Acid Proteases:Structure, Function, and Biology

350 Pages·1977·10.635 MB·English

by  Bent Foltmann, Vibeke Barkholt Pedersen (auth.), Jordan Tang (eds.)

ACID PROTEASES
Structure, Function, and Biology
ADVANCES IN EXPERIMENTAL MEDICINE AND BIOLOGY
Editorial Board:
Nathan Back State University of New York at Buffalo
N. R. Di Luzio Tulane University School of Medicine
Bernard Halpern College de France and Institute of Immuno·Biology
Ephraim Katchalski The Weizmann Institute of Science
David Kritchevsky Wistar Institute
Abel Lajtha New York State Research Institute for Neurochemistry and Drug Addiction
RodoIro Paoletti University of Milan
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ACID PROTEASES: Structure, Function, and Biology
Edited by Jordan Tang
ACID PROTEASES
Structure, Function, and Biology
Edited by
Jordan Tang
Oklahoma Medical Research Foundation
SPRINGER SCIENCE+BUSINESS MEDIA. LLC
Library of Congress Cataloging in Publication Data
Main entry under title:
Acid proteases.
(Advances in experimental medicine and biology, v. 95)
"Proceedings of a conference on acid proteases: structure, function, and biology, held
at the University of Oklahoma, Norman, Oklahoma, November 21-24, 1976."
Includes index.
1. Protease-Congresses. 1. Tang, Jordan.
QP609.P7 A24 574.1'9256 77-13032
ISBN 978-1-4757-0721-2 ISBN 978-1-4757-0719-9 (eBook)
DOI 10.1007/978-1-4757-0719-9
Proceedings of a Conference on Acid Proteases: Structurt,
Function, and Biology held at the University of Oklahoma,
Norman, Oklahoma, November 21-24,1976
©1977 Springer Science+Business Media New York
Originally published by Plenum Press, New York in 1977
All rights reserved
No part of this book may be reproduced, stored in a retrieval system, or transmitted,
in any form or by any means, electronic, mechanical, photocopying, microfilming,
recording, or otherwise, without written permission from the Publisher
PREFACE
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". 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 ether groups
of proteases. They appear to have some important functions in
various biological systems.
It is my hope that the information collected in this volume
will stimulate a broader interest in future investigations of acid
proteases.
v
vi PREFACE
For the Conference, I wish to acknowledge the sponsorship of
the Oklahoma Medical Research Foundation, and financial support
through grants from the National Institutes of Health (GH-23661)
and from the National Science Foundation (PCM76-17344).
Special thanks should go to my colleague Dr. Jean A. Hartsuck
who has contributed thoughts and work, both for the Conference and
for the editing of the Proceedings, to Dr. David Davies of NIH and
Dr. Tadashi Inagami, Vanderbilt University, for help in designing
the scientific program, to Brs. Ester Pahlka, Conference Secretary,
for able organizational planning and execution, to Mr. and Mrs.
Milton Smith, Mr. David Ponder, Ms. Jan Rogers, Ms. Mary Simpson,
Ms. Dana Pitts, Ms. Vicki Cassady, Ms. Beverly Yurtis, and other
volunteers from the Oklahoma Hedical Research Foundation, for working
at the Conference with great enthusiasm, and to Ms. Lois Fagin, for
help in editing these Proceedings.
Jordan Tang
CONTENTS
PRIMARY AND THREE-DIMENSIONAL STRUCTURE
1. Comparison of Primary Structures of Acid Proteases
and their Zymogens ............................................. 3
B. Foltmann and V. B. Pedersen
2. X-Ray Crystallographic Studies of Pepsin ...................... 23
N. S. Andreeva, A. E. Gustchina, A. A. Fedorov,
N. E. Shutzkever, and T. V. Volnova
3. The Crystal Structure of an Acid Protease from
Rhizopus Chinensis at 2.5 A Resolution ........................ 33
E. Subramanian, M. Liu, I. D. A. Swan, and
D. R. Davies
4. X-Ray Analysis and Circular Dichroism of the Acid
Protease from Endothia Parasitica and Chymosin .. '" ........... 43
John Jenkins, Ian Tickle, Trevor Sewell, Luciano
Ungaretti, Axel Wollmer, and Tom Blundell
5. Penicillopepsin: 2.8 A Structure, Active Site
Conformation and Mechanistic Implications ..................... 61
I-Nan Hsu, Louis T. J. Delbaere, Michael N. G. James
and Theo Hofmann
MECHANISM OF PEPSINOGEN ACTIVATION
6. Intramolecular Activation of Pepsinogen ....................... 85
Jean A. Hartsuck, Joseph Marciniszyn, Jr., Jung San
Huang, and Jordan Tang
7. The First Cleavage Site in Pepsinogen Activation ............. 103
John Kay and Colin W. Dykes
vii
viii CONTENTS
CATALYTIC MECHANISM OF PEPSIN
8. Specificity and Mechanism of Pepsin Action on
Synthetic Substrates ......................................... 131
Joseph S. Fruton
9. Subsite Specificity of Porcine Pepsin ........................ 141
James C. Powers, A. Dale Harley, and Dirck V. Myers
10. Anhydride Intermediates in Catalysis by Pep'sin:
Is Pepsin an Enzyme with Two Active Sites? .................. 159
E. T. Kaiser and Y. Nakagawa
11. New Data on Pepsin Mechanism and Specificity ................. 179
Vladimir K. Antonov
12. Pepstatin Inhibition Mechanism ............................... 199
Joseph Marciniszyn, Jr., Jean A. Hartsuck, and
Jordan Tang
13. Chemical Modification of a Pepsin Inhibitor from
the Activation Peptides of Pepsinogen ........................ 211
P. M. Harish Kumar, Peter H. Ward, and Beatrice
Kassell
ACID PROTEASES IN VARIOUS BIOLOGICAL SYSTEMS
14. Renin and Precursors: Purification, Characterization,
and Studies on Active Site ................................... 225
Tadashi Inagami, Kazuo Murakami, Kunio Misono,
Robert J. Workman, Stanley Cohen, and Yasunobu Suketa
15. Inactive Renin - A Renin Proenzyme? ......................... 249
B. J. Leckie, A. McConnell, and J. Jordan
16. Characteristics and Functions of Proteinase A and
Its Inhibitors in yeast ...................................... 271
Helmut Holzer, Peter BUnning, and Franz Meussdoerffer
17. Human Cathepsin D. ........................................... 291
Alan J. Barrett
18. Unique Biochemical and Biological Features of
Cathepsin 0 in Rodent Lymphoid Tissues ....................... 301
William E. Bowers, John Panagides, and Nagasumi Yago
19. Specificity and Biological Role of Cathepsin D. .............. 313
J. Frederick Woessner, Jr.
CONTENTS
ix
20. Acid Protease and its Proenzyme from Human Seminal
Plasma ....................................................... 329
Pintip Ruenwongsa and Montri Chulavatnatol
List of COIllll1unications and Posters ............................. 343
Conference Participants ........................................ 345
Subj ect Index .................................................. 351