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Biological Chemistry > Enzyme Kinetics 1 > Flashcards

Enzyme Kinetics 1 Flashcards

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1
Q

Define “enzyme (E)”

A

protein catalyst

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2
Q

Define “catalyst”

A

speed up reactions without being changed by the reaction

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3
Q

Define “substrate”

A

reactant(s) in the enzyme catalysed reaction

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4
Q

Define “active site”

A

area of where the substrate(s) bind(s)

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5
Q

What are enzymes involved in?

A

all biological processes

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6
Q

What does catalysis offer?

A

CONTROL

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7
Q

What is “catalysis”?

A

a process about energy and entropy

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8
Q

What are the conditions of an energetically favourable reaction? (3 conditions)

A
  • delta G is negative (<0)
  • spontaneous reaction
  • forward reaction occurs
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9
Q

What are the conditions of an energetically UNfavourable reaction? (4 conditions)

A
  • delta G is positive (>0)
  • non- spontaneous reaction
  • no forward reaction (unless coupled to second energetically favourable reaction)
  • reverse may occur
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10
Q

What is “entropy”

A

a measure of molecular disorder, or randomness, of a system

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11
Q

What is the formula for “dissociation rate”?

A

dissociation rate constant (k{off}) times by concentration of AB ([AB])

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12
Q

What is the formula for “association rate”?

A

association rate constant (k{on}) times by concentration of A ([A]) times concentration of B ([B])

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13
Q

Binding of an enzyme to a substrate provides what?

A

a TRANSITION state

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14
Q

What does the transition state consist of?

A

enzyme-substrate complex (ES) and enzyme-product complex (EP)

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15
Q

What are the two models for enzyme-substrate binding?

A
  • lock and key

- induced fit

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16
Q

Describe the “lock and key” model

A

the substrate binds to the active site of the enzyme due to their complementary shapes

17
Q

Describe the “induced fit” model

A

the substrate binds to the active site of the enzyme as a conformational change in the tertiary structure occurs to allow for this interaction. The enzyme then returns back to its original shape

18
Q

Describe “specificity”

A

an enzyme is specific to the substrate due to the active site

19
Q

What are/do biological catalysts (do)? (4 answers)

A
  • increases the rate of reactions
  • reduces the activation energy
  • do NOT alter reaction equilibrium
  • generally specific for a single reaction
20
Q

What is the general equation for enzymatic reactions?

A

E+S reverse ES reverse EP reverse E+P

21
Q

What is the stage between E+S and ES called?

A

catalysis

22
Q

What can be measured during an ES experiment? (5 answers)

A
  • decrease in substrate
  • increase in product
  • amount of side product
  • amount of time enzyme is BOUND to the substrate
  • amount of time enzyme is UNBOUND to the substrate
23
Q

Can substrates and products have colour?

A

Yes

24
Q

What is used to measure very fast reactions?

A

stopped flow

25
Q

Can enzymes alter the size of substrates?

A

Yes

26
Q

Give an example of an enzyme that alters the size of substrates?

A

DNA restriction endonucleases

27
Q

During an enzyme reaction, what changes concentration?

A
  • substrate(s)

- product(s)

28
Q

The differing physical characteristics of products and substrate can be used to measure what?

A

Rate of reaction

29
Q

It is important to understand how fast it goes under what conditions?

A

different concentrations of substrate available

30
Q

When characterising an enzyme what do we need to know?

A
  • the maximum rate of an enzyme catalysed reaction

- the affinity of an enzyme

31
Q

What is the method when changing the concentration of the substrate and enzyme? (4 answers)

A

1) high concentration (excess) of the substrate and a much lower concentration of enzyme
2) measure the rate
3) decrease substrate concentration
4) measure again

32
Q

When calculating the rate, what could you measure?

A
  • decrease in substrate

- increase in product

33
Q

How do you calculate the amount of product produced?

A

take the INITIAL gradient of slope

34
Q

How do you calculate the gradient for the slope?

A

initial velocity - rate (v)

35
Q

What is the rate (v) formula?

A

maximum rate of substrate conc. / constant Km + substrate conc.

36
Q

What is the constant, “Km”?

A

enzyme affinity for the substrate

37
Q

How is Km calculated?

A

1/2 Vmax (maximum velocity) (on y axis) and finding the x coordinate that corresponds

Biological Chemistry (6 decks)

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