Far more than a comprehensive treatise on initial-rate and fast-reaction kinetics, this one-of-a-kind desk reference places enzyme science in the fuller context of the organic, inorganic, and physical chemical processes occurring within enzyme active sites. Drawing on 2600 references, Enzyme Kinetics: Catalysis & Control develops all the kinetic tools needed to define enzyme catalysis, spanning the entire spectrum (from the basics of chemical kinetics and practical advice on rate measurement, to the very latest work on single-molecule kinetics and mechanoenzyme force generation), while also focusing on the persuasive power of kinetic isotope effects, the design of high-potency drugs, and the behavior of regulatory enzymes. Historical analysis of kinetic principles including advanced enzyme science Provides both theoretical and practical measurements tools Coverage of single molecular kinetics Examination of force generation mechanisms Discussion of organic and inorganic enzyme reactions

Far more than a comprehensive treatise on initial-rate and fast-reaction kinetics, this one-of-a-kind desk reference places enzyme science in the fuller context of the organic, inorganic, and physical chemical processes occurring within enzyme active sites. Drawing on 2600 references, Enzyme Kinetics: Catalysis & Control develops all the kinetic tools needed to define enzyme catalysis, spanning the entire spectrum (from the basics of chemical kinetics and practical advice on rate measurement, to the very latest work on single-molecule kinetics and mechanoenzyme force generation), while also focusing on the persuasive power of kinetic isotope effects, the design of high-potency drugs, and the behavior of regulatory enzymes. - Historical analysis of kinetic principles including advanced enzyme science - Provides both theoretical and practical measurements tools - Coverage of single molecular kinetics - Examination of force generation mechanisms - Discussion of organic and inorganic enzyme reactions

Fundamentals of Enzyme Kinetics details the rate of reactions catalyzed by different enzymes and the effects of varying the conditions on them. The book includes the basic principles of chemical kinetics, especially the order of a reaction and its rate constraints. The text also gives an introduction to enzyme kinetics - the idea of an enzyme-substrate complex; the Michaelis-Menten equation; the steady state treatment; and the validity of its assumption. Practical considerations, the derivation of steady-state rate equations, inhibitors and activators, and two-substrate reactions are also explained. Problems after the end of each chapter have also been added, as well as their solutions at the end of the book, to test the readers' learning. The text is highly recommended for undergraduate students in biochemistry who wish to study about enzymes or focus completely on enzymology, as most of the mathematics used in this book, which have been explained in detail to remove most barriers of understanding, is elementary.

Current Topics in Cellular Regulation: Volume 24, Enzyme Catalysis and Control is a compendium of papers that discusses phosphoryl transfer reactions, the role of water on the free energy of hydrolysis of pyrophosphate, and the hormonal actions of vitamin D. Other papers describe the regulation lipid metabolism by a lipid-carrying protein, the GABA, and taurine enzymes in mammalian brain. One paper examines the role of vitamin D in the metabolism of cells, as well as in the whole animal. Upon absorption in the body, the vitamin undergoes various metabolic transformations before interacting with specific receptors, and then inducting the genome in the target tissues to generate biological and hormonal responses. Another paper notes the possibility of a genetic defect in cancer cells that results in the abnormal accumulation of sterol carrier protein (SCP) and cholesterol in vivo; and also in the inability to maintain levels of SCP or cholesterol in vitro. One paper shows that tartrate, or other organic acids, secreted into the medium by the penicillia keeps the pH in an optimal range for acid protease degradation of proteins and glycoproteins. This mechanism helps the fungus to survive in a nutrient environment (which is unbalanced with respect to an optimum C/N ratio and at a pH unfavorable to many bacteria and other life forms). Another paper proposes a model for the modulation of ATP synthetase activities and medium exchange reactions by energy input, substrate concentration, or others that affect the microenvironment of the enzyme under certain conditions. The compendium will prove beneficial to molecular biologists, general biologists, microbiologists, and biochemists.

Principles of Enzyme Kinetics discusses the principles of enzyme kinetics at an intermediate level. It is primarily written for first-year research students in enzyme kinetics. The book is composed of 10 chapters. Chapter 1 provides the basic principles of enzyme kinetics with a brief discussion of dimensional analysis. Subsequent chapters cover topics on the essential characteristics of steady-state kinetics, temperature dependence, methods for deriving steady-state rate equations, and control of enzyme activity. Integrated rate equations, and introductions to the study of fast reactions and the statistical aspects of enzyme kinetics are provided as well. Chemists and biochemists will find the book invaluable.

This enzymology textbook for graduate and advanced undergraduate students covers the syllabi of most universities where this subject is regularly taught. It focuses on the synchrony between the two broad mechanistic facets of enzymology: the chemical and the kinetic, and also highlights the synergy between enzyme structure and mechanism. Designed for self-study, it explains how to plan enzyme experiments and subsequently analyze the data collected. The book is divided into five major sections: 1] Introduction to enzymes, 2] Practical aspects, 3] Kinetic Mechanisms, 4] Chemical Mechanisms, and 5] Enzymology Frontiers. Individual concepts are treated as stand-alone chapters; readers can explore any single concept with minimal cross-referencing to the rest of the book. Further, complex approaches requiring specialized techniques and involved experimentation (beyond the reach of an average laboratory) are covered in theory with suitable references to guide readers. The book provides students, researchers and academics in the broad area of biology with a sound theoretical and practical knowledge of enzymes. It also caters to those who do not have a practicing enzymologist to teach them the subject.

Enzyme structure. Isolation of enzymes. Reaction mechanisms. Enzyme kinetics. Theories of enzyme catalysis. Examples of enzyme catalysis. Enzymes without prosthetic groups. Coenzymes. Protein coenzymes. Covalent catalysis. Metals and enzymes. Control. Quaternary structure and allosteric control. Regulated enzyme reactions. Physical organization of enzymes. Chemotherapeutic control of enzyme reactions. Complex allosteric control systems.