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Acid proteases : structure, function, and biology

Author: Jordan Tang
Publisher: New York : Plenum Press, ©1977.
Series: Advances in experimental medicine and biology, v. 95.
Edition/Format:   Print book : Conference publication : EnglishView all editions and formats
Summary:
In the past ten years, a number of proceedings of symposia on the structure and function of proteolytic enzymes have been published. 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 determined, prompting the need to  Read more...
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Genre/Form: Congresses
Conference papers and proceedings
Congrès
Additional Physical Format: Online version:
Acid proteases.
New York : Plenum Press, ©1977
(OCoLC)610182484
Material Type: Conference publication
Document Type: Book
All Authors / Contributors: Jordan Tang
ISBN: 0306326957 9780306326950
OCLC Number: 3293067
Notes: "Proceedings of a conference on acid proteases: structure, function, and biology, held at the University of Oklahoma, Oklahoma City, November 21-24, 1976."
Description: ix, 355 pages : illustrations ; 26 cm.
Contents: Primary and Three-Dimensional Structure.- 1. Comparison of Primary Structures of Acid Proteases and their Zymogens.- 2. X-Ray Crystallographic Studies of Pepsin.- 3. The Crystal Structure of an Acid Protease from Rhizopus Chinensis at 2.5 A Resolution.- 4. X-Ray Analysis and Circular Dichroism of the Acid Protease from Endothia Parasitica and Chymosin.- 5. Penicillopepsin: 2.8 A Structure, Active Site Conformation and Mechanistic Implications.- Mechanism of Pepsinogen Activation.- 6. Intramolecular Activation of Pepsinogen.- 7. The First Cleavage Site in Pepsinogen Activation.- Catalytic Mechanism of Pepsin.- 8. Specificity and Mechanism of Pepsin Action on Synthetic Substrates.- 9. Subsite Specificity of Porcine Pepsin.- 10. Anhydride Intermediates in Catalysis by Pepsin: Is Pepsin an Enzyme with Two Active Sites?.- 11. New Data on Pepsin Mechanism and Specificity.- 12. Pepstatin Inhibition Mechanism.- 13. Chemical Modification of a Pepsin Inhibitor from the Activation Peptides of Pepsinogen.- Acid Proteases in Various Biological Systems.- 14. Renin and Precursors: Purification, Characterization, and Studies on Active Site.- 15. Inactive Renin - A Renin Proenzyme?.- 16. Characteristics and Functions of Proteinase A and Its Inhibitors in Yeast.- 17. Human Cathepsin D.- 18. Unique Biochemical and Biological Features of Cathepsin D in Rodent Lymphoid Tissues.- 19. Specificity and Biological Role of Cathepsin D.- 20. Acid Protease and its Proenzyme from Human Seminal Plasma.- List of Communications and Posters.- Conference Participants.
Series Title: Advances in experimental medicine and biology, v. 95.
Responsibility: edited by Jordan Tang.

Abstract:

In the past ten years, a number of proceedings of symposia on the structure and function of proteolytic enzymes have been published. 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 determined, prompting the need to discuss the meanings of the old data and the possibilities for new experimentations. It was for this purpose that this book 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 diazoacetylnorleucine 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 common features have prompted the suggestion by several investigators to name this group of enzymes "aspartyl proteases" or "carboxyl proteases". Such proposals are particularly valid if one considers that the optimal pH of renin is about 6, but its catalytic residues and mechanism obviously belong to that of the acid proteases. Regardless of the name eventually adopted, there is little question that this is a group of proteases with a structure-function relationship different from other groups of proteases. They appear to have some important functions in various biological systems.

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