Please enable JavaScript.

Coggle requires JavaScript to display documents.

BIOCATALYSIS - Coggle Diagram

- - - - Reversible inhibitors
        
        Competitive inhibitors
        
        Non-competitive inhibitors
      - Irreversible inhibitors
  - - - Transferases
        
        Catalyze the transfer of functional group
      - Oxidoreductases
        
        Catalyze biological redox reaction
      - Hydrolases
        
        Catalyze the hydrolysis of substrate (add water)
      - Isomerases
        
        Catalyze the rearrangement of functional group within a substrate molecule
      - Lyases
        
        Catalyze certain reaction which double bonds form or break
      - Ligases
        
        Catalyze reaction which new chemical bonds are formed between substrate molecule (use ATP)
  - - - Lock & key
      - Induced fit
        
        ~ The active site is flexible or not exactly complementary to the substrate
        
        Enzyme collides with substrate
        
        Substrate bind to the active site
        
        The binding induces a slight change in the active site of enzyme, allowing the substrate to fit to the enzyme precisely
        
        Active site become fully complementary with substrate to form enzyme-substrate (ES) complex
        
        Reaction takes place and converts the substrate to the product(s) to form enzyme-product (EP) complex
        
        The shapes of enzyme and products do not complement, the products are released from its enzyme
        
        Active site of enzyme return back to original conformation
        
        Enzyme ready to bind with another substrate
    - - ~ Bringing substrate molecules come together in correct orientation
      - Facilitates breakage / formation bonds
  - - - Metal ion activators
        (e.g. Mg2+)
      - Coenzyme (e.g. NAD+)
      - Prosthetic group (e.g. haem group)