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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
eBook ISBN:9780080984155
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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Handbook 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
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
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