Study your flashcards anywhere!

Download the official Cram app for free >

  • Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off
Reading...
Front

How to study your flashcards.

Right/Left arrow keys: Navigate between flashcards.right arrow keyleft arrow key

Up/Down arrow keys: Flip the card between the front and back.down keyup key

H key: Show hint (3rd side).h key

A key: Read text to speech.a key

image

Play button

image

Play button

image

Progress

1/23

Click to flip

23 Cards in this Set

  • Front
  • Back
  • 3rd side (hint)
what must the value of ∆G be for a reaction to be spontaneous
negative
None
upon what does ∆G depend?
reactants and products, not pathway
None
how is ∆G related to rate of reaction?
∆G is never related to rate, only if reaction will go or not
None
what determines the rate of the reaction?
the pathway between reactants and products (activation energy)
if the concentration of substrate in a reaction is increased, what happens to the rate?
it increases
as the activation gets greater, what happens to the rate?
it decreases
what is often used to stabilize high-energy intermediates in reactions?
enzyme
what kind of bonds do enzymes form with the reaction intermediate?
non-covalent bonds
what is the name of the site in the enzyme in which the substrate binds?
active site
what is the shape of the graph when you graph the relationship of reaction velocity and substrate concentration
hyperbolic
what is the definition of Km?
substrate concentration at which velocity = 1/2 max velocity
what does a low Km value tell us about the enzyme-substrate relationship?
efficient enzyme, high enzyme affinity for substrate
what are the two major classes of enzyme inhibitors?
competitive and non-competitive
which enzyme inhibitors bind at the same site as the normal substrate?
competitive
what effect do competitive inhibitors have on Km? Vmax?
increases Km, no effect on Vmax
what effect do non-competitive inhibitors have on Km? Vmax?
reduces Vmax, no change in Km
what does Ki measure?
affinity of inhibitor for substrate
for a competitive inhibitor, when the concentration of inhibitor equals Ki, what is the relationship between substrate and Vmax?
it take 2x as much substrate to reach Vmax/2, or Km is doubled
for a non-competitive inhibitor, when the concentration of the inhibitor equals Ki, what is the relationship between velocity and substrate?
velocity is reduced by factor of 2 at every substrate concentration
what is the relationship of ∆G for forward and backwards reactions?
∆G has the same magnitude and opposite sign for reversible reactions
None
how are ∆G values combined for coupled reactions?
additive
None
does standard free Energy depend on concentration or reactants and temperature of reaction?
no, it is independent of those factors. It is specific to reactants and products
can more than two reactions be coupled at once?
yes.