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Enzyme Fundamentals and Reaction-Rate Principles

Welcome to Enzyme Kinetics and Catalysis

Enzyme Classes, Active Sites and Catalytic Cycles

Knowledge Check: Enzyme Fundamentals

Michaelis–Menten Kinetics and Quantitative Analysis

Deriving the Michaelis–Menten Equation

Interpreting Km, Vmax, kcat and Catalytic Efficiency

Knowledge Check: Michaelis–Menten Analysis

Multi-Substrate Kinetics and Mechanistic Diagnosis

Bi-Bi Reactions: Sequential and Ping-Pong Mechanisms

Kinetic Plots, Global Fitting and Data Quality

Knowledge Check: Multi-Substrate Mechanisms

Reversible and Irreversible Enzyme Inhibition

Reversible Inhibition Models

Irreversible Inhibition and Time-Dependent Inactivation

Knowledge Check: Enzyme Inhibition

Chemical Strategies of Enzyme Catalysis

Transition-State Stabilization and Catalytic Power

Acid–Base, Covalent and Metal-Ion Catalysis

Knowledge Check: Catalytic Strategies

Catalytic Triads and Serine Protease Mechanisms

The Catalytic Triad: Serine, Histidine and Aspartate

Chymotrypsin: Acylation and Deacylation

Knowledge Check: Catalytic Triads

Allosteric Regulation and Cooperative Binding

Allostery, Cooperativity and the Hill Equation

MWC and KNF Models of Allostery

Knowledge Check: Allostery

Integrated Applications and Final Assessment

Enzyme Kinetics in Drug Discovery and Metabolic Regulation

Putting Kinetics, Chemistry and Allostery Together

Final Assessment: Kinetics, Catalysis and Allostery

An advanced course in quantitative enzyme kinetics, multi-substrate mechanisms, reversible and irreversible inhibition, catalytic chemistry, serine-protease catalytic triads, and cooperative allosteric regulation.

An advanced, mathematically grounded course in enzyme kinetics and catalytic strategy. Derive and interpret kinetic models, distinguish inhibition mechanisms, explain catalytic residue chemistry, and analyze cooperative allosteric regulation.

Enzyme Kinetics, Catalytic Mechanisms, and Allostery

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