BGM1002/L06 Enzymes II Flashcards
Name the 5 mechanisms of enzyme catalysis.
Proximity
Orientation
Strain/distortion
Acid-base catalysis
Covalent catalysis
Describe proximity in enzyme catalysis.
How closely packed substrate molecules are
Describe orientation in enzyme catalysis.
Ensuring substrates have the correct relative orientation
Describe strain/distortion in enzyme catalysis
Binding puts a strain on the bond making it easier for the reaction to occur
Describe acid-base catalysis in enzyme catalysis.
Protons are donated/accepted or hydroxyls generated
Overcomes very low concentrations of reactive molecules in environment
Describe covalent catalysis in enzyme catalysis.
Temporary covalent bond formation between enzymes and substrates
What does the interaction between enzyme and substrate depend on in terms of enzyme structure?
Specific 3D shape of active site
Hydrogen bonds
Name the 2 models for ligand interaction.
Lock and key
Induced fit
Describe the lock and key hypothesis.
Binding site of enzyme is complementary to substrate shape
Describe the induced fit hypothesis.
Contact between part of binding site and substrate induces a change in shape of active site and bind to substrate
What type of bond does the enzyme urease catalyse?
Esterase bond
What type of enzymes are in EC1?
Oxidoreductases
Oxidation/reduction reactions
What type of enzymes are in EC2?
Transferases
Transfer of one functional group from one substrate to another
What type of enzymes are in EC3?
Hydrolases
Formation of two products from one substrate by hydrolysis
What type of enzymes are in EC4?
Lyases
Non-hydrolytic addition/removal of groups/ cleavage of bonds
