Methods in Enzymology Vol.244 Proteolytic Enzymes Serine and Cysteine Peptidases

This chapter focuses on classification of peptidases. Three major criteria are used for the classification of the peptidases: (1) the reaction catalyzed; (2) the chemical nature of the catalytic site; and (3) the evolutionary relationship, as revealed by structure. The chapter describes how these criteria are used and presents their strengths and weaknesses. The sub-subclasses of peptidases fall into two sets: exopeptidases and endopeptidases. The exopeptidases act only near the ends of polypeptide chains. Those acting at a free N terminus liberate a single amino acid residue, a dipeptide, or a tripeptide. On the other hand, exopeptidases acting at a free C terminus liberate a single residue or a dipeptide. The oligopeptidases are a subset of the endopeptidases that are confined to action on oligopeptide or polypeptide substrates smaller than proteins, although the size ranges of the substrates differ between the individual enzymes. Synthetic substrates are considered increasingly important in both assay and characterization of peptidases. This is attributed to the discovery of convenient leaving groups and the recognition of the ability of dipeptide and tripeptide sequences to confer high sensitivity and selectivity on the substrates.

• Series: Methods in Enzymology (Book 244)
• Hardcover: 765 pages
• Publisher: Academic Press; 1 edition (November 22, 1994)
• Language: English
• ISBN-10: 0121821455
• ISBN-13: 978-0072971224
• Product Dimensions: 6 x 1.7 x 9 inches

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