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This document delves into the fundamentals of enzyme catalysis, focusing on the catalytic mechanisms of RNase and serine proteases. It includes average activity data, standard deviations, and detailed figures illustrating important nucleophiles and electrophiles. The content spans various tables and figures from Chapter 11, providing visual representations of enzyme action, alongside a concise analysis of serine proteases, highlighting their evolutionary significance and mechanistic details. Refer to pages 325 to 522 for comprehensive information.
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Average = 112.4 = C+ Standard deviation = 16 A = 131+ B- = 113-117 A- = 126-130 C+ = 109-112 B+ = 122-125 C = 96-105 B= 118-121 C- = 85-95
Enzyme Catalysis Chapter 11
Figure 11-12 Biologically Important Nucleophiles and Electrophiles
Figure 11-9 RNase S complexed with a nonhydrolyzable substrate.
We’re going to skip section 4 in Chapter 11 on lysozyme and continue with section 5: Serine Proteases
Figure 11-29 Catalytic mechanism ofthe serine proteases. Page 522
Figure 15-22 Relative positions of the active site residues in subtilisin, chymotrypsin, serine carboxypeptidase II, and ClpP protease. Page 521
Example of “convergent” evolution.
Figure 11-31 Trypsin and Bovine Pancreatic Trypsin Inhibitor