Polymers of amino acids joined by peptide bonds. Has the same structure sequence as a protein
Induced fit model
The substrate and active site should have a complementary shape to collide and bind to form an enzyme-substrate complex. These, however, are not perfectly complementary. The active site will mold around the substrate to form a complementary fit.
Each enzyme is specific to the substrate(s)
Why do enzymes lower the activation energy?
Bringing substrates close together in the active site, preventing them repelling each other, so they bind more readily
Putting strain/tension on the substrate when it is in the active site, so its bonds break more readily
Factors affecting rate of enzyme activity
Temperature
pH
Substrateconcentration
Enzymeconcentration
If the shape of the active site of an enzyme changes, the rate of reaction will decrease. Substrates can no longer bind and enzyme-substrate complexes cannot form
Explain why rate of reaction increases with increasing collisions between enzymes and substrates?
More substrates bind with active sites
More E-S complexes
More products
Explain why changing the shape of the active site will decrease the rate of reaction?
Bonds break
active site denatures/loses its tertiary structure
shape no longer complementary to substrate
Fewer/no E-S complexes form
Competitive inhibitors
Inhibitor has a similar shape to the substrate, so will bind to the enzymes active site. This blocks the substrate, preventing it from binding, fewer enzyme substrate complexes are formed. The rate of reaction decreases
Non-competitive inhibitors
Binds to allosteric site of the enzyme, not the active site. The tertiary structure of the enzyme changes along with the active site. Substrates cant enter or bind to the enzyme so fewer E-S complexes form. Rate of reaction decreases
These inhibitors can also be used to make a non-complementary active site complementary to its substrate