8: Enzyme Regulation
( \newcommand{\kernel}{\mathrm{null}\,}\)
- 8.1: Regulation of Enzyme Activity
- Enzymes can be slowed down or even prevented from catalyzing reactions in many ways including preventing the substrate from entering the active site or preventing the enzyme from altering conformation to catalyze the reaction. The inhibitors that do this can do so either reversibly or irreversibly. The irreversible inhibitors are also called inactivators, and reversible inhibitors are generally grouped into two basic types: competitive and non-competitive.
- 8.2: Mechanisms of Catalysis
- Enzymes accelerate reactions by stabilizing transition states and optimizing electronic environments for catalysis. Serine proteases, such as chymotrypsin, cleave peptide bonds through a well-defined catalytic mechanism and exhibit substrate specificity. Other proteases, including caspases, play essential roles in apoptosis. Protease inhibitors regulate enzyme activity and have medical applications.
- 8.3: Control of Enzymatic Activity
- Enzyme activity is tightly regulated to maintain homeostasis and respond to internal and external signals. Inhibition mechanisms include competitive, non-competitive, uncompetitive, and irreversible (suicide) inhibition, each affecting substrate binding and enzyme activity differently. Allosteric regulation and feedback inhibition fine-tune enzyme function, with models explaining conformational changes and complex formation.
