🩷 3.1.4.2 Many proteins are enzymes Flashcards
(24 cards)
What are enzymes?
It is a protein which is a biological catalysts which lower the activation energy of the reaction it catalyses
What is the induced fit model ?
- The enzymes active site and the substrate are not initially complementary
- The active site moulds around the substrate, becoming complimentary and putting pressure on the substrates bonds
- The bonds bend and break causing the activation energy of the enzyme to reduce
- Enzyme-substrate complexes are formed
What is the lock and key model?
The enzyme active site is initially complementary to the substrate. They bind and form enzyme-substrate complexes.
Define active site
The area on the enzyme to which the substrate binds. The active site is only complementary to one substrate. When they bind they form enzyme substrate complexes
Define enzyme substrate complexes
These form due to successful collisions between enzymes and substrates
Define kinetic energy
This is the movement energy conferred to particles due to temperature
Define successful collisions
Collisions which result in enzyme substrate complexes forming
Define complementary shape
When the shape of the substrate allows it to fit into the shape of the enzymes active site
Define tertiary structure
This defines the shape of the active site
Define specific shape
The shape of both the substrate and the enzyme are specific to each other so that no other substrate can bind
Define similar shape
Used to describe the relationship between competitive inhibitors and substrates
What are the four factors affecting rate of reaction?
- temperature
- concentration of substrate
- concentration of enzyme
- ph
Describe what would happen on a graph when temperature changes
When temperature increases, between … and … rate of reaction increases until optimum temperature. Final temperatures between … and … rate of reaction decreases
Explain what would happen when temperature changes on a graph
- As temperature increases rate of reaction increases due to the increase in kinetic energy of the molecules
- This means that there are more successful collisions so more enzyme substrate complexes are formed up until the optimum temperature
- After this point, the enzymes denature and bonds break, causing the tertiary structure to change
- The active site is no longer complementary to that of the substrate so no more enzyme substrate complexes are formed
Describe what would happen on a graph when ph changes
As ph increases between … and … rate of reaction increases. After the optimum ph … rate of reaction decreases
Explain what would happen when ph changes on a graph
- At low Ph there is a high concentration of hydrogen ions (H+) which are also known as protons.
- These break the hydrogen/ionic bonds causing the tertiary structure to change and making the active site no longer complementary to the substrate.
- This means that there are less enzyme substrate complexes formed
- After the optimum ph, as the ph increases the concentration of hydroxyl ions (OH) increases
- These also break the hydrogen/ionic bonds causing the same effect as the protons
Describe the effect of substrate concentration on graphs
As substrate concentration increases, the initial rate of reaction increases. The rate of reaction then plateus
Explain the effect of substrate concentration on a graph
- Initially the rate of reaction increases as the increase in substrate concentration causing as increases in the number of enzyme substrate complexes formed
- The rate of reaction then plateaus because enzymes become the limiting factor as all of there active sites have become saturated
Describe the effect of enzyme action on a graph
As enzyme concentration increases rate of reaction increases
Explain the effect of enzyme concentration on rate of reaction
- Increasing enzyme concentration increases the rate of reaction as more enzyme substrate complexes are formed however in reality, enzyme concentration would not exceed that of the substrate
Describe and explain the effect of a competitive inhibitor
- The competitive inhibitor and the substrate are a similar shape
- They can both (separately) bind to the enzymes active site and compete to do so
- The higher the concentration of the competitive inhibitor, the fewer enzyme substrate complexes formed
Describe and explain the effect of a non competitive inhibitor
- The non competitive inhibitor binds to the enzyme away from the active site
- This changes the shape of the active site as it changes its tertiary structure
- The substrate is no longer complementary to the active site so no enzyme substrate complexes can be formed
On a graph with competitive inhibitor, non competitive inhibitor and normal enzyme, which inhibitor would catch up to the normal enzyme with increasing substrate?
Competitive inhibitor
Which inhibitor cannot be overcome by increasing substrate concentration and why?
Non competitive inhibitor due to it causing a change in the shape of the active site