Chemistry of proteolysis
Proteolysis is the enzymatic hydrolysis of the amide bond in peptides and proteins. This book describes the chemical process step-by-step whereas the structure and properties of the proteases (for about 600 enzymes) and their substrates are considered. It offers data on the regularities of the homogeneous catalysis and models of proteases, phenomenological aspects of the enzymatic hydrolysis (kinetics, specificity, enzyme modification including the site-directed mutagenesis), and the regulation of proteolytic enzymes including the inhibitors of proteases. Description of the catalysis itself ranges from the formation of the enzyme-substrate complexes to the analysis of efficiency and specificity of the proteases. With more than 3,000 references this book provides a complete overview of the relevant literature.
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Nonenzymatic Hydrolysis Models
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Acad Sci USA active site acyl acylenzyme amide bond amide group amide hydrolases amino acid amino acid residues Antonov VK Arch Biochem Biophys aspartic proteases atom Bender ML Biochem Biophys Res Biochemistry Biochemistry 23 Biochim Biophys Acta Biokhimiya Biol Chem 264 Biophys Res Commun Bovine carbonyl carbon carboxyl group carboxypeptidase catalysis catalytically active Cathepsin Chem Soc chemical chymotrypsin cleavable bond cleavage compounds concentration deacylation dependence effect elastase enzyme enzyme-substrate complex equilibrium ester fccat FEBS Lett free energy G G G hydrogen bond hydrolysis hydrolyzed hydrophobic hydroxyl imidazole inhibition inhibitors interactions kcal/mol kinetic leaving group mechanism Meth Enzymol 45B Mol Biol Mol Biologia Natl Acad Sci Neurath H nucleophilic papain pepsin peptidase peptide Proc Natl Acad protein Proteinase proton proton transfer rate constant Sect serine proteases side chain specificity stabilization structure substrate subtilisin Table tetrahedral intermediate thermolysin transition trypsin uman