Lecture 12: Catalysis Flashcards

1
Q

What do enzymes do?

A

lower activation energy

stabilize the transition state

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2
Q

What do enzymes not do?

A

change the delta G of reaction

irreversibly change shape

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3
Q

A catalyst is something that does what?

A

increase the rate of a reaction

but does not undergo any permanent chemical change as a result

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4
Q

What occurs when delta H is negative?

A

energy is released from the system

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5
Q

What occurs when delta H is positive?

A

energy is added to the system

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6
Q

What occurs when delta H is zero?

A

closed system

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7
Q

What occurs when delta S is negative?

A

disorder decreases

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8
Q

What occurs when delta S is positive?

A

disorder increases

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9
Q

What occurs when delta S is zero?

A

no net change in disorder

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10
Q

What occurs when delta G is negative?

A

free energy released; exergonic reaction; favorable reaction; spontaneous

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11
Q

What occurs when delta G is positive?

A

free energy required; endergonic reaction; unfavorable reaction; driven reaction

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12
Q

What occurs when delta G is zero?

A

equilibrium

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13
Q

What are two strategies to drive an unfavorable reaction?

A
  1. Maintain Q
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14
Q

What is the transition state?

A

a high energy, unstable form of the reactants that is ready to form a product

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15
Q

What is activation energy?

A

an energy barrier that must be overcome for the reaction to proceed

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16
Q

What ways can you speed up a reaction and overcome the activation energy barrier?

A
  1. raise temperature

2. stabilize the transition state (use an enzyme)

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17
Q

what is the induced fit model for substrate binding?

A

when a substrate binds, the enzyme changes shape so that the substrate is forced into the transition shape

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18
Q

Catalysis is achieved through:

A

substrate orientation
straining substrate bonds
creating a favorable microenvironment
covalent and/or non covalent interactions between enzyme and substrate

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19
Q

Describe covalent catalysis

A

enzyme covalently binds the transition state (electron transfer)

20
Q

Describe acid base catalysis

A

partial proton transfer to the substrate

21
Q

describe approximation

A

if electrons and/or protons are being exchanged, proper spatial orientation and close contact must occur and if they are right next to each other, the more they are able to react with one another (also called entropy reduction)

22
Q

Describe electrostatic catalysis

A

stabilization of unfavorable charge on the transition state by polarizable side chains in the enzyme and/or metal ions

23
Q

Serine proteases/ chymotrypsin problem faced (uncat)

A

reaction is too slow

24
Q

Serine proteases/ chymotrypsin reaction substrates

A

polypeptide/peptide bond

25
Serine proteases/ chymotrypsin reaction products
shorter polypeptides
26
Serine proteases/ chymotrypsin type of enzyme
hydrolase
27
Serine proteases/ chymotrypsin type of reaction
hydrolysis
28
Serine proteases/ chymotrypsin reaction time (uncat)
years
29
Serine proteases/ chymotrypsin reaction time (cat)
milliseconds
30
Serine proteases/ chymotrypsin active site
catalytic triad + oxyanion hole
31
Serine proteases/ chymotrypsin specificity
hydrophobic specificity picket
32
Serine proteases/ chymotrypsin catalytic strategies
covalent catalysis | acid-base catalysis
33
carbonic anhydrases problem faced (uncat)
reaction is not fast enough
34
carbonic anhydrases reaction substates
CO2/HCO3-
35
carbonic anhydrases reaction products
HCO3-/CO2
36
carbonic anhydrases type of enzyme
hydrolase
37
carbonic anhydrases type of reaction
hydrolysis
38
carbonic anhydrases reaction time (uncat)
seconds
39
carbonic anhydrases reaction time (cat)
microseconds
40
carbonic anhydrases specificity
(size of entryway)
41
carbonic anhydrases catalytic strategies
acid base catalysis approximation electrostatic catalysis
42
Why do we need proteases?
recycling regulation defense
43
The active site of chymotrypsin is an example of _______
a catalytic triad
44
The ________ of chymotrypsin stabilizes the tetrahedral intermediate (transition state)
oxyanion hole
45
The _______ of chymotrypsin determines placement of cut
specificity pocket