英语Chapter 9 Catalytic Strategies.pdfVIP

C H A P T E R 9 Catalytic Strategies Chess and enzymes have in common the use of strategy, consciously thought out in the game of chess and selected by evolution for the action of an enzyme. The three amino acid residues at the right, denoted by the white bonds, constitute a catalytic triad found in the active site of a class of enzymes that cleave peptide bonds. The substrate, represented by the molecule with the black bonds, is as hopelessly trapped as the king in the photograph of a chess match at the left and is sure to be cleaved. [Photograph courtesy of Wendie Berg.] hat are the sources of the catalytic power and specificity of enzymes? O U T L I N E WThis chapter presents the catalytic strategies used by four classes of enzymes: serine proteases, carbonic anhydrases, restriction endonucleases, 9.1 Proteases Facilitate a and myosins. Each class catalyzes reactions that require the addition of Fundamentally Difficult Reaction water to a substrate. The mechanisms of these enzymes have been revealed 9.2 Carbonic Anhydrases Make a Fast through the use of incisive experimental probes, including the techniques of Reaction Faster protein structure determination (Chapter 3) and site-directed mutagenesis (Chapter 5). The mechanisms illustrate many important principles of 9.3 Restriction Enzymes Catalyze catalysis. We shall see how these enzymes facilitate the formation of the Highly Specific DNA-Cleavage Reactions transition state through the use of binding energy and induced fit as well as classes of several specific catalytic strategies.