Hydrolytic enzymes
Author(s)
Bibliographic Information
Hydrolytic enzymes
（New comprehensive biochemistry / general editors, A. Neuberger, L.L.M. van Deenen, v. 16）
Elsevier, 1987
Available at 49 libraries
Note
Includes bibliographical references and index
Description and Table of Contents
Description
This newest volume in the impressive New Comprehensive Biochemistry series presents up-to-date discussions of six types of hydrolytic enzyme that are well characterized structurally: aspartic-, cysteins-, and serine-proteinases, carboxypeptidase A, pancreatic ribonuclease A, and the phosphomonoesterases. The emphasis is on molecular mechanisms deduced by crystallographic, kinetic, spectroscopic and molecular genetic studies. The chapters on the various types of proteinases are complemented by others on proteinase inhibitors and intracellular proteolysis. This book will prove valuable to researchers in general biochemistry, particularly those with interest in enzyme mechanism and protein chemistry, and to Honours and Postgraduate students.
Table of Contents
Chapter 1. Aspartyl proteinases (J.S. Fruton). Molecular properties. Action on Protein Substrates. Action on Synthetic Substrates. Mechanism of Action. Chapter 2. Cysteine proteinases (K. Brocklehurst, F. Willenbrock and E. Salih). The Cysteine Proteinases: General Considerations. An Historical Perspective from Papaine to Calpain. Physiological and Pathological Aspects. Isolation and Assay. Molecular Structure. Specificity. Chemical Modification. Spectroscopic Studies. Kinetics and Catalytic Mechanism. Chapter 3. Structure and function of serine proteases (L. Polgar). The Pre-crystallographic Age. Structural Features of the Catalytic Mechanism. Beyond the Structure. Conclusion. Chapter 4. Carboxypeptidase A (D.S. Auld and B.L. Vallee). Structural Properties. Catalytic Properties. Chemical Modification of Active Site Residues. Structure-Function Studies by Site-Directed Mutagenesis. Function of the Metal. The Chromophoric Cobalt Atom as an Active Site Probe. Cryospectrokinetic Studies. Hydrolysis of Peptide Substrates. Rate Determining Step in Ester and Peptide Hydrolysis. Relationship to Other Metalloproteases. Summary. Chapter 5. Proteinase Inhibitors (Y. Birk). Distribution and Occurrence. Classification and Nomenclature. Mechanism of Action of Proteinase Inhibitors. Plant Proteinase Inhibitors. Proteinase Inhibitors of Animal Origin. Concluding Remarks. Chapter 6. Intracellular proteolysis (P. Bohley). Turnover of Proteins in Organelles. Cell Proteinases. Substrate Properties Determining Proteolysis in Cells. Regulation of Intracellular Proteolysis. Concluding Remarks. Chapter 7. Pancreatic Ribonuclease A: The most studied endoribonuclease (M.R. Eftink and R.L. Biltonen). Biological Function and Occurrence of RNases. Structure of RNase A. Thermodynamics of Ligand Binding to RNase A. Kinetics. Miscellaneous Topics. Specificity, Mechanism, and Energetics of Catalysis. Concluding Remarks. Chapter 8. Phosphomonoesterases (J.E. Coleman and M.J.A. Besman). Zinc Alkaline Phosphatases, Introduction. Alkaline Phosphatase from Escherichia coli. Mammalian Alkaline Phosphatase. Acid Phosphatase from Eukaryotes (Lysosomal). Manganese(III)-containing Violet Acid Phosphatases. Binuclear Iron-containing Purple Acid Phosphatases, Uteroferrins. (Each chapter is sub-divided into sections, including an introductory section, acknowledgements, and references)
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