Please enable JavaScript.

Coggle requires JavaScript to display documents.

Chapter 6B: Enzymes - Coggle Diagram

- - - - INACTIVATING the oxygen radicals is very important
        
        oxygen radical is acted on by superoxide dismutase
        
        hydrogen peroxide is acted on by catalase
        
        water and oxygen
  - - - catalyzed reaction has a LOWER activation energy than an uncatalyzed reaction
- - - - allostery: change something else on the protein (not directly on active site)
        
        activation: modulator binds to 1 region of protein and turns on protein
- - - - interactions between aa side chains (positive charge) and oxygen (negative) position the substrate inside the catalase active site
    - - consistent product specificity
  - - - diffraction pattern predicts the electron density in protein
  - - - drive specific binding - the ring of the substrate is very hydrophobic
    - - important for shape of active site
      - secondary structure side chains project AWAY from the face of the secondary structure
        
        point side chains into middle of active site so they can interact specifically with this molecule
    - - hydrogen bonding with OH- GROUP
        
        the correct substrate has an OH- group at a specific place to bind to enzyme specifically
- - - - interactions between enzyme and substrate stabilizes the transition state and decreases the activation energy
- - - - changing activation energy is about changing the microenvironment (the context)