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Author: Jordan Tang
Publisher: Springer Science & Business Media
ISBN: 1475707193
Category : Science
Languages : en
Pages : 350
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Book Description
In the past ten years, a number of proceedings of symposia on the structure and function of proteolytic enzymes have been pub lished. Their coverage of acid proteases has been limited, mainly due to the lack of significant new information on the structure of these enzymes. In the last four years, however, the primary and tertiary structures of a number of acid proteases have been deter mined, prompting the need to discuss the meanings of the old data and the possibilities for new experimentations. It was for this purpose that the "Conference on Acid Proteases: Structure, Function, and Biology" was organized. It took place at the University of Oklahoma on November 21-24, 1976. This book is a collection of the main lectures delivered at the Conference. Acid Proteases, by definition refers to a group of proteases having an optimal pH in acidic solutions. The classic examples are pepsin and chymosin. Some catalytic features are obviously shared by these proteases, most notably, their inhibition by pepstatin. The use of active center-directed inactivators such as diazoacetyl norleucine methyl ester and 1,2-epoxy-3-(p-nitrophenoxy)propane has shown that two catalytic aspartyl residues are present in most of these enzymes. These apparent cornmon features have prompted the suggestion by several investigators to name this group of enzymes "aspartyl proteases" or "carboxyl proteases".
Author: Jordan Tang
Publisher: Springer Science & Business Media
ISBN: 1475707193
Category : Science
Languages : en
Pages : 350
Get Book
Book Description
In the past ten years, a number of proceedings of symposia on the structure and function of proteolytic enzymes have been pub lished. Their coverage of acid proteases has been limited, mainly due to the lack of significant new information on the structure of these enzymes. In the last four years, however, the primary and tertiary structures of a number of acid proteases have been deter mined, prompting the need to discuss the meanings of the old data and the possibilities for new experimentations. It was for this purpose that the "Conference on Acid Proteases: Structure, Function, and Biology" was organized. It took place at the University of Oklahoma on November 21-24, 1976. This book is a collection of the main lectures delivered at the Conference. Acid Proteases, by definition refers to a group of proteases having an optimal pH in acidic solutions. The classic examples are pepsin and chymosin. Some catalytic features are obviously shared by these proteases, most notably, their inhibition by pepstatin. The use of active center-directed inactivators such as diazoacetyl norleucine methyl ester and 1,2-epoxy-3-(p-nitrophenoxy)propane has shown that two catalytic aspartyl residues are present in most of these enzymes. These apparent cornmon features have prompted the suggestion by several investigators to name this group of enzymes "aspartyl proteases" or "carboxyl proteases".
Author: Jordan Tang
Publisher:
ISBN: 9781475707205
Category :
Languages : en
Pages : 370
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Book Description
Author: P. Desnuelle
Publisher: Elsevier
ISBN: 1483261174
Category : Science
Languages : en
Pages : 310
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Book Description
Structure–Function Relationships of Proteolytic Enzymes provides information pertinent to the fundamental aspects of proteolytic enzymes. This book presents the historical role of proteolytic enzyme as a group in protein and enzyme chemistry. Organized into 23 chapters, this book begins with an overview of the results obtained from investigation on the chymotrypsinogens of porcine origin. This text then examines the differences of amino acid sequence between chymotrypsin, trypsin, and elastase that affect the substrate binding site, which reflect the specificity differences between these enzymes. Other chapters consider the kinetic parameters related to the trypsin-catalyzed hydrolysis of several model peptides. This book discusses as well the acetylation of trypsin, which result in functional consequences varying from complete inactivation to promotion of activity. The final chapter deals with the physical properties of stem bromelain in comparison with the data for three other sulfhydryl proteases of plant origin. This book is a valuable resource for enzymologists, microbiologists, and biochemists.
Author: Bruce Alberts
Publisher:
ISBN: 9780815332183
Category : Cytology
Languages : en
Pages : 0
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Book Description
Author:
Publisher: Academic Press
ISBN: 9780080865966
Category : Technology & Engineering
Languages : en
Pages : 459
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Book Description
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.
Author: Laszlo Polgar
Publisher: CRC Press
ISBN: 9780849369018
Category : Medical
Languages : en
Pages : 236
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Book Description
A uniform treatment of the four protease groups and a discussion of the differences and similarities in their action is presented in this important new publication. Serine, cysteine, aspartate, and zinc proteases are systematically discussed by nomenclature, evolution, specificity and their regulatory role. The chemistry of the peptide bond, including the catalysis of ester and peptide hydrolyses, is explained. For each protease group the emphasis is placed on the structure and function. Kinetics, enzyme modifications, isotope effects, subzero temperature investigations, nuclear magnetic resonance measurements, X-ray diffraction data, binding of transition-state analogs, zymogen activation, and site-specific mutagenesis are combined to rationalize the action of proteases. Both natural and synthetic inhibitors are considered because of their importance in mechanistic studies and drug design.
Author: Kenji Takahashi
Publisher: Springer Science & Business Media
ISBN: 1461518717
Category : Science
Languages : en
Pages : 614
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Book Description
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.
Author: Ben M. Dunn
Publisher: Springer Science & Business Media
ISBN: 1468460129
Category : Science
Languages : en
Pages : 561
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Book Description
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.
Author: Klaudia Brix
Publisher: Springer
ISBN: 9783709119396
Category : Science
Languages : en
Pages : 0
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Book Description
Proteolysis is an irreversible posttranslational modification affecting each and every protein from its biosynthesis to its degradation. Limited proteolysis regulates targeting and activity throughout the lifetime of proteins. Balancing proteolysis is therefore crucial for physiological homeostasis. Control mechanisms include proteolytic maturation of zymogens resulting in active proteases and the shut down of proteolysis by counteracting endogenous protease inhibitors. Beyond the protein level, proteolytic enzymes are involved in key decisions during development that determine life and death – from single cells to adult individuals. In particular, we are becoming aware of the subtle role that proteases play in signaling events within proteolysis networks, in which the enzymes act synergistically and form alliances in a web-like fashion. Proteases come in different flavors. At least five families of mechanistically distinct enzymes and even more inhibitor families are known to date, many family members are still to be studied in detail. We have learned a lot about the diversity of the about 600 proteases in the human genome and begin to understand their physiological roles in the degradome. However, there are still many open questions regarding their actions in pathophysiology. It is in this area where the development of small molecule inhibitors as therapeutic agents is extremely promising. Approaching proteolysis as the most important, irreversible post-translational protein modification essentially requires an integrated effort of complementary research disciplines. In fact, proteolytic enzymes seem as diverse as the scientists working with these intriguing proteins. This book reflects the efforts of many in this exciting field of research where team and network formations are essential to move ahead.
Author: T. Shantha Raju
Publisher: John Wiley & Sons
ISBN: 1119053366
Category : Science
Languages : en
Pages : 293
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Book Description
A Comprehensive Guide to Crucial Attributes of Therapeutic Proteins in Biological Pharmaceuticals With this book, Dr. Raju offers a valuable resource for professionals involved in research and development of biopharmaceutical and biosimilar drugs. This is a highly relevant work, as medical practitioners have increasingly turned to biopharmaceutical medicines in their search for safe and reliable treatments for complex diseases, while pharmaceutical researchers seek to expand the availability of biopharmaceuticals and create more affordable biosimilar alternatives. Readers receive a thorough overview of the major co-translational modifications (CTMs) and post-translational modifications (PTMs) of therapeutic proteins relevant to the development of biotherapeutics. The majority of chapters detail individual CTMs and PTMs that may affect the physicochemical, biochemical, biological, pharmacokinetic, immunological, toxicological etc. properties of proteins. In addition, readers are guided on the methodology necessary to analyze and characterize these modifications. Thus, readers gain not only an understanding of CTMs/PTMs, but also the ability to design and assess their own structure-function studies for experimental molecules. Specific features and topics include: Discussion of the research behind and expansion of biopharmaceuticals Twenty chapters detailing relevant CTMs and PTMs of proteins, such as glycosylation, oxidation, phosphorylation, methylation, proteolysis, etc. Each chapter offers an introduction and guide to the mechanisms and biological significance of an individual CTM or PTM, including practical guidance for experiment design and analysis An appendix of biologic pharmaceuticals currently on the market, along with an assessment of their PTMs and overall safety and efficacy This volume will prove a key reference on the shelves of industry and academic researchers involved in the study and development of biochemistry, molecular biology, biopharmaceuticals and proteins in medicine, particularly as biopharmaceuticals and biosimilars become ever more prominent tools in the field of healthcare.
