Specificity of Proteolysis presents a survey and conclusions on the action or proteinases - enzymes which are cleaving proteins or peptides. The specificity of proteinases which is determined as the sequence of amino acids at the cleavage site of a substrate, is an important criteria to choose an enzyme as tool in protein research. Whenever one is looking for an enzyme to act at a defined site or to give defined cleavage products one will find comprehensive information in this work. Comprehensive information about more than 280 endopeptidases which are based on the database LYSIS including a calculation program to determine cleavage sites, is given in the book.

1 Introduction

2 Nomenclature and Conventions
2.1 EC Numbers
2.2 Enzyme Names
2.3 Enzyme and Substrate Codes
2.4 Subsite Nomenclature
2.5 Bibliography
3 Data Treatment
3.1 Data Bank LYSIS
3.2 Statistical Approach to Specificity
4 Standard Polypeptide Substrates
4.1 Choice of Standard Polypeptides
4.2 Available Data on Cleavages of Insulin Chains and Glucagon
4.3 Repartition of Cleavage-Susceptible Bonds
4.4 Binding Sites - Proposal for Fixation Site Types
4.5 Influence of Subsites
5 Essential Substrate Residues for Action of Endopeptidases
5.1 Basic Residue
5.2 Acidic Residue
5.3 Neutral Residue
5.4 Proline Residue
5.5 Alpha-Epsilon Peptide Bond
5.6 Peptidases with Occasional Endopeptidase Activity
5.7 Vague or Insufficient Information on Specificity
5.8 No Information on Bond Specificity
6 Comments
6.1 Frequently Used Proteinases and Restriction Proteinases
6.2 Group of Microbial Proteinases
References
Appendices
A Tabular Index of LYSIS Enzyme Codes
B Tabular Index of LYSIS Protein Codes.