Enzymes

• enymes are tertiary structures
• induced fit model suggests the active site is flexible and the substrate forms weak hydrogen and ionic bonds so the enzyme molds and puts a strain on the bonds lowering enzyme activity
• anabolic enzymes carry out condensation reactions
• catabolic enzymes carry out hydrolysis
• temperature

  • when temp. is low there is not enough kinetic energy for successful collisions between the enzyme and the substrate
• temperature

  • if the temperature is too high the enzyme denatures and the active site changes because the bonds holding the amino acids in their fixed 3d tertiary structure breaks
• pH

  • too many H + ions or OH - ions that interfere with the charges in the amino acids and breaks bonds
• Substrate and enzyme concentration

  • insufficient substrate means theres fewer collisions so a slow reaction
  • insufficient enzymes means all the current active site is taken up so the rate of reaction is slow
• competitive inhibitors are the same shape as the substrate so fits in the active site blocking substrates from fitting in. a higher concentration of substrates will knock of inhibitors
• non-competitive inhibitors bind at allosteric sites, when it binds it slightly changes the shape of the active site
• how does the active site of an enzyme cause a high rate of reaction?

  • lowering activation energy
  • induced fit causes the active site to shape
  • enzyme substrate complex causes bonds to break or form