1.4.2 Enzymes Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

What are enzymes?

A

Enzymes are biological catalysts that increase the rate of reaction by lowering the activation energy of the reaction they catalyse

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

How do enzymes lower activation energy?

A

Specific tertiary structure determines shape of active site, complementary to a specific substrate
Formation of enzyme-substrate (ES) complexes lowers activation energy of metabolic reactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are enzymes made up of?

A

Enzymes are 3D tertiary structured globular proteins whose shape is determined by the primary sequence of amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Describe the active site of an enzyme

A

The active site is an area of the enzyme that is made up of only a few amino acids and forms a small depression in the overall enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Describe the substrate

A

The substrate is the part of the molecule that the enzyme acts upon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Explain the induced it model of enzyme action

A
  • Shape of active site is not directly complementary to substrate and is flexible
  • Conformational change enables ES complexes to form
  • This puts strain on substrate bonds, lowering activation energy
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

How have models of enzyme action changed?

A
  • Initially lock and key model: rigid shape of active site complementary to only 1 substrate
  • Currently induced fit model: also explains why binding at allosteric sites can change shape of active site
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

How could a student identify the activation energy of a metabolic reaction from an energy level diagram?

A

Difference between free energy of substrate and peak of curve

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Name the 5 factors that affect the rate of enzyme-controlled reactions

A
  1. Enzyme concentration
  2. Substrate concentration
  3. Concentration of inhibitors
  4. pH
  5. Temperature
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

How does substrate concentration affect rate of reaction?

A

As concentration of substrate increases, rate of reaction increases as more ES complexes are formed
Beyond a certain point, the rate of reaction no longer increases as enzyme concentration becomes the limiting factor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

How does enzyme concentration affect rate of reaction?

A

The rate of reaction increases as enzyme concentration increases as there are more active sites for substrates to bind to
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 factor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

How does temperature affect the rate of reaction?

A

Rate of reaction increases up to the optimum temperature as the kinetic energy of the enzyme increases
Above the optimum temperature rate of reaction decreases beyond the optimum temperature as the enzyme becomes denatured

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

How does pH affect rate of reaction?

A

pH affects the enzymes shape as it can disrupt the bonds in the tertiary structure of the enzyme. Like temperature all enzymes work at different optimum pH’s

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Describe competitive inhibitors

A
  • Similar shape to substrate = bind to active site
  • Don’t stop reaction ; ES complex forms when inhibitor is released
  • Increasing substrate concentration decreases their effect
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Describe non-competitive inhibitors

A
  • Bind at allosteric binding site
  • May permanently stop reaction ; triggers active site to change shape
  • Increasing substrate concentration has no impact on their effect
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Outline how to calculate rate of reaction from a graph

A
  • Calculate gradient of line or gradient of tangent to a point
  • Initial rate: draw tangent at t=0
17
Q

Outline how to calculate rate of reaction from raw data

A

Change in concentration of product or reactant / time taken

18
Q

Why is it advantageous to calculate initial rate?

A

Represents maximum rate of reaction before concentration of reactants decreases and ‘end product inhibition’

19
Q

State the formula for pH

A

pH = -log10(H+)

20
Q

How do competitive inhibitors affect the rate of reaction?

A

As concentration of competitive inhibitors increase, rate of reaction decreases as active sites are temporarily blocked by inhibitors so substrates cannot bind to them

21
Q

How do non-competitive inhibitors affect the rate of reaction?

A

As concentration on non-competitive inhibitors increases, rate of reaction decreases as shape of the enzyme is altered by the inhibitors