Michaelis Menten Kinetics Flashcards

1
Q

Why is kinetics needed

A
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2
Q

Draw a Michaelis menten plot

A
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3
Q

What does the Michaelis menten equation assume

A

Also assumes that the reverse reaction( [ES]→ [E]+[S] (k-1) ) can be neglected

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4
Q

What is the expression for the disocciation constant

A
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5
Q

Recall the Michaelis menten equation

A
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6
Q

derive the Michaelis menten equation for initial velocity from the expression for the dissociation constant

A
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7
Q

what is the steady state assumption and draw the graph for it *

A

intermediate species in a reaction mechanism remains constant over the time course of the reaction, even though the reactants and products are changing. This means that the rate of formation of the intermediate is equal to the rate of its consumption
Intermediate = ES

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8
Q

recall the equation for the Michaelis menten constant involving rate constants

A
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9
Q

how do you find initial velocity of a reaction using the Michaelis menten constant

A
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10
Q

Explain what the Michaelis menten equation shows and how Vmax and Km are obtained from a Michaelis menten plot

A
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11
Q

What does Km tell you

A

The affinity of the enzyme for the substrate

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12
Q

What does it mean if [Substrate]<Km

A
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13
Q

What does it mean if [Substrate]>Km

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14
Q

What are the units of Km and velocity

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15
Q

What does it mean if an enzyme has a low Km

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16
Q

What factors affect Km

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17
Q

Write an expression relating Km and Ks

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18
Q

What is Km a measure of

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19
Q

What does a high Km mean

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20
Q

How does Km affect an individuals susceptibility to alcohol

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21
Q

What is kcat

A
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22
Q

How do you calculate initial velocity using kcat and Km

23
Q

What is kcat/Km used to measure

A

The greater the kcat/Km value, the more efficient the enzyme

24
Q

What are the uses of kcat/Km

25
Q

What is a catalytically perfect enzyme

A

Is when k2»k1
This means when the formation of [P] from the ES complex is fast compared to breakdown of ES complex back to enzyme and substrate

26
Q

What is a catalytically perfect enzyme limited by

27
Q

How do enzymes achieve catalytic perfection

28
Q

What does Michaelis- menten kinetics assume

29
Q

What does a Michaelis menten plot show

30
Q

What is the equation that is plotted on a lineweaver - burk plot

31
Q

Draw an example of a lineweaver - burk plot and recall the information you can obtain from it

32
Q

What are the disadvantages of using the lineweaver - burk plot to measure kinetic parameters

33
Q

Recall the equation used to produce a hofstee - eadie plot

34
Q

What information can you obtain from a hofstee -eadie plot and what is the disadvantage of using this plot to obtain kenetic parameters

35
Q

What equation is used to plot a Hanes - Woolf plot

36
Q

Draw an example of a Hanes - Woolf plot and what you can obtain from it

37
Q

Why is the hanes-woolf plot the most accurate out of the other plots discussed

38
Q

What’s an equation that can be used to calculate Vmax from kcat and total conc. of enzyme

39
Q

What is the principle of Michaelis- menten kinetics

A

Until the enzyme is fully saturated

40
Q

What is the modified version of the Michaelis-menten equation that includes k-1 (the backwards reaction)

A

This treats ES as an intermediate

41
Q

What is the equation for the haldane relationship

A

Km s and Km p are the Michaelis constants for the substrate and product, respectively.
Vmax f and Vmax r are the maximum velocities/ rate for the forward and backward reactions respectively

42
Q

What does the haldane relationship tell you

A

At equilibrium v=0

43
Q

What is the effect of pH on enzymes

44
Q

At acidic, basic and optimum pH what are the charges of the residues on the substrate and the active site

45
Q

According to Michaelis menten kinetics how do enzymes behave at different pHs*(watch vid)

46
Q

What are lonization constants used for*

A

Ionization constants are used to describe the extent to which a compound, typically an acid or base, dissociates or ionizes in a solvent, usually water

47
Q

What is the effect of temperature on enzymes

48
Q

What are bisubstrate reactions

49
Q

How are substrates characterised using cleland nomenclature

50
Q

What are the names of the mechanism for bisubstrate reactions and the subcategories

A

Sequential reactions and ping-pong reactions which can be subdivided into ordered and random

51
Q

What is a sequential reaction

52
Q

What is a ping-pong reaction

53
Q

What are ordered and random reactions

54
Q

Which enzyme doesn’t follow Michaelis - menten kinetics and why