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Coursera

Enzymes and Enzyme Kinetics

via Coursera

Overview

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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.

Syllabus

  • Enzyme Catalysis
    • This module explains how enzymes accelerate biochemical reactions, from the induced-fit model of catalysis and the mechanism of serine proteases to the kinetic parameters described by the Michaelis-Menten equation.
  • Enzyme Classification
    • This module covers how enzyme kinetics are quantified and graphed, how allosteric enzymes shift between active and inactive conformations, and how enzymes are classified by their catalytic mechanisms and functional roles.
  • Enzyme Inhibitors
    • This module compares the major types of enzyme inhibition, showing how competitive, non-competitive, and uncompetitive inhibitors affect reaction kinetics differently from irreversible, mechanism-based inhibitors.

Taught by

Kevin Ahern, PhD

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