Basic Kinetics Tutorial

• The top depicts a graph of the Enzyme rate vs. [S]. There are two lines on the first graph here:
  • The black one is a reference graph whose Data (K_m and V_max) ALWAYS remain unchanged even as the scale on the graph changes.
  • The RED one is the one whose data that you manipulate with the sliders.
  • A relative scale of the graph is indicated at the top.
• The two bar graphs on the top right represent formation about the current conditions chosen
  • The panel at top right gives a bar graph representation of the current [S], [P], and enzyme rates as well as
  • the log of the final equilibrium position.
• The middle panel provides numerical representation of the same data.
  • units for the parameters
  • all concentrations ([S], [P], [E]) are in M/l (Molar)
  • k_cat = sec^-1
  • enzyme rates (v_max and v_o=Rate of [P]) = moles/sec (moles of product produced per sec)
  • K_m = Molar
  • k_cat/K_m = Molar sec
  • K_eq is unitless
• The bottom panel provides some interaction.

• Sliders on the bottom panel allow you to independently alter the [S], [P], [E], k_cat, K_m, V_max, k_cat/K_m, K_eq and the Hill coefficient independently to observe the effects.
• The Radio buttons on the right allow you to maintain the [P]= 0 or allow [P] to accumulate.

In the latter case you should observe that eventually the ratio of [S] and [P] will come to the same ratio as indicated in the "final equilibrium position" window. This final equilibrium position can be altered by changing the DG of the reaction.