Handbook of Proteolytic Enzymes

by Alan J. Barrett (Editor), Neil D. Rawlings (Editor), J. Fred Woessner (Editor)

Overview

Extensively revised and updated, the new edition of the highly regarded Handbook of Proteolytic Enzymes is an essential reference for biochemists, biotechnologists and molecular biologists. Edited by world-renowned experts in the field, this comprehensive work provides detailed information on all known proteolytic enzymes to date. This two-volume set unveils new developments on proteolytic enzymes which are being investigatedin pharmaceutical research for such diseases as HIV, Hepatitis C, and the common cold. Volume I covers aspartic and metallo petidases while Volume II examines peptidases of cysteine, serine, threonine and unknown catalytic type. A CD-ROM accompanies the book containing fully searchable text, specialised scissile bond searches, 3-D color structures and much more.

• The only comprehensive book on proteolytic enzymes
• Includes 671 chapters, each written by experts in their field, on proteolytic enzymes from all groups of living organisms and the viruses, including those that are currently major targets of pharmaceutical research
• Accompanying CD-ROM provides fully searchable text, 2D structures of peptidases in color and links directly to PubMed and MEROPS databases
• Each chapter describes in detail the enzyme name, its history, activity and specificity, structural chemistry, preparation, biological aspects and distinguishing features
• Over 1000 peptidases included

Product Details

ISBN-13:	9780123822208
Publisher:	Elsevier Science
Publication date:	10/30/2012
Series:	Handbook of Proteolytic Enzymes, Two-Volume Set with CD-ROM
Sold by:	Barnes & Noble
Format:	eBook
Pages:	4094
File size:	90 MB
Note:	This product may take a few minutes to download.

About the Author

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.

Read an Excerpt

From Chapter 14: Enteropeptidase

Name and History Enteropeptidase was discovered in the laboratory of I.P. Pavlov, who was awarded the 1904 Nobel Prize in Medicine or Physiology for his studies of gastrointestinal physiology. Digestive enzymes within the pancreas were known to be inert compared to their potent activity within the intestine, but the basis of this difference was unknown. In 1899, Pavlov's student, N.P. Schepowalnikov, demonstrated that canine duodenal secretions dramatically stimulated the digestive activity of pancreatic enzymes, especially trypsinogen. The active principle in small intestine was heat labile and was attributed to a special enzyme in the intestine that could activate other enzymes ('a ferment of ferments'). Pavlov named it enterokinase (Schepowalnikov, 1900; Pavlov, 1902). Whether enterokinase was an enzyme or a cofactor remained controversial until Kunitz proved that the activation of trypsinogen by enterokinase was catalytic (Kunitz, 1939). In the 1950s, cattle trypsinogen was shown to be activated autocatalytically by cleavage of an N-terminal hexapeptide, Val-Asp-Asp-Asp-Asp-Lys6 Ile (Davie & Neurath, 1955) and enterokinase was shown to cleave the same bond (Yamashina, 1956). The more precise IUBMB name enteropeptidase has been in existence since 1970. However, the original name 'enterokinase' has a long history and remains in common use.

Activity and Specificity Enteropeptidase cleaves internal bonds of peptides and proteins at sites that closely resemble the activation cleavage site of cattle trypsinogen: Asp-Asp-Asp-Asp-Lys Ile. The (Asp)4-Lys activation peptide sequence is highly conserved among vertebrate trypsinogens (Bricteux-Gregoire et al., 1972). Most of the few exceptions have Glu instead of Asp at P2, P3 or P4; a minor rat trypsinogen has Arg at P1 and Asn at P3. Trypsinogens from some fish and from Xenopus laevis have Ile, Leu, Ala or Phe at P5. Limited data with small synthetic peptides indicate that cleavage requires two acidic residues at P2 and P3 in addition to Lys at P1; additional acidic residues at P4 and P5 markedly increased the affinity for enteropeptidase (Maroux et al., 1971; Light & Janska, 1989). In contrast to the stringent requirements for the P1-P5 positions, enteropeptidase shows little dependence on the structure of the peptide on the C-terminal side of the scissile bond (Maroux et al., 1971). This remarkable specificity has made enteropeptidase a useful reagent for the separation of recombinant fusion proteins that are joined by engineered enteropeptidase cleavage sites (Hopp et al., 1988).

Table of Contents

Aspartic Peptidases Introduction / Clan AA - Family A1 / Clan AA - Family A2 And Others / Other Clans of Aspartic Peptidases

Glutamic Peptidases

Asparragine Peptide Lyases

Metallopeptidases Introduction / Clan MA subclan E - Family M1 / Family M2 / Family M3 / Families M4,M5 and M9 / Family M13 / Other families in subclan MA(E) / Clan MA subclan M - Families M10 and M11 / Family M12 subfamily A / Other families in clan MA / Clan MC / Clan MD / Clan ME / Clan MF / Clan MG / Clan MM / Clan MO / Clan MP / Clan MH / Other clans of metallopeptidases / Metallopeptidases not yet assigned to clans

Cysteine Peptidases Introduction / Clan CA - Family C1 / Other families in clan CA / Clan CD / Clan CE / Clan PA subclan C / Other clans of cysteine peptidases / Cysteine peptidases not assigned to families

Serine and Threonine Peptidases Introduction / Clan PA subclan S - Family S1 / Other families in clan PA(S) / Clan SB - Family S8 / Family S53 / Clan SC - Family S9 / Other families in clan SC / Clan SE / Clan SF / Clan SH / Other clans of serine peptidases / Serine peptidases not assigned to family / Clan PB / Unsequenced serine peptidases / Peptidases of uncertain catalytic type

What People are Saying About This

From the Publisher

The one-stop resource for proteolytic enzymes

Editorial Reviews

5 Stars! from Doody

This handbook presents summary characterizations of over 500 proteolytic enzymes as described by as many contributors. It is edited by three giants in the field. It is meant to present practical information in terms of name, history, activity, specificity, structural chemistry, preparation, biological aspects, distinguishing features, and relevant references for each enzyme. Representative assay conditions are also included. The information will be very useful for students or experienced investigators who need a brief but useful summary of any type of known proteolytic enzyme. The information will be very useful to enzymologists also in terms of protein sequence comparisons with newly discovered enzymes or to molecular biologists in terms of determining whether newer DNA sequences harbor coding information on already-characterized or newer enzymes. The enzymes are presented not only according to the Enzyme Commission system for four mechanistic classes, but are further subdivided within each class to include clans and families, based on genetic relatedness. This latter classification previously developed by the editors also allows for expansion in the future. Referencing information to sequence data in the Swiss Protein database, and the PIR and EMBL cDNA and EMBL genomic DNA databases is also given. This book is highly recommended for anyone with an interest in proteolytic enzymes and is probably the only truly comprehensive handbook of this type available. It represents a massive effort by the editors and contributors and will likely be the primary source of such information in the future.

Gene A. Homandberg

Contains information on almost every known peptidase included in the current EC List. Also includes many that have not yet been included in the List, gene products that are shown by their amino acid sequences to be close relatives of known peptidases, and a few entities that show petidase-like activity. On the basis of primary and tertiary structures, entries are grouped into families and clans which are further grouped by catalytic mechanism, thus taking into account molecular structures and evolutionary relationships that are of importance but are not considered in the EC classification. The included CD-ROM contains the full text with a number of enhancements. Annotation c. by Book News, Inc., Portland, Or.

Booknews

Praise for the Second Edition: "The clear goal of these volumes is to provide complete coverage of proteases. All known enzymes of this class are described. As a reference, this is a very worthwhile contribution. The goals of this book are well met...The major strength of this book is the comprehensive coverage...An essential reference for scientific research...A very impressive offering…Any investigator with a protease question should start here." —Doody’s, 2005 "This handbook would be very useful a reference for a library that serves graduate and post-graduate researchers in molecular biology and related fields." —E-STREAMS, 2005

"A very impressive offering. While many of the chapters are short, they provide essential information as well as appropriate references. Any investigator with a protease question should start here." —Doody’s "The Handbook of Proteolytic Enzymes, Second Edition provides a structured and systematic, up-to-date account of the information about proteolytic enzymes...an indispensable reference for all researchers utilizing such enzymes in areas of organic chemistry, biochemistry, biotechnology and molecular biology." —Carbohydrate Polymers, April 2005

"This handbook would be a very useful reference for a library that serves graduate and post-graduate researchers in molecular biology and related fields. However, the CD-ROM version may be significantly more useful than the print version, especially for workers adept with bioinformatics." —Rafael Garcia, Chemical

From the Publisher