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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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