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Cells to Systems > enzymes + enzyme kinetics > Flashcards

enzymes + enzyme kinetics Flashcards

1
Q

What is S⟶P?

A

from substrate to product

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2
Q

What is G‡?

A

free energy to overcome transition state

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3
Q

What is ∆G‡ₛ⟶ₚ?

A

energy to get from substrate to product

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4
Q

What is ∆G‡ₚ⟶ₛ?

A

energy to get from product to substrate

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5
Q

What is ∆G’ᵒ?

A

standard free energy

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6
Q

enzyme

A

a catalyst that lowers activation energy but is not used up in reaction

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7
Q

cofactor

A

an inorganic ion/coenzyme required for enzyme activity

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8
Q

What are the classes of enzyme classification?

A

1) oxidoreductases
2) transferases
3) hydrolases
4) lyases
5) isomerases
6) ligases

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9
Q

oxidoreductases

A

oxidation/reduction (transfer of electrons)

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10
Q

transferases

A

transfer of functional groups

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11
Q

hydrolases

A

breaking of single bonds through addition of water (hydrolytic cleavage)

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12
Q

Give an example of hydrolytic cleavage.

A

transfer of functional groups to water

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13
Q

lyases

A

breaking of bond(s) by means other than hydrolysis + oxidation, often forming a new double bond/ring structure

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14
Q

isomerases

A

rearrangement of groups (producing isoforms)

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15
Q

ligases

A

formation of new bond

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16
Q

zymogen

A

inactive form of enzyme

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17
Q

holoenzyme

A

apoenzyme + cofactor

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18
Q

lock-and-key

A

active site of unbound enzyme is complimentary to shape of substrate

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19
Q

induced fit

A

active site complimentary to shape of substrate only after substrate binds (enzyme changes shape when substrate binds)

20
Q

collagen

A

major structural components of connective tissues

21
Q

specificity

A

always cut in the same place

22
Q

SDS-PAGE

A

separates proteins based on their mass (lighter proteins travel further than heavier proteins)

23
Q

How can collagenolysis be assessed?

A

SDS-PAGE

24
Q

What are the factors affecting enzyme activity?

A

1) pH
2) temperature
3) [substrate]
4) presence of inhibitors

25
Q

How does pH affect enzyme activity?

A

pH outside optimum range will change conformation + may denature enzymes

26
Q

How does temperature affect enzyme activity?

A

1) affects kinetic energy of substrate + enzyme
2) determines frequency of substrate + enzyme interaction
3) increases rate of reaction until enzyme is saturated

27
Q

How does [substrate] affect enzyme activity?

A

1) determines frequency of substrate + enzyme interaction

2) increases rate of reaction until enzyme is saturated

28
Q

coenzyme

A

organic (non-metal) cofactor required for action of certain enzymes

29
Q

V₀

A

initial velocity

30
Q

Vₘₐₓ

A

maximum velocity of enzymatic reaction when binding site is saturated with substrate

31
Q

Kₘ

A

1) substrate concentration at which enzyme-catalysed reaction proceeds at 1/2 maximum velocity
2) inverse measure of substrate’s affinity for enzyme

32
Q

rate, v =

A

1) ∆[P]/∆t (product formation

2) -∆[S]/∆t (substrate depletion)

33
Q

ES

A

enzyme-substrate complex

34
Q

EP

A

enzyme-product complex

35
Q

What is the following equation simplified?

E + S ⇌ ES ⇌ EP ⇌ E + P

A

E + S ⇌ ES ➝ E + P

36
Q

Why is the initial velocity the maximum rate?

A

enzyme + substrate concentrations are at highest

37
Q

What is the relationship between {S] and rate?

A

as [S] increases, enzyme becomes saturated with substrate + rate reaches Vₘₐₓ

38
Q

Michaelis-Menten equation, V₀ =

A

Vₘₐₓ[S]/Kₘ + {S]

39
Q

reversible/irreversible inhibitors

A

depends on strength of bond between inhibitor + substrate

40
Q

What are the types of inhibitors?

A

1) reversible
2) irreversible
3) competitive
4) uncompetitive
5) non-competitive

41
Q

What happens in the presence of a competitive inhibitor?

A

1) Vₘₐₓ unchanged (sufficient [S] out-competes inhibitor)

2) Kₘ increased (reduced binding affinity as ES can dissociate + EI form, due to competition)

42
Q

What happens in the presence of an un-competitive inhibitor?

A

1) Vₘₐₓ reduced (some unproductive ESI complex will always be present)
2) Kₘ reduced (formation of ESI to maintain equilibrium, more S binds to E + lower [S] required)

43
Q

What happens in the presence of a non-competitive inhibitor?

A

1) Vₘₐₓ reduced (like un-competitive inhibitor)

2) Kₘ unchanged (no change in position of equilibrium)

44
Q

What does less signal mean on a spectrophotometer?

A

more product

45
Q

What does more signal mean on a spectrophotometer?

A

less product

46
Q

Why are spectrophotometers used?

A

to measure product formation

47
Q

What does a small Kₘ indicate?

A

high affinity (rate will approach Vₘₐₓ more quickly)

Cells to Systems (4 decks)

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