Interfacial enzyme kinetics

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Interfacial enzyme kinetics / Otto G. Berg, Mahendra Kumar Jain

資料種別:

図書

出版情報:

Chichester : John Wiley & Sons, 2002

形態:

xxvi, 301 p. ; 25 cm

著者名:

ISBN:

9780471493044 [047149304X]

書誌ID:

BA5652117X

子書誌情報

フルテキスト

所蔵情報

他の版・巻

書誌詳細

注記:

Includes bibliographical references and index.

主題:

Biological interfaces; Enzyme kinetics

言語:

英語

目次情報:

Preface

Theory Boxes

List of Symbols

Why Interfacial Enzymes? / 1：

Structural Diversity of Nonpolar and Amphiphilic Solutes / 1.1：

To Be or Not to Be in Water / 1.2：

The Hydrophobic Effect / 1.3：

Knotty Issues of Interfacial Enzymology / 1.4：

Pathophysiology of Lipolytic Enzymes / 1.5：

Secreted PLA2 (sPLA2) Prototype for Interfacial Enzymology / 1.6：

Summary and Outlook: Towards the Paradigm for Interfacial Enzymology / 1.7：

Further Reading

Interface Phenomena: Accessibility and Exchange / 2：

Aggregates and Dispersions / 2.1：

Organized Micellar Aggregates in Aqueous Dispersions / 2.2：

Amphiphile Organization and the Monomer-Micelle Equilibrium and Exchange / 2.3：

The Concentration Issues in the Monomer-Aggregate Equilibria / 2.4：

Exchange of Amphiphiles between Organized Interfaces / 2.5：

Dispersed Phases / 2.6：

Choice of Interface for Study of an Interfacial Enzyme / 2.7：

Summary: Interface Determines the Accessibility and Replenishment Rate / 2.8：

To Be or Not To Be: Dilemma for the Substrate in Solution / 3：

Constrained Reaction Path for the Turnover in the Aqueous Phase / 3.1：

Analysis of the Steady State Turnover Cycle in the Aqueous Phase / 3.2：

Ascertaining the Reaction Path in the Aqueous Phase / 3.3：

PAF-Acetylhydrolase Hydrolyzes the Monodisperse Substrate / 3.4：

Equilibrium Partitioning and Binding to Aggregates / 3.5：

Summary: The Equilibrium Dilemma / 3.6：

Interfacial Processivity: Ensemble Behavior in the Scooting Mode / 4：

Conceptualizing Interfacial Processivity / 4.1：

The Fourfold Meaning of the Substrate Concentration / 4.2：

Constraints for Defining the Variables for the Reaction Progress in the Scooting Mode / 4.3：

Integrity of Vesicles during the Scooting Mode Reaction Progress / 4.4：

Tests for the Scooting Mode Reaction Progress by PLA2 / 4.5：

Ensemble Behavior of the Binding of the Enzyme to Vesicles / 4.6：

Summary: Ensemble Behavior in a Microscopically Heterogeneous Environment / 4.7：

Analysis of the Processive Reaction Progress / 5：

Michaelis-Menten Equation for the Turnover in the Interface / 5.1：

Catalytic Parameters from the Integrated Processive Reaction Progress / 5.2：

Additional Constraints for the Analysis of the Interfacial Turnover Events for PLA2 / 5.3：

Uses of the Primary Catalytic Parameters / 5.4：

Catalytic Mechanism of PLA2 / 5.5：

The Quality-of-Interface Effects / 5.6：

Apparent Interfacial Activation / 5.7：

Hopping and the Fast Enzyme Exchange Limit / 5.8：

Summary: Variations in the Processivity / 5.9：

Detailed Balance Conditions for Interfacial Equilibria / 6：

Binding of Ions to the Interface / 6.1：

Equilibria for the Binding of the Enzyme to the Interface / 6.2：

Effective Equilibrium Constants / 6.3：

The Cofactor Binding Obligatory for the Substrate Binding / 6.4：

Detailed Balance Conditions and Local Concentrations for Effective Ligand Binding / 6.5：

Resolution of the Interfacial Constants for PLA2 / 6.6：

Detailed Balance Conditions for PLA2 / 6.7：

Summary: Primary Equilibrium Parameters for the Kinetic Path / 6.8：

Rapid Substrate Replenishment in the Quasi-Scooting Mode / 7：

Interfacial Catalytic Cycle Turnover in the Quasi-Scooting Mode / 7.1：

Sparingly Soluble Substrates / 7.2：

Reaction Rate with the Partitioned Substrate / 7.3：

Interfacial Turnover by Triglyceride Lipase / 7.4：

Lid on tl-Lipase Active Site / 7.5：

Interfacial Allostery for the Quality-of-Interface Effects / 7.6：

Motifs for Close Contact of Proteins with the Interface / 7.7：

Summary: Multiple States of the Enzyme at the Interface / 7.8：

Interfacial Allostery / 8：

Interfacial Catalytic Turnover in the Quasi-Scooting Mode / 8.1：

The Apparent Rate Parameters for the Pig Pancreatic PLA2 / 8.2：

K*[subscript S] Allosteric Effects of the Interface / 8.3：

Analysis of the Interfacial Anionic Charge Preference: k*[subscript catS] Activation / 8.4：

The Structural Basis for the Anionic Interface Preference / 8.5：

Modeling the i-face of PLA2 / 8.6：

Site-Directed Mutagenesis to Discern Interactions Along the i-face / 8.7：

Summary: Residues Involved in Charge Compensation / 8.8：

Inhibition: Specific or Nonspecific / 9：

Specific Inhibitors / 9.1：

Kinetic Effects of Nonspecific Inhibitors / 9.2：

Kinetic Effects of the Interface-Based Competitive Inhibitors / 9.3：

Influence of Cofactor on the Scooting Kinetics / 9.4：

Effects of the Interface-Based Inhibitor on the Integrated Rate Equation in the Scooting Mode / 9.5：

Partitioning of the Inhibitor and Substrate between the Interface and the Aqueous Phase / 9.6：

Summary: Multiple Pathways for Reduction of the Observed Rate / 9.7：

The Delay to the Steady State in the Reaction Progress / 10：

Effects of the Accumulated Products in Zwitterionic Bilayers / 10.1：

Model for the Delay Due to the Product Accumulation during the Reaction Progress on Phosphatidylcholine Vesicles / 10.2：

Effect of the Accumulated Products on the Delay in the Monolayer Reaction Progress / 10.3：

Summary: Activation by the Anionic Charge Induced by the Product Accumulation / 10.4：

Nonidealities of the Dispersed Phases / 11：

The Exchange Limit / 11.1：

Exchange-Limited Kinetics of PLA2 in Detergent-Dispersed Mixed Micelles of Long Chain Phospholipids / 11.2：

Effect of Bile Salts on the Pancreatic PLA2 Catalyzed Hydrolysis of Phosphatidylcholines / 11.3：

Kinetic Concerns for Interfaces of the Dispersed Phase / 11.4：

The Nonideality Factor / 11.5：

Summary: Nonidealities for Replenishment and Binding / 11.6：

Effects of Reduction of Dimensionality / 12：

Dissection of the Entropy Loss on Interface Binding / 12.1：

Synergistic Effects of the Interface on Enzyme-Substrate Binding, Local Concentration and Scaffolding / 12.2：

Diffusion Times in 1D, 2D and 3D / 12.3：

Rate Enhancement by Facilitated Diffusion in 2D / 12.4：

Summary: Dimensionality Effects on the Equilibrium and Diffusion / 12.5：

References

Index

Preface

Theory Boxes

List of Symbols

Why Interfacial Enzymes? / 1：

Structural Diversity of Nonpolar and Amphiphilic Solutes / 1.1：

To Be or Not to Be in Water / 1.2：

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