Enzymes Flashcards

1
Q

What is a chemical reaction?

A

Converting substrate into product
by breaking old bonds
forming new ones

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2
Q

What is activation energy?

A

Energy required to be put into the substrate in order to start it off

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3
Q

What is the transition state?

A

Point of maximum energy

have intermediate between substrate and product

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4
Q

How can the rate of a reaction be increased?

A

Increase temperature

Increase concentration

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5
Q

How does increasing temperature increase rate of reaction?

A

Molecules have more energy

more molecules with activation energy

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6
Q

How does increasing concentration increase rate of reaction?

A

More collisions between molecules

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7
Q

What are enzymes?

A

Biological catalysts

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8
Q

What do catalysts do?

A

Increase the rate of reaction

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9
Q

How do enzymes increase the rate of reaction?

A

Lower activation energy

Facilitate formation of transition state

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10
Q

How do enzymes lower the activation energy of chemical reactions?

A

Bring substrate molecules closer to each other
more likely to collide

Weaken the bonds in substrates
so less energy is required to break them

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11
Q

What is the active site of an enzyme?

A

Point where substrate binds

where the chemical reaction occurs

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12
Q

How much space of the enzyme does the active site take up?

A

Small amount

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13
Q

What is the function of the rest of the enzyme, other than the active site?

A

Act as a scaffold to form the active site

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14
Q

How are the amino acids that form the active site related to each other?

A

Active site is formed by amino acids at different points in the primary sequence
they come together by folding of the protein

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15
Q

What structure do most active sites form? Why?

A

Form clefts or crevices

to exclude water

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16
Q

How does the active site relate to the subtrate?

A

Active site has complementary shape to substrate

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17
Q

What is the lock and key hypothesis?

A

Substrate has completely complementary shape to active site

substrate fits into active site perfectly

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18
Q

What is the induced fit hypothesis?

A

Substrate has somewhat complementary shape to active site
binding of substrate to active site induces conformational change in active site
so that they fit together properly

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19
Q

How do substrates bind to active sites of enzymes? Why?

A

By multiple non-covalent bonds

binding must be weak

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20
Q

What are some examples of bonds that form between the substrate and active site?

A

Hydrogen bonds

Van der waals

Hydrophobic interactions

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21
Q

What shape would a graph of y axis-product against x axis-time look like? Describe the shape

A

Rectangular hyperbola

  • steep
  • flatter
  • completely flat
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22
Q

What does the gradient of a graph of y axis-product against x axis-time measure?

A

Measures the rate of reaction

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23
Q

Why does a graph of y axis-product against x axis-time take a hyperbolic shape?

A

Initially, lots of substrate molecules so have high rate of reaction

Then fewer substrate molecules, reduced rate of reaction

Then no substrate molecules, reaction stops

24
Q

Why does more substrate molecules means an increased rate of reaction?

A

More likely to collide with each other

form more product

25
What is another term for rate of reaction? What is its symbol?
Reaction velocity, V
26
What is V0?
The reaction velocity at time 0s
27
How does temperature affect the rate of an enzyme-controlled reaction?
Initially, as temperature increases so does rate of reaction but after optimum temperature, it decreases
28
What is the optimum temperature?
Temperature that gives maximum enzyme activity and maximum rate of reaction
29
Why does the rate of an enzyme-controlled reaction decrease after the optimum temperature?
Enzyme denatures with high temperatures
30
What is enzyme denaturation?
Bonds in enzyme tertiary structure break enzyme loses its tertiary structure active site loses its 3D shape
31
What are the consequences of the active site losing its shape?
Substrate can no longer bind | reaction stops
32
How does pH affect the rate of an enzyme-controlled reaction?
Below or above optimum pH, rate of reaction decreases
33
Why does the rate of an enzyme-controlled reaction decrease above or below the optimum pH?
Enzymes denatures
34
What is the shape of a graph of y axis-reaction velocity against x axis-substrate concentration?
Rectangular hyperbola
35
How does low or high pH cause enzyme denaturation?
Affects ionisation state on amino acids | affects electrostatic interactions in tertiary structure
36
What is Vmax?
The maximum reaction velocity
37
How is Vmax drawn on a graph?
Horizontal line above end point of graph
38
What is happening with enzyme and substrate molecules at Vmax?
Enzyme active sites are saturated with substrate | cannot bind any more
39
What is the Michaelis Menten model?
E + S E-S -----> P
40
What is E-S?
Enzyme-substrate complex | is the intermediate between substrate and product
41
What does the Michaeles Menten equation predict?
That the graph of y axis-reaction velocity against x axis-substrate concentration will be rectangular hyperbola
42
What is Km?
Substrate concentration that gives half of Vmax
43
What do Km values measure?
Affinity of enzyme for its substrate
44
What does a low Km value mean? Why?
Enzyme has high affinitiy for substrate | because require lower concentration to reach Vmax/2
45
What does a high Km value mean? Why?
Enzyme has low affinity for substrate | because require higher concentration to reach Vmax/2
46
What do rates generally measure?
Amount per unit time
47
How is enzyme activity measured?
Amount of enzyme that produces 1micromole of product per minute under standardised conditions
48
How is measure of enzyme activity standardised?
Per litre Per gram of tissue
49
How does the rate of an enzyme-controlled reaction relate to enzyme concentration?
Rate of enzyme-controlled reaction is proportional to enzyme concentration
50
How does enzyme concentration affect rate of reaction and enzyme activity?
Rate of reaction changes with enzyme concentration Enzyme activity is not affected by enzyme concentration
51
What is the Lineweaver-Burk plot?
Converting the rectangular hyperbola of y axis-reaction velocity against x axis-substrate concentration into a linear graph
52
What are the x- and y-axes of the Lineweaver-burk plot?
x-axis is 1/substrate concentration y-axis is 1/reaction velocity
53
What is the advantage of the Lineweaver-burk plot over the rectangular hyperbola?
Can more easily measure Km and Vmax
54
How is Km measured from a Lineweaver-burk plot?
x-intercept is -1/Km
55
How is Vmax measured from a Lineweaver-burk plot?
y-intercept is 1/Vmax
56
What is the gradient of the Lineweaver-burk plot?
Km/Vmax