28.16.1 Synergistic effects
556(1)
28.16.2 Antagonisms
556(2)
28.16.3 Integration
558(1)
28.17 Biotic and Environmental Stress Responses
559(6)
28.17.1 A general model
563(1)
28.17.2 Specific examples
564(1)
28.18 Plant Products
565(1)
28.19 Summary
566(6)
28.19.1 Enlightenment and debate in equal measure
566(3)
28.19.2 Amino acids of `particular distinction'
569(1)
28.19.3 Innovation
570(2)
28.20 Outlook
572(13)
References
573(12)
Index 585
J.P.F. D'Mello is a double graduate of the University of Nottingham, obtaining a BSc Honours in 1964 and a PhD in 1967, both in the Department of Applied Biochemistry. He began work at the Edinburgh School of Agriculture in 1968, lecturing to students and commencing research with grants from the Agricultural Research Council, Tropical Products Institute (ODA), BP and ICI. He has supervised a number of Honours, MSc and PhD students during his years at Edinburgh, published extensively in refereed journals, and took charge of the Environmental Protection and Management degree course for four years until retirement. Since retiring, he has edited 5 books for CABI, with A Handbook of Environmental Toxicology: Human Disorders and Ecotoxicology published in December 2019 and the authored text Introduction to Environmental Toxicology publishing in late 2020.
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