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Comprehensive Natural Products III : chemistry and biology /

Bibliographic Details
Corporate Author: ScienceDirect (Online service)
Other Authors: Begley, Tadhg P. (Editor), Liu, Hung-wen, 1952- (Editor)
Format: eBook
Language:English
Published: [San Diego, California] : Elsevier, 2020.
Edition:3rd edition.
Subjects:
Natural products.
Electronic books.
Online Access:Connect to the full text of this electronic book
Table of Contents:
  • 1.02.3.1.3. PKS-NRPS and other hybrids
  • 1.02.4. Enzymology and Structural Biology of Modular PKS Domains
  • 1.02.4.1. Acyl Transferases
  • 1.02.4.2. Ketosynthases
  • 1.02.4.2.1. A [beta]-branch forming KS domain
  • 1.02.4.3. Ketoreductases
  • 1.02.4.3.1. [alpha]-Specific ketoreductase domains
  • 1.02.4.4. Dehydratases
  • 1.02.4.4.1. DH variants
  • 1.02.4.5. Enoyl Reductases
  • 1.02.4.5.1. ER catalyzing cyclopropanation
  • 1.02.4.6. C-Methyl Transferases
  • 1.02.4.7. Thioesterases
  • 1.02.4.7.1. VariantTEs
  • 1.02.4.8. Acyl Carrier Proteins
  • 1.02.4.9. Domains Catalyzing Unusual Chemistries
  • 9780081026915_WEB01
  • Comprehensive Natural Products III Chemistry and Biology
  • Copyright
  • Contents of Volume 1
  • Editors-in-Chief
  • Volume Editors
  • List of Contributors for Volume 1
  • Volume Contents
  • Preface
  • 1.01. Overview and Introduction
  • 1.02. Bacterial Type IPolyketide Synthases
  • 1.02.1. Preface
  • 1.02.2. Introduction to the Complex Polyketides
  • 1.02.3. Modular Polyketide Synthases and Relationship to Fatty Acid Synthases
  • 1.02.3.1. Modular PKSs: Variations on aTheme
  • 1.02.3.1.1. Trans-ATPKSs
  • 1.02.3.1.2. Modular PKS modules which iterate
  • 1.02.5. The 3D Architectures of PKS Modules/Subunits
  • 1.02.5.1. Structural Insights Into Intact PKS Modules
  • 1.02.5.2. Modular PKS Structural Biology: FutureGoals
  • 1.02.6. Protein-Protein Interactions in ModularPKSs
  • 1.02.6.1. ACP-Centered Domain-Domain Interactions
  • 1.02.6.2. Interactions Between Modules/Subunits
  • 1.02.6.2.1. Intramolecular intermodular interactions
  • 1.02.6.2.2. Intermolecular intermodular interactions (or docking)
  • 1.02.7. Programming of Modular Polyketide Biosynthesis
  • 1.02.8. Modular PKS Synthetic Biology
  • 1.02.9. Conclusions and Future Perspectives
  • Acknowledgment
  • References
  • 1.03. Structural Biology of Tailoring Domains in Polyketide Synthases
  • 1.03.1. Introduction
  • 1.03.2. The KR Domain
  • 1.03.3. The DH Domain
  • 1.03.4. The ER Domain
  • 1.03.5. The MT Domain
  • 1.03.6. The EI Domain
  • 1.03.7. The PS Domain
  • 1.03.8. The PT Domain
  • 1.03.9. The TE Domain
  • 1.03.10. Conclusion
  • References
  • 1.04. Structural Basis of Acyl-Carrier Protein Interactions in Fatty Acid and Polyketide Biosynthesis
  • 1.04.1. Introduction
  • 1.04.2. Methods to Study ACP Interactions
  • 1.04.2.1. Chemoenzymatic Modification of theACP
  • 1.04.2.2. Molecular Probes and Methods to Study ACP Interactions
  • 1.04.2.2.1. Cysteine-reactive pantetheine crosslinking probes
  • 1.04.2.2.2. Histidine-reactive pantetheine crosslinking probes
  • 1.04.2.2.3. Noncovalent pantetheine probes
  • 1.04.2.2.4. Caged pantetheine crosslinking probes
  • 1.04.2.2.5. Photoaffinity crosslinking probes
  • 1.04.2.3. Molecular Probes and Methods to Study ACP-Substrate Interactions
  • 1.04.2.3.1. Polyketone surrogates
  • 1.04.2.3.2. Solvatochromic probes
  • 1.04.2.3.3. Vibrational spectroscopic probes
  • 1.04.2.4. Structural Methods to Study ACP Interactions