Enzymes are the catalysts that make the chemical reactions of life happen fast enough to sustain it, and this course explains how they work and how their activity is measured and controlled. You'll start with the basics of catalysis, the induced-fit model, and the stepwise mechanism of serine proteases. The course covers allosteric enzymes and the classification of enzymes into their six traditional functional classes, then examines how enzymes are inhibited – competitively, non-competitively, uncompetitively, and irreversibly through suicide inhibition – and how each inhibition type changes an enzyme's kinetic plots. These concepts recur throughout the rest of the program, since drug mechanisms and metabolic regulation are both, at their core, questions of enzyme kinetics.

Enzymes and Enzyme Kinetics

Enzymes and Enzyme Kinetics
This course is part of Biochemistry for Science & Health Careers Specialization

Instructor: Kevin Ahern, PhD
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What you'll learn
Explain enzyme catalysis, including the induced-fit model and serine protease mechanisms
Apply Michaelis-Menten kinetics and interpret Lineweaver-Burk plots
Classify enzymes into their six traditional functional classes and describe allosteric regulation
Compare competitive, non-competitive, uncompetitive, and irreversible enzyme inhibition
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September 2026
18 assignments
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