Part II: Enzymes
Biological Catalysis
Enzymes are nature's catalysts, accelerating biochemical reactions by factors of 10⁶ to 10¹⁷ while maintaining exquisite specificity. Understanding enzyme mechanisms, kinetics (Michaelis–Menten theory), inhibition strategies, and allosteric regulation is central to biochemistry, pharmacology, and biotechnology. This part develops the quantitative framework for analyzing enzyme behavior.
10¹⁷
Max Rate Enhancement
Kᵤ
Michaelis Constant
6 Classes
EC Classification
Topics in This Part
5. Enzyme Catalysis & Mechanisms
Transition state theory, activation energy lowering, acid–base and covalent catalysis, the serine protease mechanism
6. Enzyme Kinetics
Michaelis–Menten equation, Vᵤᴁᴝ, Kᵤ, kᴄᴁᴛ, Lineweaver–Burk plots, and multi-substrate kinetics
7. Enzyme Inhibition
Competitive, uncompetitive, noncompetitive, and mixed inhibition; Kᵢ determination; drug design applications
8. Allosteric Regulation & Cooperativity
MWC and KNF models, the Hill equation, feedback inhibition, covalent modification, and zymogens