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In September, 1990, a group of 160 scientists from 19 countries and 21 of the United States met at the Red Lion Inn in Rohnert Park, Sonoma County, California. The purpose of this meeting was to share new information from recent research on the Aspartic Proteinases. This book is a compilation of the information transferred in that forum. The Aspartic Proteinases include all those enzymes from the "fourth" class of proteolytic enzymes, the first three being the Serine, Cysteine and Metalloproteinases. Of course, all the scientists in attendance at the Sonoma Aspartic Proteinase Conference would agree that our current level of understanding of the structure and function of the Aspartic Proteinase class of enzymes is clearly first class. The reasons for this require a bit of historical perspective. The group of scientists who are engaged in study of this family of enzymes first met as a separate entity in 1976, in Norman, Oklahoma, at a meeting organized by Jordan Tang of the Oklahoma Medical Research Foundation. This was an exciting time, as the first crystal structures of some of these enzymes were described by Blundell, James and Davies. During that conference, the relationship between the two halves of the mammalian and fungal enzymes was recognized and this has provided a structural foundation for analysis of the retroviral enzymes, which came later. A book was published by Plenum Press documenting l this conference, and the current book is an update to that important work.
The 5th International Conference on Aspartic Proteinases was held on September 19 through 24, 1993, at Naito Museum of Pharmaceutical Science and Industry, Kawashima cho, Gifu Prefecture, Japan, about 15 miles northwest of Nagoya City. About 100 scientists attended the conference, including 52 from 14 countries outside Japan, and 32 papers were presented by invited speakers, and 58 papers as posters. The purpose of this conference was to present and discuss new information on the structure, function, and biology, and related topics, including biomedical implications, of aspartic proteinases, and this book is a collec tion of nearly all the papers presented at the meeting. Aspartic proteinases belong to one of the four major classes of proteinases, the others being serine, cysteine, and metalloproteinases, and are so called since they have two catalytic aspartic acid residues in common in their active sites. Most of them are optimally active at acidic pH, hence the long-used name "acid proteinases," which, indeed, was the major title of the first conference of this series. However, some of them are active at around neutral pH, indicating their physiological roles in a wider range of pH than hitherto considered.
The VIIth International Conference on Aspartic Proteinases was held in Banff, Alberta, Canada, from October 22 to 27, 1996. The venue was the Banff Centre in the Canadian Rockies, a setting well known worldwide for the scenic beauty and mountain grandeur. It was perhaps presumptuous of the organizers to call this the seventh Aspartic Proteinase Conference but it was felt that the meeting in 1982, organized by Tom Blundell and John Kay, was of an international stature and covered topics sufficiently broad to constitute a conference. Thus, there is a discontinuity in that the Gifu Conference organized by Prof. Kenji Takahashi was the fifth International Conference on Aspartic Proteinases. Officially, there has not been a sixth Conference and if there is confusion, it is the result of my desire to recognize the importance of the London meeting. Banffhosted 106 scientists from 14 different countries. There were 26 invited speak ers among the 44 oral presentations of the 7 main sessions. In addition, there were 53 con tributed poster presentations that spanned the whole range of interest in aspartic proteinases.
Published in 1995: Aspartic Proteinases: Physiology and Pathology focuses on the advantages and limitations of the use of proteinases and their inhibitors in human pathology. A virus-specific aspartic proteinase enzyme is required for the maturation of a virus. If the enzyme can be eliminated, so can the maturation of the virus. This book reviews the wealth of recently published information sparked by the renewed interest in these enzymes.
In this ground-breaking practical reference, the family of aspartic acid proteases is described from a drug developer's perspective. The first part provides a general introduction to the family of aspartic acid proteases, their physiological functions, molecular structure and inhibition. Parts two to five present various case studies of successful protease inhibitor drug design and development, as well as current and potential uses of such inhibitors in pharmaceutical medicine, covering the major therapeutic targets HIV-1 protease, renin, beta-secretase, gamma-secretase,plasmepsins and fungal proteases. A ready reference aimed primarily at professionals in the pharmaceutical industry, as well as for anyone studying proteases and their function.
In this volume of Methods in Enzymology and its companion Volume 244, the chapters on specific methods, enzymes, and inhibitors are organized within the rational framework of the new systems for classificationand nomenclature. A wide variety of specificities of peptide bond hydrolysis are represented in each set of peptidases, together with an equally wide range of biological functions. Key Features * Aspartic peptidases * Metallopeptidases * New information on classification of proteolytic enzymes * Medical implications of research in this area * Biotechnological uses of these enzymes.
Handbook of Proteolytic Enzymes, Second Edition, Volume 1: Aspartic and Metallo Peptidases is a compilation of numerous progressive research studies on proteolytic enzymes. This edition is organized into two main sections encompassing 328 chapters. This handbook is organized around a system for the classification of peptidases, which is a hierarchical one built on the concepts of catalytic type, clan, family and peptidase. The concept of catalytic type of a peptidase depends upon the chemical nature of the groups responsible for catalysis. The recognized catalytic types are aspartic, cysteine, metallo, serine, threonine, and the unclassified enzymes, while clans and families are groups of homologous peptidases. Homology at the level of a family of peptidases is shown by statistically significant relationship in amino acid sequence to a representative member called the type example, or to another member of the family that has already been shown to be related to the type example. Each chapter discusses the history, activity, specificity, structural chemistry, preparation, and biological aspects of the enzyme. This book will prove useful to enzyme chemists and researchers.
The remarkable expansion of information leading to a deeper understanding of enzymes on the molecular level necessitated the development of this volume which not only introduces new topics to The Enzymes series but presents new information on some covered in Volume I and II of this edition.