Recent developments in concepts and techniques have brought enzyme research to a changing yet exciting stage. Enzymes have served as indispensable tools in the phenomenal rise of molecular biology, and the resultant biotechnology thrusts enzymes to new heights and territories. This volume, the proceedings of a recent symposium on the Dynamics of Soluble and Immobilized Enzyme Systems, provides a current overview of the field to help scientists utilize long-established and newly acquired information.

Enzyme Catalysis and Regulation is an introduction to enzyme catalysis and regulation and covers topics ranging from protein structure and dynamics to steady-state enzyme kinetics, multienzyme complexes, and membrane-bound enzymes. Case studies of selected enzyme mechanisms are also presented. This book consists of 11 chapters and begins with a brief overview of enzyme structure, followed by a discussion on methods of probing enzyme structure such as X-ray crystallography and optical spectroscopy. Kinetic methods are then described, with emphasis on the general principles of steady-state and transient kinetics. The chemical principles involved in enzyme catalysis are also discussed, and case studies of a few well-documented enzymes are presented. The regulation of enzyme activity is analyzed from a nongenetic viewpoint, with particular reference to binding isotherms and models for allosterism. Two particular enzymes, aspartate transcarbamoylase and phosphofructokinase, are used as examples of well-studied regulatory enzymes. The last two chapters focus on multienzyme complexes and membrane-bound enzymes. This monograph is intended for graduate students, advanced undergraduates, and research workers in molecular biology and biochemistry.

We live in the age of science-the human and numerous other living beings' genomes have been sequenced and we are beginning to understand the capacity of the metabolic machinery responsible for life on our planet. A huge number of new genes have been discovered, a significant number of these coding for enzymes of yet obscure capacity. Understanding the kinetic behavior of an enzyme provides clues to its possible physiological role. From a biotechnological perspective, knowledge of the reactant properties of an enzyme is required for the design of immobilized enzyme-based modern processes. Biotransformations are of key importance to the pharmaceutical and sustenance industries, and knowledge of the reactant properties of enzymes, essential. This book is tied in with understanding the principles of enzyme kinetics and knowing how to use mathematical models to describe the reactant capacity of an enzyme. Coverage of the material is in no way, shape or form exhaustive. There exist many books on enzyme kinetics that offer intensive, in-depth treatises of the subject. Intracellular and extracellular physiological cascades are regulated by initiation and hindrance of different enzymes involved in these pathways. Investigating and understanding the mechanism of enzyme hindrance has become the premise of development of pharmaceutical agents. Organically active regular and synthetic inhibitors have been developed and special emphasis has been placed on investigations that define their structure-work relationships in an effort to understand the inception of their natural properties. A powerful complement to the assessment of these agents is the preparation and subsequent examination of key fractional structures, deep-seated auxiliary adjustments and the corresponding unnatural enantiomers of characteristic items. We sincerely hope that this book will represent an element in the tool kit of graduate students in applied science and chemical and biochemical engineering and furthermore of undergraduate students with formal preparing in natural chemistry, biochemistry, thermodynamics and chemical reaction kinetics.

General Description of the Volume: This volume, as do the other Enzyme Kinetics and Mechanism volumes in the Methods in Enzymology series, provides treatment of dynamic and chemical approaches for investigating enzyme catalysis and regulation, as well as designing metabolic inhibitors. It will greatly interest those involved in enzyme chemistry, metabolic control, and drug design. It should also interest those developing commercial applications for enzymes whose properties have been re-engineered using recombinant DNA technology and site-directed mutagenesis. General Description of the Series: The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.

This book covers the most recent developments in the analysis of allosteric enzymes and provides a logical introduction to the limits for enzyme function as dictated by the factors that are limits for life. The book presents a complete description of all the mechanisms used for changing enzyme activity. It is extensively illustrated to clarify kinetic and regulatory properties. Eight enzymes are used as model systems after extensive study of their mechanisms. Wherever possible, the human form of the enzyme is used to illustrate the regulatory features.

This book discusses how biological molecules exert their function and regulate biological processes, with a clear focus on how conformational dynamics of proteins are critical in this respect. In the last decade, the advancements in computational biology, nuclear magnetic resonance including paramagnetic relaxation enhancement, and fluorescence-based ensemble/single-molecule techniques have shown that biological molecules (proteins, DNAs and RNAs) fluctuate under equilibrium conditions. The conformational and energetic spaces that these fluctuations explore likely contain active conformations that are critical for their function. More interestingly, these fluctuations can respond actively to external cues, which introduces layers of tight regulation on the biological processes that they dictate. A growing number of studies have suggested that conformational dynamics of proteins govern their role in regulating biological functions, examples of this regulation can be found in signal transduction, molecular recognition, apoptosis, protein / ion / other molecules translocation and gene expression. On the experimental side, the technical advances have offered deep insights into the conformational motions of a number of proteins. These studies greatly enrich our knowledge of the interplay between structure and function. On the theoretical side, novel approaches and detailed computational simulations have provided powerful tools in the study of enzyme catalysis, protein / drug design, protein / ion / other molecule translocation and protein folding/aggregation, to name but a few. This work contains detailed information, not only on the conformational motions of biological systems, but also on the potential governing forces of conformational dynamics (transient interactions, chemical and physical origins, thermodynamic properties). New developments in computational simulations will greatly enhance our understanding of how these molecules function in various biological events.