Keywords:
Amino acids.
;
Plants -- Metabolism.
;
Electronic books.
Description / Table of Contents:
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. This book collates chapters on plant enzymes and metabolism, modulation, molecular aspects, secondary products, ecology, the environment and mammalian nutrition and toxicology.
Type of Medium:
Online Resource
Pages:
1 online resource (632 pages)
Edition:
1st ed.
ISBN:
9781780642642
URL:
https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=2031814
DDC:
572/.65
Language:
English
Note:
Intro -- Amino Acids in Higher Plants -- Copyright -- Contents -- Contributors -- Preface -- Overview -- Part I: Enzymes and Metabolism -- Part II: Dynamics -- Part III: Chemical Ecology -- Part IV: Plant Products: Quality and Safety -- Part V: Conclusions -- Acknowledgements -- Disclaimer -- References -- Glossary -- Introduction -- Definition of Terms and Acronyms -- References -- 1: Glutamate Dehydrogenase -- 1.1: Abstract -- 1.2: Introduction -- 1.3: Glutamate Dehydrogenase Structure and Localization -- 1.4: Control Plants and Control Glutamate Dehydrogenase -- 1.5: Availability of Ammonium Ions -- 1.5.1: Ammonium ion contents of experimental tissues and plants -- 1.5.2: Glutamate deaminationin mitochondria -- 1.6: Glutamate Dehydrogenase-Linked Schiff Base Amination Complex -- 1.6.1: Pesticide treatment and ammonium ion fertilization -- 1.6.2 Pesticide treatment, ammonium ion fertilization and protein contents -- 1.7: Protect the Glutamine Synthetase-Glutamate Synthase Cycle in Glutamate Dehydrogenase Research -- 1.8: Molecular Biology of Glutamate Dehydrogenase -- 1.8.1: The supply of α-ketoglutarate from the citric acid cycle to glutamatede hydrogenase and glutamate synthase -- 1.8.2: Aminating and deaminating activities -- 1.8.3: Amination-based crop yield doubling biotechnology -- 1.8.4: The aminating cassette of glutamate dehydrogenase isoenzymes -- 1.9: Food Security -- 1.10: Conclusions -- Acknowledgements -- References -- 2: Alanine Aminotransferase: Amino Acid Metabolism in Higher Plants -- 2.1: Abstract -- 2.2: Introduction -- 2.3: Structure and Functions of Alanine -- 2.3.1: Structure of alanine -- 2.3.2: Functions of alanine -- 2.4: Alanine Metabolism -- 2.4.1: Alanine metabolism by alanine aminotransferase -- 2.5: Specific Cellular and Sub-cellular Functions of Alanine Aminotransferase.
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2.5.1: Homologues and tissue localization -- 2.5.2: Sub-cellular localization -- 2.6: A Phylogenetic Analysis of Alanine Aminotransferase -- 2.7: Purification of Alanine Aminotransferase -- 2.8: Protein Characterization of Alanine Aminotransferase -- 2.8.1: Subunits and substrate specificities -- 2.8.2: Kinetics and reaction mechanism -- 2.8.3: Inhibitors of the enzyme -- 2.8.4: Crystal structure -- 2.9: Diverse Roles of Alanine Aminotransferase in Plants -- 2.9.1: Roles in metabolism -- 2.9.1.1: Roles in carbon metabolism -- 2.9.1.2: Roles in photorespira -- 2.9.1.3: Role in nitrogen use efficiency -- 2.9.2: Role in stress biology -- 2.9.2.1: Roles in hypoxia -- 2.9.2.2: Other abiotic and biotic stresses -- 2.10: Conclusions -- References -- 3: Aspartate Aminotransferase -- 3.1: Abstra -- 3.2: Introduction -- 3.3: The Vitamin B6 Cofactor -- 3.4: Enzyme Function -- 3.4.1: The reaction mechanism -- 3.4.2: Enzyme properties -- 3.5: Enzyme Structure -- 3.5.1: K258 -- 3.5.2: R292* -- 3.5.3: R386 -- 3.5.4: D222 -- 3.5.5: Y225 -- 3.6: Enzyme Genetics -- 3.7: The Enzyme during Plant Development -- 3.8: The Role of Aspartate in Plants -- 3.8.1: C4 metabolism -- 3.9: Other Roles of Aspartate Aminotransferase -- 3.9.1: Moonlighting -- 3.9.2: Genetic engineering with aspartate aminotransferases -- 3.10: Future Research -- 3.11: Conclusions -- References -- 4: Tyrosine Aminotransferase -- 4.1: Abstract -- 4.2: Introduction -- 4.2.1: Aminotransferases: a brief introduction -- 4.2.2: A brief history of aminotransferase activity in plants -- 4.2.3: Oligomeric state, cofactor requirement and mechanism of action of aminotransferases -- 4.3: Aminotransferases from the Model Organism Arabidopsis thaliana -- 4.4: The Anabolism of Tyrosine and Phenylalanine in Plants and Bacteria -- 4.4.1: The anabolism of tyrosine and phenylalanine in bacteria.
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4.4.2: A second pathway for the synthesis of tyrosine and phenylalanine in plants -- 4.5: Properties of Tyrosine Aminotransferase Annotated by the Locus Tag At5g36160 from Arabidopsis thaliana -- 4.5.1: Kinetic and physical properties -- 4.5.2: Substrate specificity -- 4.5.3: In vivo analysis of tyrosine aminotransferase -- 4.6: The Role of Tyrosine Aminotransferase in Plants -- 4.7: Conclusions -- Acknowledgement -- References -- 5: An Insight into the Role and Regulation of Glutamine Synthetase in Plants -- 5.1: Abstract -- 5.2: Introduction -- 5.3: Classification of Glutamine Synthetase -- 5.4: Glutamine Synthetase in Plants -- 5.4.1: Chloroplastic glutamine synthetase -- 5.4.2: Cytosolic glutamine synthetase -- 5.5: Modulation of Glutamine Synthetase Expression inTransgenic Plants -- 5.6: Regulation of Glutamine Synthetase Gene Expression in Plants -- 5.6.1: Transcriptional regulation -- 5.6.2: Post-transcriptional regulation -- 5.6.3: Translational regulation -- 5.6.4: Post-translational regulation -- 5.7: Concluding Remarks -- Acknowledgements -- References -- 6: Asparagine Synthetase -- 6.1: Abstract -- 6.2: Introduction: the Role of Asparagine and Asparagine Synthetasein Nitrogen Metabolism -- 6.3: Asparagine: History, Chemical Properties and Role in Plants -- 6.4: Asparagine Synthetase: an Early History of Research in Humans, Microbes and Plants -- 6.5: The Occurrence of Asparagine Synthetase in Nature -- 6.6: The Expression and Function of Asparagine Synthetase in Plants -- 6.6.1: Nutritional and mineral deficiency -- 6.6.2: Seed germination -- 6.6.3: Light signalling -- 6.6.4: Developmental stage and tissue specificity -- 6.6.5: Environmental stress and carbohydrate depletion -- 6.6.6: Senescence and nitrogen remobilization -- 6.6.7: Seed maturation -- 6.6.8: Photorespiration.
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6.6.9: Nitrogen signalling and the glutamine:asparagine ratio -- 6.6.10: Asparagine: a nitrogen carrier, storage compound, detoxification mechanism and signal -- 6.7: Phylogeny, Subunit Structure and Enzymatic Activity of Asparagine Synthetase -- 6.7.1: Phylogeny -- 6.7.2: Subunit structure -- 6.7.3: The enzymatic activities of asparagine synthesis -- 6.8: Kinetics, Reaction Mechanism and Crystal Structure of B-type Asparagine Synthetases -- 6.8.1: Kinetics of plant asparagine synthetase -- 6.8.2: The crystal structure and reaction mechanism of asparagine synthetase -- 6.9: Other Routes of Asparagine Synthesis in Plants -- 6.10: Asparagine Catabolism -- 6.11: Asparagine Synthetase and Agriculture -- 6.11.1: Seed protein contentand crop yield -- 6.11.2: The impact of plant nutrition -- 6.11.3: Metabolic engineering and transgenic studies -- 6.12: Conclusions -- Acknowledgements -- References -- 7: Glutamate Decarboxylase -- 7.1: Abstract -- 7.2: Introduction -- 7.3: Characteristics of Glutamate Decarboxylase in Plants -- 7.4: Glutamate Decarboxylase Gene Family -- 7.5: Expression of GlutamateDecarboxylase Genes -- 7.6: γ-Aminobutyric Acid Synthesis and its Metabolic Context -- 7.6.1 The γ-aminobutyric acid shunt pathway and stress -- 7.6.2 Alternative sources of γ-aminobutyric acid in plant tissues and transport -- 7.7: Classical and Recent Evidence Supporting the Functions of Glutamate Decarboxylase and γ-Aminobutyric Acid -- 7.8: Future Research -- Acknowledgement -- References -- 8: L-Arginine-Dependent Nitric Oxide Synthase Activity -- 8.1: Abstract -- 8.2: Introduction -- 8.3: Arginine Catabolism in Plants: Urea, Polyamines and Nitric Oxide -- 8.3.1: Urea metabolism -- 8.3.2: L-Arginine modulates polyamine and nitric oxide biosynthesis -- 8.3.3: Arginine and nitric oxide synthesis in higher plants.
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8.4: Modulation of L-Arginine-Dependent Nitric Oxide Synthase Activity During Plant Development and Under Stress Conditions -- 8.4.1: Nitric oxide synthase activity during plant development -- 8.4.2: Nitric oxide synthase activity inplants under stress condition -- 8.5: A Genetic Engineering Approach to Study of the Relevance of Nitric Oxide Synthase Activity in Plants -- 8.6: Conclusions -- Acknowledgements -- References -- 9: Ornithine: At the Crossroads of Multiple Paths to Amino Acids and Polyamines -- 9.1: Abstract -- 9.2: Introduction -- 9.3: Ornithine Biosynthesis and Utilization -- 9.4: Cellular Contents -- 9.5: Mutants of Ornithine Biosynthesis -- 9.6: Genetic Manipulation of Ornithine Metabolism and its Impact on Amino Acids and Other Related Compounds -- 9.7: Ornithine Biosynthesis and Functions in Animals -- 9.8: Exogenous Supply of D- and L-Ornithine -- 9.9: Modelling of Ornithine Metabolism and Associated Flux: Ornithine as a Regulatory Molecule -- 9.10: Conclusions -- Acknowledgements -- References -- 10: Polyamines in Plants: Biosynthesis From Arginine, and Metabolic, Physiologicaland Stress-Response Roles -- 10.1: Abstract -- 10.2: Introduction -- 10.3: Substrates and Enzymes Catalysing Polyamine Biosynthes -- 10.3.1: The route to the diamine putrescine -- 10.3.2: The route to higher polyamines, spermidine and spermine/thermospermine -- 10.3.3: S-Adenosylmethionine decarboxylase -- 10.3.4: Spermidine synthase -- 10.3.5: Spermine/thermospermine synthases -- 10.4: Substrate Flux into the Polyamine Versus Ethylene Pathway -- 10.5: Back Conversion of Polyamines and Reactive Oxygen Species Signalling -- 10.6: Polyamines have an Impacton Metabolism -- 10.7: Polyamines and Plant Growth Processes -- 10.8: Polyamines in Plant Responses to Abiotic Stress -- 10.9: Conclusions -- References -- 11: Serine Acetyltransferase -- 11.1: Abstract.
,
11.2: Introduction.
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