Introduction to Enzymes - Oct 4th


  • Define rates equations and rate constants for 0-order, 1st, 2nd order elementary reaction steps
  • Describe reaction coordinate diagram for a catalyzed vs uncatalyzed reaction
    • Use reaction coordinate diagram to describe rate enhancement and rate determining step in enzyme catalysis
  • Classification of Enzymes
  • Describe how enzymes mediate catalysis
    • Transition-state stabilization
      • General acid-base catalysis
  • Describe molecular recognition between enzyme and substrate or transition state
    • Intermolecular forces
    • Hydrophobic Effect
    • Transition-state stabilization
  • Articulate why the shape of enzymes actives sites more precisely complement the transtion state rather than the substrate

Reading (to be completed before class!)

Lehninger Chp 6, Sect. 6.1-6.3 (page 201)

  • Know and understand all terms in bold
  • Table 6-3 (memorize)
  • Be able to label and define terms in figure 6.3
  • Know residues (Fig 6-9) that can act in general acid-base catalysts
  • Define initial velocity (Fig 6-10)
  • Understand the relationship between Fig 6-10 and Fig 6-11
  • Relate terms in M-M equation to Figure 6-12


No assignment. Instead complete Hb worksheet and bring questions to class

In Class Activities

  • PowerPoint
  • Worksheet