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Handbook of Proteolytic Enzymes. Serine and Threonine Peptidases. Edition No. 4

  • Book

  • March 2024
  • Elsevier Science and Technology
  • ID: 5894655
The Handbook of Proteolytic Enzymes, Fourth Edition is the latest release in this esteemed publication that stands as the most comprehensive work in applied enzymology and biocatalysis since the first edition published in 1998. Extensively updated, the new edition is an essential reference for biochemists, biotechnologists, and molecular biologists across academia and industry. Edited by world-renowned experts in the field, and with five volumes available for individual sale, this work provides detailed information on all known proteolytic enzymes researched to-date, with expanded coverage of metallopeptidases, cysteine peptidases, serine and threonine peptidases, aspartic and glutamic peptidases, and inhibitors of proteolytic enzymes.

This volume includes over 400 chapters on known serine and threonine peptidases, including their name, history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing features, with 2D and 3D structures of peptidases in color, extensive references, and links to PubMed and MEROPS databases.

Table of Contents

SERINE AND THREONINE PEPTIDASES (Volume 2)

New chapters Transmembrane peptidase, serine 4 Mesotrypsin Kallikrein-related peptidase 6 Arginyl peptidase HtrA peptidase (Helicobacter) HtrA peptidase (Borrelia burgdorferi) Zika virus NS2B-NS3 peptidase Keratinase K1 (Stenotrophomonas maltophilia) Mycosin-1 Dipeptidylpeptidase homologue DPP6 ClpP1 peptidase (Streptomyces) ClpP2 peptidase (Streptomyces)

Major revisions Chymotrypsin A (cattle-type) Granzyme B (Homo sapiens-type) Tryptase beta Kallikrein-related peptidase 3 Kallikrein-related peptidase 5 Kallikrein-related peptidase 7 Corin Factor VII-activating peptidase Trypsin 1 Cationic trypsin (Homo sapiens-type) Elastase-2 Cathepsin G Myeloblastin Chymase (Homo sapiens-type) Prostasin Mesotrypsin Coagulation factor VIIa Coagulation factor IXa Coagulation factor Xa Coagulation factor XIa Coagulation factor XIIa Thrombin Plasma kallikrein Urokinase-type plasminogen activator t-Plasminogen activator Plasmin Hepsin Epitheliasin Matriptase Matriptase-2 HtrA1 peptidase (Homo sapiens-type) HtrA2 peptidase Flavivirin Hepacivirin Bacterial proteasome, beta component Proteasome subunit beta1c Proteasome subunit beta2c Proteasome subunit beta5c Proteasome subunit beta1i Proteasome subunit beta5i Taspase-1 Subtilisin Carlsberg PfSUB1 peptidase PCSK1 peptidase PCSK9 peptidase Site-1 peptidase Furin Tripeptidyl-peptidase I Prolyl oligopeptidase Dipeptidyl-peptidase IV (eukaryote) Fibroblast activation protein alpha subunit Dipeptidyl-peptidase 9 Serine carboxypeptidase A Lysosomal Pro-Xaa carboxypeptidase Signal peptidase I Lon-A peptidase PIM1 peptidase Peptidase Clp (type 1)

Authors

Neil D. Rawlings Senior Scientist, Proteins Department, EMBL-European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, Cambridgeshire, UK. 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.