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Handbook of Proteolytic Enzymes, Volume 1
- 2nd Edition - May 17, 2004
- Editors: Alan J. Barrett, J. Fred Woessner, Neil D. Rawlings
- Language: English
- Paperback ISBN:9 7 8 - 0 - 1 2 - 4 1 2 1 0 5 - 8
- eBook ISBN:9 7 8 - 0 - 0 8 - 0 9 8 4 1 5 - 5
Handbook of Proteolytic Enzymes, Second Edition, Volume 1: Aspartic and Metallo Peptidases is a compilation of numerous progressive research studies on proteolytic enzymes. This… Read more
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Request a sales quoteHandbook of Proteolytic Enzymes, Second Edition, Volume 1: Aspartic and Metallo Peptidases is a compilation of numerous progressive research studies on proteolytic enzymes. This edition is organized into two main sections encompassing 328 chapters. This handbook is organized around a system for the classification of peptidases, which is a hierarchical one built on the concepts of catalytic type, clan, family and peptidase. The concept of catalytic type of a peptidase depends upon the chemical nature of the groups responsible for catalysis. The recognized catalytic types are aspartic, cysteine, metallo, serine, threonine, and the unclassified enzymes, while clans and families are groups of homologous peptidases. Homology at the level of a family of peptidases is shown by statistically significant relationship in amino acid sequence to a representative member called the type example, or to another member of the family that has already been shown to be related to the type example. Each chapter discusses the history, activity, specificity, structural chemistry, preparation, and biological aspects of the enzyme. This book will prove useful to enzyme chemists and researchers.
Editor Biographies
Contributors
Preface
Introduction
Abbreviations
Aspartic Peptidases
Introduction
1 Aspartic Peptidases and their Clans
2 Catalytic Pathway of Aspartic Peptidases
Clan AA
Family A1 3 Pepsin A
4 Pepsin B
5 Chymosin
6 Cathepsin E
7 Gastricsin
8 Cathepsin D
9 Napsin A
10 Renin
11 Mouse Submandibular Renin
12 Memapsin 1
13 Memapsin 2
14 Plasmepsins
15 Plasmepsin II
16 Tick Heme-Binding Aspartic Proteinase
17 Phytepsin
18 Nepenthesin
19 Saccharopepsin
20 Neurosporapepsin
21 Acrocylindropepsin
22 Aspergillopepsin I
23 Penicillopepsin
24 Endothiapepsin
25 Rhizopuspepsin
26 Mucorpepsin
27 Polyporopepsin
28 Candidapepsin
29 Candiparapsin
30 Canditropsin
31 Syncephapepsin
32 Barrierpepsin
33 Yapsin 1
34 Yapsin 2
35 Yapsin A
36 Pregnancy-Associated Glycoproteins
37 Pepsin F
38 Rhodotorulapepsin
39 Cladosporopepsin
40 Pycnoporopepsin
Family A2 and Others 41 Human Immunodeficiency Virus 1 Retropepsin
42 Human Immunodeficiency Virus 2 Retropepsin
43 Simian Immunodeficiency Virus Retropepsin
44 Equine Infectious Anemia Virus Retropepsin
45 Rous Sarcoma Virus Retropepsin and Avian Myeloblastosis Virus Retropepsin
46 Human T-Cell Leukemia Virus Type I (HTLV-I) Retropepsin
47 Bovine Leukemia Virus Retropepsin
48 Mason-Pfizer Monkey Virus Retropepsin
49 Mouse Mammary Tumor Virus Retropepsin
50 Moloney Murine Leukemia Virus Retropepsin
51 Feline Immunodeficiency Virus Retropepsin
52 Human Retrovirus K10 Retropepsin
53 Miscellaneous Viral Retropepsins
54 Spumapepsins
55 Fungal, Plant and Animal Retrotransposon Elements
56 Cauliflower Mosaic Virus Proteinase
Other Clans of Aspartic Peptidases
57 Nodavirus Endopeptidase
58 Signal Peptidase II
59 Type IV Prepilin Peptidase
60 Presenilins
61 Omptin
62 Plasminogen Activator of Yersinia Pestis
63 Scytalidopepsin B
64 Aspergillopepsin II
65 Scytalidopepsin A
66 Thermopsin
Metallopeptidases
Introduction
67 Metallopeptidases and their Clans
68 Catalytic Mechanisms for Metallopeptidases
Clan MA Subclan E
Family M1 69 Membrane Alanyl Aminopeptidase
70 Aminopeptidase Ey
71 Insect Aminopeptidase N
72 Aminopeptidase A
73 Pyroglutamyl-Peptidase II
74 Cystinyl Aminopeptidase, Oxytocinase and Insulin-Regulated Aminopeptidase
75 Aminopeptidase PILS
76 Aminopeptidase PS
77 Yeast Aminopeptidases Ape2, Aap1' and Yin7
78 Lysyl Aminopeptidase (Bacteria)
79 Aminopeptidase N (Streptomyces Lividans)
80 Leukotriene A4 hydrolase
81 Aminopeptidase B
Family M2 82 Peptidyl-Dipeptidase A/Angiotensin I-Converting Enzyme
83 Peptidyl-Dipeptidase A (Invertebrate)
84 Angiotensin-Converting Enzyme
Family M3 85 Thimet Oligopeptidase
86 Neurolysin
87 Saccharolysin
88 Oligopeptidase A
89 Peptidyl-Dipeptidase Dcp
90 Mitochondrial Intermediate Peptidase
91 Oligopeptidase F
92 Oligopeptidase PepB
93 Oligopeptidase MepB
Families M4, M5 and M9 94 Thermolysin and Related Bacillus Metallopeptidases
95 Lambda Toxin (Clostridium Perfringens)
96 Aureolysin
97 Listeria Metalloprotease Mp1
98 Griselysin
99 Coccolysin
100 Pro-Aminopeptidase Processing Protease
101 Vibriolysin
102 Pseudolysin
103 Legionella Metalloendopeptidase
104 Vimelysin
105 Mycolysin
106 Vibrio Collagenase
107 Clostridium Collagenases
Family M13 108 Neprilysin
109 Neprilysin-2
110 Endothelin-Converting Enzyme 1
111 Endothelin-Converting Enzyme 2
112 Endothelin-Converting Enzyme-Like Peptidase 1
113 PHEX Endopeptidase
114 Kell Blood-Group Protein
115 Neprilysin Homolog of Streptococci
116 Oligopeptidase O
Other Families in Subclan MA(E) 117 Tentoxylysin
118 Bontoxilysins
119 Hyicolysin
120 Procollagen III N-Proteinase
121 Ste24 Protease
122 Mammalian Famesylated Protein-Converting Enzyme 1
123 Baculovirus Enhancin
124 Glycyl Aminopeptidase (Sphingomonas)
Clan MA Subclan M
Families M10 and M11 125 Collagenase 1
126 Neutrophil Collagenase
127 Collagenase 3
128 Collagenase 4
129 Gelatinase A
130 Gelatinase B
131 Stromelysin 1
132 Stromelysin 2
133 Stromelysin 3
134 Matrilysin
135 Matrilysin 2
136 Macrophage Elastase
137 Membrane-Type Matrix Metalloproteinase 1
138 Membrane-Type Matrix Metalloproteinase 2
139 Membrane-Type Matrix Metalloproteinase 3
140 Membrane-Type Matrix Metalloproteinase 4
141 Membrane-Type Matrix Metalloproteinase 5
142 Membrane-Type Matrix Metalloproteinase 6
143 RASI-1, MMP-19
144 Enamelysin
145 Matrix Metalloproteinase 21
146 Chicken Matrix Metalloproteinase 22
147 Matrix Metalloproteinase 23
148 Epilysin
149 Plant Matrixins
150 Hydra Matrix Metalloproteinase (HMMP)
151 Envelysin
152 Serralysin and Related Enzymes
153 Aeruginolysin
154 Mirabilysin
155 Epralysin
156 Fragilysin
157 Gametolysin
Family M12 Subfamily A 158 Astacin
159 Meprin A
160 Meprin B
161 Procollagen C-Endopeptidase
162 Tolloid (Drosophila)
163 Mammalian Tolloid-Like Peptidases
164 Choriolysin L
165 Choriolysin H
166 Hydra Metalloproteinase 1 (HMP1)
167 Flavastacin
168 Other Astacin Homologs
Family M12 Subfamily B 169 Brevilysin H6
170 Acutolysin
171 Bilitoxin
172 Fibrolase
173 Venom Metalloproteinases of Agkistrodon Contortrix Laticinctus
174 Gloydius Halys Venom Metalloproteinases
175 Leucolysin
176 Bids Arietans Hemorrhagic Proteinases
177 Bothrops Asper Hemorrhagic Proteinases
178 Jararhagin
179 Bothrolysin
180 Bothropasin
181 Jararafibrases II-IV of Bothrops Jararaca
182 Basic Endopeptidases of Bothrops Moojeni Venom
183 Kistomin
184 Adamalysin
185 Atrolysin A
186 Atrolysin B
187 Atrolysin C
188 Atrolysin E
189 Atrolysin F
190 Atroxase
191 Basilysin
192 Horrilysin
193 Ruberlysin
194 Russellysin
195 Carinactivase
196 Multactivase
197 Ecarin
198 Mutalysins
199 Najalysin
200 Mocarhagin
201 Ophiolysin
202 Philodryas Venom Metalloproteinases
203 Trimerelysin I
204 Trimerelysin II
205 Mucrolysin
206 Lebetase
207 ADAM Metalloproteinases
208 ADAM9
209 ADAM28, Mouse Form
210 ADAM19
211 Kuzbanian (Drosophila)
212 ADAM12
213 Tumor Necrosis Factor α-Converting Enzyme
214 The ADAMTS Endopeptidases
215 ADAMTS1
216 Procollagen N-Endopeptidase, ADAMTS2
217 Aggrecanases 1 and 2
218 ADAMTS13: Von Willebrand Factor-Cleaving Protease
219 ADAM10, Myelin-Associated Metalloendopeptidase
Other Families in Clan MA 220 Pappalysin-1 (Pregnancy-Associated Plasma Protein-A)
221 Immune Inhibitor A
222 IgA Protease of Clostridium Ramosum
223 Snapalysin
224 Leishmanolysin
225 BlaR1 and MecR1 Gene Products of Staphylococcus Aureus
226 IgA-Specific Metalloendopeptidase
227 Carboxypeptidase Taq
228 Archaean Thermostable Carboxypeptidases
229 Anthrax Lethal Factor
230 Penicillolysin
231 Deuterolysin
232 Peptidyl-Lys Metalloendopeptidase
233 Fungalysin
234 FtsH Protease
235 Mitochondrial m- and i-AAA Proteases
236 Paraplegin
237 FtsH Homolog in Chloroplasts
238 Cytophagalysin
239 Dipeptidyl-Peptidase III
Clan MC
240 Carboxypeptidase A
241 Carboxypeptidase A2
242 Carboxypeptidase U
243 Mast Cell Carboxypeptidase
244 Carboxypeptidase B
245 Carboxypeptidase MeCPA
246 Carboxypeptidase T
247 Lysine Carboxypeptidase
248 Carboxypeptidase E
249 Carboxypeptidase Z
250 Adipocyte-Enhancer Binding Unit 1
251 Metallocarboxypeptidase D
252 Carboxypeptidase M
253 y-D-Glutamyl-(L)-Meso-Diaminopimelate Peptidase I
Clan MD
254 Zinc D-Ala-D-Ala Carboxypeptidase (Streptomyces)
255 D-Ala-D-Ala Carboxypeptidase VanY
256 VanX D-,D-Dipeptidase
257 N-Acetylmuramoyl-L-Alanine Amidase
Clan ME
258 Pitrilysin
259 Insulysin
260 Nardilysin
261 Axllp Gene Product (Saccharomyces Cerevisiae)
262 Mitochondrial Processing Peptidase
263 Chloroplast Stromal Processing Peptidase
264 Metalloprotease 1
265 Falcilysin
266 Vaccinia Virus Metalloproteinase
Clan MF
267 Leucyl Aminopeptidase (Animal)
268 Leucyl Aminopeptidase (Plant)
269 Leucyl Aminopeptidase PepA
270 Peptidase B (Escherichia Coli)
Clan MG
271 Methionyl Aminopeptidase Type 1
272 Methionyl Aminopeptidase Type 2
273 X-Pro Dipeptidase (Bacteria)
274 X-Pro Dipeptidase (Eukaryotes)
275 X-Pro Dipeptidase (Archaea)
276 X-Pro Aminopeptidase (Prokaryote)
277 X-Pro Aminopeptidase (Lactococcus)
278 Aminopeptidase P1
279 Aminopeptidase P2
Clan MH
280 Aspartyl Aminopeptidase
281 Aminopeptidase I
282 Glutamate Carboxypeptidase
283 Peptidase T
284 Peptidase V
285 Gly-X Carboxypeptidase
286 X-His Dipeptidase (Bacteria)
287 Sulfolobus Carboxypeptidase
288 Aminopeptidase Y
289 Streptomyces Griseus Aminopeptidase
290 Glutamate Carboxypeptidase II
291 Vibrio Aminopeptidase
292 Glutamyl Aminopeptidase (Lactococcus)
293 Bacillus Aminopeptidase I
294 N-Terminal Deblocking Aminopeptidase (Pyrococcus Furiosus)
Other Clans of Metallopeptidases
295 IadA β-Aspartyl Dipeptidase
296 O-Sialoglycoprotein Endopeptidase
297 Hydrogenase Maturation Endopeptidase
298 Endopeptidase GPR
299 S2P Protease
300 Sporulation Factor SpoIVFB
301 D-Aminopeptidase DppA
302 Membrane Dipeptidase
303 Dipeptidase AC (Acinetobacter)
304 β-Lytic Metalloendopeptidase
305 Staphylolysin
306 Lysostaphin
307 Aminopeptidase T
308 PepS Gene Product (Streptococcus Thermophilus)
Metallopeptidases not Yet Assigned to Families
309 Tripeptide Aminopeptidase
310 Clostridial Aminopeptidase
311 X-Trp Aminopeptidase
312 Tryptophanyl Aminopeptidase
313 Aminopeptidase yscCo-II
314 X-Arg Dipeptidase
315 Met-X Dipeptidase
316 Cytosol Nonspecific Dipeptidase
317 X-His Dipeptidase
318 β-Ala-His Dipeptidase
319 Lysosomal Dipeptidase
320 Peptidyl-Dipeptidase B
321 Peptidyl-Dipeptidase (Streptomyces)
322 Alanine Carboxypeptidase
323 Membrane Pro-X Carboxypeptidase
324 Carboxypeptidase G3
325 Mitochondrial Carboxypeptidase
326 Peptidyl-Asp Metalloendopeptidase
327 Magnolysin
328 Dactylysin
329 Myxococcus Xanthus Metalloendopeptidase
330 Dynorphin-Converting Enzyme
Appendix 1 Organisms Mentioned in the Handbook
Appendix 2 Suppliers Cited in the Handbook
Index
- No. of pages: 984
- Language: English
- Edition: 2
- Published: May 17, 2004
- Imprint: Academic Press
- Paperback ISBN: 9780124121058
- eBook ISBN: 9780080984155
AB
Alan J. Barrett
Affiliations and expertise
Wellcome Trust Sanger Institute, Cambridge, U.K.JW
J. Fred Woessner
Affiliations and expertise
University of Miami, Florida, U.S.A.NR
Neil D. Rawlings
Currently Dr. Neil Rawlings is a Senior Scientist in the Proteins Department at the EMBL-European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, Cambridgeshire, UK. Dr. Rawlings has been an active researcher at the Wellcome Trust Sanger Institute for over twenty years. He is extremely well known in the proteolytic enzyme community for his work curating the MEROPS database, an information resource covering peptidases and the proteins that inhibit them, which is used by expert researchers and students worldwide. Dr. Rawlings has published widely in such peer reviewed journals as Genome Research, BMC Bioinformatics, PloS ONE, Nucleic Acids Research, the Journal of Biological Chemistry, and Science.
Affiliations and expertise
Senior Scientist, Proteins Department, EMBL-European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, Cambridgeshire, UK