Desnuelle / Neurath / Ottesen Structure-Function Relationships of Proteolytic Enzymes

Proceedings of the International Symposium, Copenhagen June 16-18, 1969, No. 37 in the Series of the International Union of Biochemistry Sponsored Symposia
1. Auflage 2014
ISBN: 978-1-4832-6117-1
Verlag: Elsevier Science & Techn.
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, 310 Seiten, Web PDF

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.

Autoren/Hrsg.

Desnuelle, P.

Neurath, H.

Ottesen, M.

Inhaltsverzeichnis

1;Front Cover;1
2;Structure-Function Relationships of Proteolytic Enzymes;4
3;Copyright Page;5
4;Table of Contents;8
5;Preface;6
6;List of Participants;12
7;Foreword
;18
8;Chapter 1. On the Three Chymotrypsinogens
of Porcine Pancreas;22
8.1;REFERENCES;34
8.2;COMMENTS;35
9;Chapter 2. Chymotrypsin:
Tertiary Structure and Enzymatic Activity;37
9.1;ABSTRACT;37
9.2;REFERENCES;37
9.3;COMMENTS;38
9.4;REFERENCES;39
10;Chapter 3. The Role of Carboxylates and Phenol Side-chains in the Activity and Conformation of Trypsinogen, Trypsin, Chymotrypsinogen, and
Chymotrypsin;43
10.1;I.
THE ROLE OF CARBOXYLATES;43
10.2;II. THE ROLE OF PHENOL SIDE-CHAINS;53
10.3;ACKNOWLEDGMENTS;55
10.4;REFERENCES;56
11;Chapter 4. Chemical Modifications of Bovine Trypsinogen
and Trypsin;57
11.1;ACETYLATION OF TRYPSIN WITH
N-ACETYLIMIDAZOLE;58
11.2;MECHANISM OF TRYPSINOGEN
ACTIVATION;62
11.3;ROLE OF CALCIUM IN THE ACTIVATION
PROCESS;64
11.4;WATER-INSOLUBLE TRYPSIN;67
11.5;ACKNOWLEDGMENTS;69
11.6;REFERENCES;69
12;Chapter 5. The Specificity Site of Trypsin;71
12.1;CHEMICAL MODIFICATION STUDIES;71
12.2;AUTODIGESTION OF TRYPSIN WITH
LOSS OF BINDING SPECIFICITY;76
12.3;SUMMARY;79
12.4;REFERENCES;79
12.5;COMMENTS;80
13;Chapter 6. Structure and Mechanism of Action
of a Pancreatic Trypsin Inhibitor;81
13.1;THE COVALENT STRUCTURE;81
13.2;MECHANISM OF ACTION;83
13.3;REFERENCES;88
14;Chapter 7. The Chemistry of the Reactive Site
of Soybean Trypsin Inhibitor;90
14.1;REACTIVE SITE;90
14.2;EQUILIBRIUM IN PEPTIDE BOND
CLEAVAGE;93
14.3;RESYNTHESIS OF THE CLEAVED
REACTIVE SITE BY RAPID DISSOCIATION OF THE COMPLEX;95
14.4;ENZYMATIC MUTATION;97
14.5;OTHER TOPICS;100
14.6;ACKNOWLEDGMENTS;101
14.7;REFERENCES;101
15;Chapter 8. Structural Aspects of Interaction of Trypsin with
Macromolecular Inhibitors;103
15.1;HYPOTHETICAL THREE-DIMENSIONAL
STRUCTURE OF TRYPSIN;103
15.2;TENTATIVE STRUCTURE OF TRYPSIN
INHIBITOR;104
15.3;NITRATION OF TYROSINE RESIDUES;104
15.4;ROLE OF CARBOXYL GROUPS;108
15.5;BASIC AMINO ACIDS AND
TRYPTOPHAN RESIDUES;109
15.6;FRAGMENT OF TRYPSIN BOUND
TO INHIBITOR;109
15.7;BINDING OF INHIBITOR TO ZYMOGEN;110
15.8;HOMOLOGY OF ACTIVE SITES IN
TWO POLYPEPTIDE INHIBITORS;111
15.9;REFERENCES;112
16;Chapter 9. Homology and Phylogeny of Proteolytic Enzymes;114
16.1;I.
PANCREATIC ENZYMES;117
16.2;II.
TRYPSINOGEN;118
16.3;III. METALLOGARBOXYPEPTIDASES;126
16.4;ACKNOWLEDGMENT;134
16.5;REFERENCES;134
16.6;COMMENTS;136
16.7;REFERENCES;138
17;Chapter 10. Structural Aspects of Thrombin and Prothrombin;139
17.1;ACKNOWLEDGEMENT;144
17.2;REFERENCES;144
18;Chapter 11. Cobalt Proteases: Implications of Absorption
and Circular Dichroism Spectra for Catalysis;145
18.1;REFERENCES for Table I;151
18.2;REFERENCES for Table II;153
18.3;REFERENCES;159
19;Chapter 12. Some Structure-Function Relationships
in the Subtilisins;161
19.1;PRIMARY SEQUENCE;161
19.2;ACTIVE SITE STUDIES;164
19.3;MODIFICATION STUDIES;166
19.4;SUBSTRATE SPECIFICITY;167
19.5;INHIBITORS;169
19.6;REFERENCES;172
20;Chapter 13. Subtilisin BPN':
Tertiary Structure and Inhibitor Binding;174
20.1;ABSTRACT;174
20.2;COMMENTS;175
21;Chapter 14. Subtilisin:
Stability Properties and Secondary Binding Sites;176
21.1;STABILITY PROPERTIES;176
21.2;ENZYMATIC PROPERTIES;179
21.3;REFERENCES;187
21.4;COMMENTS;188
21.5;REFERENCES;188
22;Chapter 15. Aminopeptidases from Thermophilic Microorganisms;189
22.1;ACKNOWLEDGEMENT;198
22.2;REFERENCES;198
23;Chapter 16. A Synthetic Approach to the Study of Microenvironmental
Effects on Enzyme Action;199
23.1;I. WATER-INSOLUBLE ENZYME
DERIVATIVES;200
23.2;II. ENZYME MEMBRANES;209
23.3;REFERENCES;221
24;Chapter 17. Specificity and Mechanism of Pepsin Action;223
24.1;REFERENCES;233
24.2;COMMENTS ;235
24.3;ACKNOWLEDGMENT;237
24.4;REFERENCES;237
25;Chapter 18. Towards a Mechanism for Pepsin;238
25.1;MECHANISTIC PROPOSALS;246
25.2;REFERENCES;250
25.3;COMMENTS

;252
26;Chapter 19. Chemical Studies on Purified Pepsin;254
26.1;PREPARATION OF PURIFIED PEPSIN;254
26.2;PROPERTIES OF THE PURIFIED ENZYME;256
26.3;REACTIONS WITH RESIDUES AT
THE ACTIVE SITE;256
26.4;MECHANISM OF INACTIVATION BY
DIAZO REAGENTS;260
26.5;CONCLUSIONS;260
26.6;REFERENCES;261
27;Chapter 20. Porcine Pepsinogen and Pepsin;262
27.1;CHEMICAL PROPERTIES OF PEPSINOGEN
AND PEPSIN;263
27.2;CONFORMATIONAL PROPERTIES OF
PEPSINOGEN AND PEPSIN;264
27.3;ACKNOWLEDGMENT;270
27.4;REFERENCES;271
27.5;COMMENTS;272
28;Chapter 21. The Three-Dimensional Structure of Papain;273
28.1;THE AMINO ACID SEQUENCE OF
THE MOLECULE;273
28.2;STRUCTURE OF THE MOLECULE;277
28.3;MECHANISM OF ACTION OF THE ENZYME;280
28.4;GEOMETRY OF THE ACTIVE SITE
AND PRODUCT BINDING;283
28.5;ACKNOWLEDGEMENT;289
28.6;REFERENCES;289
29;Chapter 22. Streptococcal Proteinase;290
29.1;PREPARATION AND PROPERTIES OF
THE ENZYME;290
29.2;COMPARISON OF THE STREPTOCOCCAL
PROTEINASE A N D PAPAIN;294
29.3;CONCLUSIONS;296
29.4;REFERENCES;297
30;Chapter 23. Structure and Function of Stem Bromelain;299
30.1;PURIFICATION A N D GENERAL
PROPERTIES;299
30.2;STEM BROMELAIN AS A GLYCOPROTEIN;300
30.3;ACTIVE SITE SEQUENCE;304
30.4;KINETIC FEATURES;306
30.5;PHYLOGENETIC REMARKS;309
30.6;REFERENCES;309