This comprehensive book on Enzymology seamlessly merges theoretical biochemistry with practical, hands-on applications. Designed for advanced students and researchers, it covers the molecular foundations of biocatalysis, enzyme kinetics, and cutting-edge biotechnological uses, making it an essential resource for mastering modern molecular biology. The book explores the historical discovery of biological catalysts, basic nomenclature, and international classifications, establishing a foundational understanding of how these proteins function in living systems. Details the 3-dimensional architecture of proteins, amino acid residues in the active site, and how structural folding dictates specificity, cofactors, and coenzymes. Focuses on the mathematical models of reaction rates, examining the Michaelis-Menten equation, and linear transformations like the Lineweaver-Burk plot. Unpacks the chemical logic behind accelerating reactions, including transition-state stabilization, acid-base catalysis, covalent catalysis, and the induced-fit model. Discusses how cells maintain homeostasis through feedback inhibition, zymogen activation, allosteric regulation, and reversible covalent modifications. Analyzes reversible (competitive, non-competitive, uncompetitive) and irreversible inhibitors, illustrating their roles in metabolic regulation and pharmaceutical drug design. Explores the commercial exploitation of biocatalysts, covering enzyme immobilization, large-scale production, and applications in food, beverage, and detergent manufacturing. Examines the use of enzymes as biomarkers for diseases (such as liver and cardiac markers), evaluating how clinical assays guide patient diagnosis and treatment.
Karolina W. Christianson the brilliant author is known for her quiet life and her passionate crusade to decode the molecular engines of life. A dedicated scholar, her writing bridges the gap between complex molecular biochemistry and everyday biological functions. Growing up in a modest home where her only escape was a towering bookshelf, Dr. Karolina was fascinated by how small changes create massive impacts. This obsession\ with the invisible world drove her to dedicate her life to studying enzymes, the biological catalysts that make life possible. After earning her PhD at the University of Cambridge, she spent decades unraveling the mysteries of enzyme kinetics. Unlike typical researchers glued entirely to lab benches, Dr. Karolina is known for her unconventional pedagogical approach. She famously teaches complex Michaelis-Menten kinetics by comparing enzyme-substrate reactions to a busy, overcrowded dance floor. She held legendary, informal weekend seminars for students in her cramped, tea-scented campus office. She firmly believes in Louis Pasteur's famous dictum that mastering the core theory of science is the only path to true applied innovation. She painstakingly structured the book to take students with zero background in chemistry and guide them into the highest levels of structural biology. Today, Dr. Karolina continues her work in a private research facility, writing fiction in her spare time and spending weekends hiking the mountains to gain perspective on the world's microscopic intricacies.
| Preface Chapter 1. Introduction to Enzymology Nature and Importance of Enzymes Historical Development of Enzymology Classification of Enzymes Nomenclature and Enzyme Commission (EC) System Chemical Nature of Enzymes Structure–Function Relationship Enzyme Cofactors and Coenzymes Methods of Enzyme Study Chapter 2. Enzyme Structure and Function Primary, Secondary, Tertiary, and Quaternary Structure Active Site Architecture Binding Interactions and Specificity Transition State Theory Protein Folding and Stability Role of Metal Ions Allosteric Sites Substrate Recognition Chapter 3. Enzyme Kinetics Michaelis–Menten Model Steady-State Assumptions Lineweaver–Burk and Other Plots Enzyme Efficiency and Turnover Number Multi-Substrate Reactions Pre-Steady-State Kinetics Kinetic Isotope Effects Factors Affecting Reaction Rates Chapter 4. Enzyme Catalysis Mechanisms General Acid–Base Catalysis Covalent Catalysis Metal Ion Catalysis Proximity and Orientation Effects Catalytic Triads and Dyads Reaction Pathway Analysis Enzyme Dynamics and Conformational Changes Enzyme–Substrate Complexes Chapter 5. Enzyme Regulation and Control Allosteric Regulation Feedback Inhibition Covalent Modification Zymogens and Proenzymes Isoenzymes Hormonal Regulation Metabolic Pathway Control Regulatory Networks |
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$280.00