Acid Proteases: Structure, Function, and Biology

1. Front Matter

   Pages i-ix

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2. Primary and Three-Dimensional Structures

   1. Front Matter

      Pages 1-1

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   2. Comparison of the Primary Structures of Acidic Proteinases and of Their Zymogens

      • Bent Foltmann, Vibeke Barkholt Pedersen

      Pages 3-22

   3. X-Ray Crystallographic Studies of Pepsin

      • N. S. Andreeva, A. E. Gustchina, A. A. Fedorov, N. E. Shutzkever, T. V. Volnova

      Pages 23-31

   4. The Crystal Structure of an Acid Protease from Rhizopus Chinensis at 2.5 a Resolution

      • E. Subramanian, M. Liu, I. D. A. Swan, D. R. Davies

      Pages 33-41

   5. X-Ray Analysis and Circular Dichroism of the Acid Protease from Endothia Parasitica and Chymosin

      • John Jenkins, Ian Tickle, Trevor Sewell, Luciano Ungaretti, Axel Wollmer, Tom Blundell

      Pages 43-60

   6. Penicillopepsin: 2.8 a Structure, Active Site Conformation and Mechanistic Implications

      • I-Nan Hsu, Louis T. J. Delbaere, Michael N. G. James, Theo Hofmann

      Pages 61-81

3. Mechanism of Pepsinogen Activation

   1. Front Matter

      Pages 83-83

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   2. Intramolecular Activation of Pepsinogen

      • Jean A. Hartsuck, Joseph Marciniszyn Jr., Jung San Huang, Jordan Tang

      Pages 85-102

   3. The First Cleavage Site in Pepsinogen Activation

      • John Kay, Colin W. Dykes

      Pages 103-127

4. Catalytic Mechanism of Pepsin

   1. Front Matter

      Pages 129-129

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   2. Specificity and Mechanism of Pepsin Action on Synthetic Substrates

      • Joseph S. Fruton

      Pages 131-140

   3. Subsite Specificity of Porcine Pepsin

      • James C. Powers, A. Dale Harley, Dirck V. Myers

      Pages 141-157

   4. Anhydride Intermediates in Catalysis by Pepsin: Is Pepsin an Enzyme with Two Active Sites?

      • E. T. Kaiser, Y. Nakagawa

      Pages 159-177

   5. New Data on Pepsin Mechanism and Specificity

      • Vladimir K. Antonov

      Pages 179-198

   6. Pepstatin Inhibition Mechanism

      • Joseph Marciniszyn Jr., Jean A. Hartsuck, Jordan Tang

      Pages 199-210

   7. Chemical Modification of a Pepsin Inhibitor from the Activation Peptides of Pepsinogen

      • P. M. Harish Kumar, Peter H. Ward, Beatrice Kassell

      Pages 211-222

5. Acid Proteases in Various Biological Systems

   1. Front Matter

      Pages 223-223

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   2. Renin and Precursors: Purification, Characterization, and Studies on Active Site

      • Tadashi Inagami, Kazuo Murakami, Kunio Misono, Robert J. Workman, Stanley Cohen, Yasunobu Suketa

      Pages 225-247

   3. Inactive Renin — A Renin Proenzyme?

      • B. J. Leckie, A. McConnell, J. Jordan

      Pages 249-269

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".

• biology
• enzyme
• enzymes
• experiment
• information
• structure
• tertiary structure
• tissue

• Oklahoma Medical Research Foundation, USA

  Jordan Tang

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