Dalbey Co- and Posttranslational Proteolysis of Proteins

3. Auflage 2001
ISBN: 978-0-08-054244-7
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, Band Volume 22, 509 Seiten

Reihe: The Enzymes

This volume examines a number of different proteases, a type of enzyme, that are required in order for the change to a biologically active mature protein to occur. The discussion of these various proteases is rarely undertaken in one volume and will serve as a great resource for scientists studying the group of proteases on signal peptide processing as well as those working on propeptide processing. These areas of research do not normally overlap, and yet they are each of common importance to the same cell processes.

Autoren/Hrsg.

Dalbey, Ross

Inhaltsverzeichnis

1;Front Cover;1
2;The Enzymes;4
3;Copyright Page;5
4;Contents;6
5;Preface;12
6;Section I: Signal Peptide Processing;14
6.1;Chapter 1. The Eubocteriol Lipoprotein-Specific (Type II) Signal Peptidase;16
6.1.1;I. General Introduction;17
6.1.2;II. Type ll SPases;18
6.1.3;III. Lipoproteins;25
6.1.4;IV. The Role of Lipoprotein Processing by SPase II;33
6.1.5;V. Outlook;34
6.1.6;VI. Summary;34
6.1.7;References;36
6.2;Chapter 2. Bacterial Type I Signal Peptidases;40
6.2.1;I. Introduction: Bacterial Signal Peptidase, Signal Peptides and Protein Targeting;41
6.2.2;II. Type I Signal Peptidase Enzymology;50
6.2.3;III. Three-Dimensionai Structure;59
6.2.4;IV. Other Ser-Lys Dyad Proteases and Amidases;64
6.2.5;V. Conclusions and Perspective;64
6.2.6;References;66
6.3;Chapter 3. Structure and Function of the Endoplasmic Reticulum Signal Peptidase Complex;70
6.3.1;I. Introduction;71
6.3.2;II. Structure of the Signal Peptidase Complex;74
6.3.3;III. Function of SPC;81
6.3.4;IV. Roles of the SPC Subunits;84
6.3.5;V. Future Directions;86
6.3.6;References;86
6.4;Chapter 4. Mitochondrial Processing Peptidase/Mitochondrial Intermediate Peptidase;90
6.4.1;I. Introduction;91
6.4.2;II. Overview of Mitochondrial Protein Import;91
6.4.3;III. Mitochondrial Processing Peptidase;93
6.4.4;IV. Mitochondrial Intermediate Peptidase;102
6.4.5;References;110
6.5;Chapter 5. Chloroplast and Mitochondrial Type I Signal Peptidases;114
6.5.1;I. Chloroplast Type I Signal Peptidase: The Thylakoidal Processing Peptidase;114
6.5.2;II. Mitochondrial Type I Signal Peptidase: The Mitochondrial Inner Membrane Protease;124
6.5.3;III. Origins of the Chloroplast and Mitochondrial Type I Signal Peptidases;134
6.5.4;References;136
6.6;Chapter 6. Type IV Prepilin Leader Peptidases;140
6.6.1;I. Introduction;140
6.6.2;II. The Substrates of Type IV Prepilin Peptidases;142
6.6.3;III. Genetic Characterization of Type IV Prepilin Peptidases;148
6.6.4;IV. Cellular Localization and Topology of Type IV Prepilin Peptidases;152
6.6.5;V. Characterization of Type IV Prepilin Peptidase Activity;156
6.6.6;VI. Role of Leader Peptide Cleavage and N-Methylation in Pilus Biogenesis and Type II Secretion;159
6.6.7;VII. Structure–Function of the Type IV Prepilin Peptidases;161
6.6.8;VIII. Substrate Specificity of Type IV Peptidases and Enzyme Kinetics;166
6.6.9;IX. Future Directions;169
6.6.10;References;170
7;Section II: Preprocessing;174
7.1;Chapter 7. The Prohormone Convertases and Precursor Processing in Protein Biosynthesis;176
7.1.1;I. Introduction and Historical Perspective;177
7.1.2;II. The Proprotein Convertase Family;195
7.1.3;III. Effects of Mutations and/or Disruptions in Convertase Genes;199
7.1.4;IV. Are There Other Convertases?;203
7.1.5;V. Conclusions and Future Glimpses;204
7.1.6;References;206
7.2;Chapter 8. Furin;212
7.2.1;I. Introduction;212
7.2.2;II. Identification/Expression;214
7.2.3;III. Structure;216
7.2.4;IV. Biochemical Characteristics;217
7.2.5;V. Furin Cleavage Site Requirements;219
7.2.6;VI. Furin Biosynthesis;221
7.2.7;VII. Intracellular Localization and Trafficking of Furin;225
7.2.8;VIII. Furin Substrates;230
7.2.9;IX. Furin Inhibitors;234
7.2.10;X. Role of Furin in Vivo ;236
7.2.11;XI Furin and Pathogenesis;239
7.2.12;XII. Conclusion;241
7.2.13;References;242
7.3;Chapter 9. Cellular Limited Proteolysis of Precursor Proteins and Peptides;250
7.3.1;I. Processing of Precursors at Single and Dibasic Residues and at Nonbasic Sites;250
7.3.2;II. The Regulation of Processing within the Constitutive and Regulated Secretory Pathways;253
7.3.3;III. Convertases' Gene Structures, Evolution, and Knockout;257
7.3.4;IV. Proprotein Convertases and the Processing of a- and ß-Secretases Implicated in the Etiology of Alzheimer's Disease;266
7.3.5;V. Conclusions;268
7.3.6;VI. Summary;268
7.3.7;References;269
7.4;Chapter 10. Yeast Kex2 Protease;272
7.4.1;I. General Introduction;273
7.4.2;IL Primary Structure of Kex2 Protease;275
7.4.3;in. Phenotypes Associated with kex2 Mutations;277
7.4.4;IV. Characterization of Kex2 Specificity in Vivo;279
7.4.5;V. Cellular Aspects of Kex2 Function;280
7.4.6;VI. Purification and Characterization of Kex2 Protease;282
7.4.7;VII. Detailed Characterization of Specificity in Vitro;286
7.4.8;VIII. Pre-Steady-State Characterization of Kex2 Protease;292
7.4.9;IX. Kex2 as a Paradigm for Processing Protease Structure and Function;295
7.4.10;References;299
7.5;Chapter 11. The Enzymology of PC1 and PC2;304
7.5.1;I. Introduction;304
7.5.2;II. Substrate Specificity of PC1 and PC2;312
7.5.3;III Inhibitory Specificity of PC1 and PC2;326
7.5.4;IV. General Summary and Conclusions;338
7.5.5;References;341
8;Section III: Other Proteases That Cleave Proteins;346
8.1;Chapter 12. Self-Processing of Subunits of the Proteosome;348
8.1.1;I. Introduction;348
8.1.2;II. The 20S Proteasome;352
8.1.3;III. Maturation of ß-Type Subunits;360
8.1.4;IV. Functional Aspects: Why Proregions?;373
8.1.5;References;380
8.2;Chapter 13. Tsp and Related Tail-Specific Proteases;386
8.2.1;I. Introduction;386
8.2.2;II. Identification and General Structural Properties;387
8.2.3;III. Activity and Active-Site Residues;388
8.2.4;IV. Kinetic Constants;390
8.2.5;V. Substrate Specificity;391
8.2.6;VI. Phylogenetic Distribution;395
8.2.7;VII. Phenotypes;397
8.2.8;VIII. Biological Functions;397
8.2.9;References;398
8.3;Chapter 14. Co- and Posttranslational Processing: The Removal of Methionine;400
8.3.1;I. N-Terminal Processing: An Overview;400
8.3.2;II. Initiation of Protein Synthesis;403
8.3.3;III. The Methionine Aminopeptidases;404
8.3.4;IV. Future Directions;429
8.3.5;References;430
8.4;Chapter 15. Corboxypeptidases E and D;434
8.4.1;I. Introduction;434
8.4.2;II. Carboxypeptidase E;435
8.4.3;III. Carboxypeptidase D;449
8.4.4;IV. Other Members of the Carboxypeptidase E/D Subfamily;459
8.4.5;V Concluding Remarks;460
8.4.6;References;461
9;Author Index;466
10;Subject Index;506
11;Color Plate Section;516