Chapter 1 Biological molecules - Enzymes (1.7-1.9) Flashcards
What are enzymes
Enzymes are tertiary structure proteins which catalyse and control chemical reactions in the body without being changed by the reaction
What is the active site
It’s a specific and unique shape due to the specific folding and bonding in the tertiary structure of the protein
How do enzymes speed up the reaction
When the enzymes attach to the substrate they lower the activation energy needed for the reaction to occur by providing an alternative reaction pathway with a lower activation energy and allow the reaction to proceed at body temperature and therefore speed up the reaction
What two models explain how enzymes react with substrates
Lock and key theory
Induced fit model
Explain the lock and key theory
The enzyme is the lock and the substrate is the key that fits into it due to their complimentary shape
This model suggests that the enzymes active site is a fixed shape and that due to the random collisions the substrate can collide and attach to the enzyme forming an enzyme substrate complex. And once the enzyme substrate complex has formed the charged groups within the active site will cause the substrate to distort in shape and lower the activation energy. The products are then released and the enzymes active site is empty and ready to be reused
Explain the induced fit model
- suggests that the enzyme active site is slightly different from the shape of the substrate at first
1) Substrate binds to the active site forming Enzyme-substrate complex
2) Active site changes shape so it is complementary to substrate putting strain and breaking bonds in the substrate
3) therefore lowers the activation energy as less energy is needed for the reaction to occur
4) The product are then removed and the enzyme active site returns to its original shape
Factors that affect enzyme action
- temperature
- pH
- substrate concentration
- enzyme concentration
- inhibitors
How does temperature affect enzymes
- if the temperature is too low there is not enough kinetic energy for successful collisions between the enzyme and substrate so fewer E-S complexes can form
- if the temperature is too high enzymes denature and enzyme substrate complexes cannot form as the hydrogen/ionic bonds are broken changing the shape of the teritiary structure and altering the specific shape of the active site, so it may no longer be complementary to the substrate so the enzymes cannot bind with the substrateso fewer E-S complexes can form
Explain the temperature graph on enzyme activity
1) the enzyme activity increases as the enzymes are gaining kinetic energy so there is a higher frequency of successful collisions between enzyme and substrate
2) the enzymes have reached their optimum temperature so enzyme activity has reached its maximum
3) the enzymes have denatured as its gone beyond its optimum temperature so enzyme activity decreases as the enzymes cannot bind to substrate and form enzyme substrate complex
How does pH affect enzyme activity
- as pH increases or decreases this causes the hydrogen/ionic bonds to break, causing the enzyme tertiary structure and active site to change shape
- so the active site is no longer complemenry to the substrate so fewer enzyme substrate complexes can form
How does substrate and enzyme concentration affect enzyme activity
- as substrate concentration increases the rate of reaction increases as at this point the substrate is limiting so more E-S complexes can form until the enzymes become saturated making the enzymes the limiting factor causing the rate of reaction to plateau
- as the enzyme concentration increase the rate of reaction increases as the increase in enzymes results in more active sites to become available until at a certain point the rate if reaction plateaus as the substrate becomes limiting as they all binded to the enzymes
How does substrate conc. affect inhibitorsand enzyme activity
Competitive inhibitors - adding more substrate will out compete the inhibitors, knocking them out of the active site increasing the rate of reaction (vice versa)
Non competitive inhibitors - substrate concentration has no affect on the enzyme activity as the inhibitors change the shape of the active site and enzyme
What are competitive inhibitions
This is when the inhibitor is a SIMULAR shape as the substrate and can bind to the active site. This prevents the substrate from binding and REDUCES THE AMOUNT OF ENZYME COMPLEXES from forming
What is non competitive inhibition
This is when the inhibitor binds to the enzyme away from the active site, the allosteric site, changing the tertiary structure of the enzyme this causes the active site to change shape so the substrate is no longer complimentary to the enzyme
Why is the Vmax the same as the Vmax without an inhibitor in competitive inhibitions
As when there is a high amount of substrate concentration the substrates out compete the inhibitors, knocking them off the active site so the substrate can bind with the enzyme returning the rate of reaction to normal