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Biochemistry Exam 2 > Lecture 12: Catalysis > Flashcards

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
Q

Serine proteases/ chymotrypsin reaction products

A

shorter polypeptides

26
Q

Serine proteases/ chymotrypsin type of enzyme

A

hydrolase

27
Q

Serine proteases/ chymotrypsin type of reaction

A

hydrolysis

28
Q

Serine proteases/ chymotrypsin reaction time (uncat)

A

years

29
Q

Serine proteases/ chymotrypsin reaction time (cat)

A

milliseconds

30
Q

Serine proteases/ chymotrypsin active site

A

catalytic triad + oxyanion hole

31
Q

Serine proteases/ chymotrypsin specificity

A

hydrophobic specificity picket

32
Q

Serine proteases/ chymotrypsin catalytic strategies

A

covalent catalysis

acid-base catalysis

33
Q

carbonic anhydrases problem faced (uncat)

A

reaction is not fast enough

34
Q

carbonic anhydrases reaction substates

A

CO2/HCO3-

35
Q

carbonic anhydrases reaction products

A

HCO3-/CO2

36
Q

carbonic anhydrases type of enzyme

A

hydrolase

37
Q

carbonic anhydrases type of reaction

A

hydrolysis

38
Q

carbonic anhydrases reaction time (uncat)

A

seconds

39
Q

carbonic anhydrases reaction time (cat)

A

microseconds

40
Q

carbonic anhydrases specificity

A

(size of entryway)

41
Q

carbonic anhydrases catalytic strategies

A

acid base catalysis
approximation
electrostatic catalysis

42
Q

Why do we need proteases?

A

recycling
regulation
defense

43
Q

The active site of chymotrypsin is an example of _______

A

a catalytic triad

44
Q

The ________ of chymotrypsin stabilizes the tetrahedral intermediate (transition state)

A

oxyanion hole

45
Q

The _______ of chymotrypsin determines placement of cut

A

specificity pocket

Biochemistry Exam 2 (12 decks)

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