Specificity of Proteolysis presents a survey and conclusionson the action or proteinases - enzymes which are cleavingproteins or peptides. The specificity of proteinases whichis determined as the sequence of amino acids at the cleavagesite of a substrate, is an important criteria to choose anenzyme as tool in protein research. Whenever one is lookingfor an enzyme to act at a defined site or to give definedcleavage products one will find comprehensive information inthis work.Comprehensive information about more than 280 endopeptidaseswhich are based on the database LYSIS including acalculation program to determine cleavage sites, is given inthe 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.