Interfacial Enzyme Kinetics,9780471493044

Interfacial Enzyme Kinetics

by ;
Edition: 1st
ISBN13: 9780471493044
ISBN10: 047149304X
Format: Hardcover
Pub. Date: 2002-02-15
Publisher(s): WILEY
List Price: $483.13

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Summary

A vast number of biochemical reactions are catalysed by molecules fixed to the surface of membranes (or other biological structures) with molecules in the surrounding solution. The study of the mechanisms at these "Biointerfaces" are becoming increasingly important for the understanding of biological catalysts, such as enzymes. This project is the first book to deal with the physical and chemical principles of an emerging field of science, for which the authors have set the ground-work. * The first book to deal with this newly emerging area. * Concentrates on the chemical and physical foundation of enzyme catalysis * Key area for the deeper understanding of biocatalytic processes * Examples for proteins and nucleic acids, two central areas of biochemical and bioorganic research

Author Biography

Otto G. Berg and Mahendra Kumar Jain are the authors of Interfacial Enzyme Kinetics, published by Wiley.

Table of Contents

Preface
Theory Boxes
List of Symbols
1 Why Interfacial Enzymes?
Structral Diversity of Nonpolar and Amphiphilic Solutes
To Be or Not to Be in Water
The Hydrophobic Effect
Knotty Issues of Interfacial Enzymology
Pathophysiology of Lipolytic Enzymes
Secreted PLA2 (sPLA2) Prototype for Interfacial Enzymology
Summary and Outlook: Towards the Paradign for Interfacial Enzymology
2 Interface Phenomena: Accessibility and Exchange
Aggregates and Dispersions
Organized Micellar Aggregates in Aqueous Dispersions
Amphiphile Organization and the Monomer - Micelle Equilibrium and Exchange
The Concentration Issues in the Monomer - Aggregate Equilibria
Exchange of Amphiphiles between Organized Interfaces
Dispersed Phases
Choice of Interface for Study of an Interfacial Enzyme
Summary:Interface Determines the Accessibility and Replenishment Rate
3 To Be or Not To Be: Dilemma for the Substrate in Solution
Constrained Reaction Path for the Turnover in the Aqueous Phase
Analysis of the Steady State Turnover Cycle in the Aqueous Phase
Ascertaining the Reaction Path in the Aqueous Phase
PAF-Acetylhydrolase Hydrolyzes the Monodisperse Substrate
Equilibrium Partitioning and Binding to Aggregates
Summary: The Equilibrium Dilemma
4 Interfacial Processivity: Ensemble Behavior in the Scooting Mode
Conceptualizing Interfacial Processivity
The Fourfold Meaning of the Substrate Concentration
Constraints for Defining the Variables for the Reaction Progress in the Scooting Mode
Integrity of Vesicles during the Scooting Mode Reaction Progress
Tests for the Scooting Mode reaction progress by PLA2
Ensemble Behavior of the Binding of the Enzyme to Vesicles
Summary: Ensemble Behavior in a Microscopically Heterogeneous Environment
5 Analysis of the Processive Reaction Progress
Michaelis - Menten Equation for the Turnover in the Interface
Catalytic Parameters from the Integrated Processive Reaction Progress
Additional Constraints for the Analysis of the Interfacial Turnover Events for PLA2
Uses of the Primary Catalytic Parameters
Catalytic Mechanism of PLA2
The Quality-of-Interface Effect
Apparent Interfacial Activation
Hopping and the Fast Enzyme Exchange Limit
Summary: Variations in the Processivity
6 Detailed Balance Conditions for Interfacial Equilibria
Binding of Ions to the Interface
Equilibria for the Binding of the Enzyme to the Interface
Effective Equilibrium Constants
The Cofactor Binding Obligatory for the Substrate Binding
Detailed Balance Conditions and Local Concentrations for Effective Ligand Binding
Resolution of the Interfacial Constants for PLA2
Detailed Balance Conditions for PLA2
Summary: Primary Equilibrium Parameters for the Kinetic Path
7 Rapid Substrate Replenishment in the Quasi-Scooting Mode
Interfacial Catalytic Cycle Turnover in the Quasi-Scooting Mode
Sparingly Soluble Substrates
Reaction Rate with the Partitioned Substrate
Interfacial Turnover by Triglyceride Lipase
Lid on tl-Lipase Active Site
Interfacial Allostery for the Quality-of-Interface effects
Motifs for Close Contact of Proteins with the Interface
Summary: Multiple States of the Enzyme at the Interface
8 Interfacial Allostery
Interfacial Catalytic Turnover in the Quasi-Scooting Mode
The Apparent Rate Parameters for the Pig Pancreatic PLA2
Ks Allosteric effects of the Interface
Analysis of the Interfacila Anionic Charge Preference: kcatS
The Structural Basis for the Anionic Interface preference
Modeling the i-face of PLA2
Site-Directed Mutagenesis to Discern Interactions Along the i-face
Summary: Residues involved in Charge Compensation
9 Inhibition: Specific or Nonspecific
Specific Inhibitors
Kinetic effects of Nonspecific Inhibitors
Kinetic effects of the Interface-Based Competitive Inhibitors
Influence of Cofactor on the Scooting Kinetics
Effects of the Interface-Based Inhibitor on the Integrated Rate Equation in the Scooting Mode
Partitioning of the Inhibitor and Substrate between the Interface and the Aqueous Phase
Summary: Multiple Pathways for Reduction of the Observed Rate
10 The Delay to the Steady State in the Reaction Progress
Effects of the Accumulated products in the Zwitterionic Bilayers
Model for the Delay Due to the Product Accumulation during the Reaction Progress on Phosphatidylcholine Vesicles
Effect of the Accumulated Products on the Delay in the Monolayer Reaction Progress
Summary: Activation by the Anionic Charge Induced by the Product Accumulation
11 Nonidealities of the Dispersed Phases
The Exchange Limit
Exchange-Limited Kinetics of PLA2 in Detergent-Dispersed Mixed Micelles of Long Chain Phospholipids
Effect of Bile Salts on the Pancreatic PLA2 Catalyzed Hydrolosis of Phosphatidylochines
Kinetic Concerns for Interfaces of the Dispersed Phase
The Nonideality Factor
Summary: Nonidealities for Replenishment and Binding
12 Effects of Reduction of Dimensionality
Dissection of the Entropy Loss on Interface Binding
Synergistic effects of the Interface on Enzyme-Substrate Binding, Local Concentration and Scaffolding
Diffusion Times in 1D, 2D and 3D
Rate Enhancement by Facilitated Diffusion in 2D
Summary: Dimensionality effects on the Equilibrium and Diffusion
Reference
Index

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