Many Proteins Are Enzymes (3.1.4.2) Flashcards
(10 cards)
1
Q
What is the activation energy?
A
- The energy required for a chemical reaction to take place
2
Q
What are enzymes?
A
- Proteins that act as biological catalysts
- They speed up chemical reactions by providing an alternative reaction pathway of lower activation energy, increasing the rate of reaction
3
Q
What is the lock and key hypothesis?
A
- Suggests that the enzyme’s active site has a specific, rigid shape that is complementary to its substrate
- Only substrates that perfectly fit the active site can bind and form an enzyme-substrate complex
4
Q
What is the induced fit model?
A
- Suggests that the active site of the enzyme is not initially complementary to the substrate, but it changes shape to better fit the substrate
- As the enzyme changes shape a strain is placed on bonds within the substrate molecule, forming an enzyme-substrate complex, thus lowering the activation energy
5
Q
What is the effect of enzyme concentration?
A
- The rate of reaction increases as the enzyme concentration increases as there are more active sites for the substrates to bind to
- However, increasing the enzyme concentration beyond a certain point has no effect on the rate of reaction as there are more active sites than substrates so substrate concentration becomes the limiting factpr
6
Q
What is the effect of substrate concentration?
A
- The rate of reactions increases as the substrate concentration increases as more enzyme-substrate complexes are formed
- However, increasing the substrate concentration beyond a certain point has no effect on the rate of reaction as all the active sites are occupied at one time so enzyme concentration becomes the limiting factor
7
Q
What is the effect of temperature?
A
- As the temperature increases, the rate of reaction rises, due to increased kinetic energy, resulting in more frequent collisions and more enzyme-substrate complexes are formed
8
Q
What is the effect of pH?
A
- Enzymes are only active over a narrow pH range. At lower or higher pHs than the optimum, denaturation can occur
- Changes in pH alter hydrogen and ionic bonds in the enzyme’s tertiary structure, altering the active site and preventing substrate binding
9
Q
What are competitive inhibitors?
A
- The inhibitor has a similar structure to the substrate
- Binds to active site
- Blocks the substrate from binding, preventing enzyme-substrate complexes from forming
- Reduces the rate of reaction
10
Q
What are non competitive inhibitors?
A
- Different shape to the substrate
- Attaches to the enzyme at a site other than the active site
- Changes tertiary structure of enzyme
- So active site and substrate no longer complementary so no substrate can bind