Chemical Mechanisms in Enzyme Catalysis - Substrate-active site complementarity
4 important questions on Chemical Mechanisms in Enzyme Catalysis - Substrate-active site complementarity
What forces cause binding between enzyme and substrate?
- Hydrogen bonding
- Hydrophobic forces
- VDW interactions
- Electrostatic interachtons
They overcome energy that is needed to overcome the rotation freedom
What are the 5 things typical for the active site?
- Active site is small compared to the rest of the enzyme
- 3D structure, because it is made by tertiary structures
- The binding between substrate is non covalent
- Active side is in a cleft (aloof), so water is kept out.
- Binding is done because specific molecules bind to each other.
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What explains the substrate selectivity?
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