Outline
Introduction
Chemical Reaction Rates and the Effects of Catalysts
Reaction Rates and Reaction Order
First-Order Rates: The Rate Constant (Equations 11.1, 11.2, 11.3, 11.4a, 11.4b, Figure 11.1, Eqs. 11.5, 11.6a, 11.6b)
Second-Order Reactions (Equation 11.7)
Transition States and Reaction Rates (Figure 11.2, Eqs. 11.8, 11.9, 11.10, 11.11, Figure 11.3, Eqs. 11.12, 11.13)
What a Catalyst Does (Figure 11.4, Figure 11.5, Figure 11.6)
How Enzymes Act as Catalysts: Principles and Examples
General Principles: The Induced Fit Model (Figure 11.7, Figure 11.8, Reaction)
Triose Phosphate Isomerase (Reaction, Figure 11.9, Reaction, Reactions, Figure 11.10)
Serine Protease (Table 5.4, Figure 11.11, Figure 11.12, Figure 11.13)
The Kinetics of Enzymatic Catalysis
Reaction Rate for a Simple Enzyme-Catalyzed Reaction: Michaelis-Menten Kinetics
(Reaction, Eqs. 11.14, 11.15, 11.16, Figure 11.14, Eqs. 11.17, 11.18, 11.19, 11.20, 11.21, 11.22, 11.23, 11.24, Figure 11.15, Eqs. 11.25, 11.26)Expressing Reaction Rates for Multistep Reactions (Reaction, Equation 11.27)
The Significance of KM, kCAT, and kCAT/KM (Table 11.1, Eqs. 11.28, 11.29, Table 11.2)
Analysis of Kinetic Data: Testing the Michaelis-Menten Equation (Figure 11.16, eqs. 11.30a, 11.30b, 11.31, 11.32, 11.33, Figure 11.17)
Random Substrate Binding (Scheme #1, #2, #3, #4)
A Closer Look at Some Complex Reactions (Scheme, Eqs. 11.34, 11.35a, 11.35b, 11.35c, Figure 11.18, Table 11.3)
Competitive Inhibition (Figure 11.19, Scheme, Eqs. 11.36, 11.37a, 11.37b, Figure 11.20, Figure 11.21)
Noncompetitive Inhibition (Figure 11.22, Scheme, Eqs. 11.38, 11.39, Figure 11.23)
Coenzymes, Vitamins, and Essential Metals
Coenzymes and What They Do (Table 11.5, Structure, Figure 11.25, Figure 11.26)
Metal Ions in Enzymes (Figure 11.27)
The Diversity of Enzymatic Function
Classification of Protein Enzymes (Table 11.7)
1. Oxidoreductases catalyze oxidation-reduction reactions.
2. Transferases catalyze transfer of functional groups from one molecule to another.
3. Hydrolases catalyze hydrolytic cleavage
4. Lyases catalyze removal of a group from or addition of a group to a double bond, or other cleavages involving electron rearrangement.
5. Isomerases catalyze intramolecular rearrangement.
6. Ligases catalyze reactions in which two molecules are joined.Molecular Engineering of New and Modified Enzymes
Nonprotein Biocatalysts: Ribozymes (Figure 11.29, Figure 11.30)
The Regulation of Enzyme Activity: Allosteric Enzymes
Substrate-Level Control (Reaction)
Feedback Control (Scheme #1, #2, #3)
Aspartate Carbamoyltransferase: An Example of an Allosteric Enzyme (Figure 11.35, Figure 11.36, Figure 11.37, Figure 11.38)
Covalent Modifications to Regulate Enzyme Activity
Pancreatic Proteases: Activation by Cleavage (Figure 11.39, Figure 11.40)
A Further Look at Activation by Cleavage: Blood Clotting (Figure 11.42)