Lecture 12 Flashcards

1
Q

What do enzymes do

A

Lower the activation energy

Stabilize the transition state

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2
Q

What do enzymes not do

A
Change the (triangle)G of the reaction
Irreversibly change shape
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3
Q

A catalyst is something that

A

Increases the rate of a reaction but does not undergo any permanent chemical change as a result

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4
Q

Change in S positive/negative/0

A

Positive- Increase in disorder
Negative- Decrease in disorder
0- No change in disorder

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5
Q

Change in G positive/negative/0

A

Positive- Endergonic, unfavorable reaction
Negative- Exergonic, favorable reaction
0- Equilibrium

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6
Q

Change in H positive/negative/0

A

Positive- Energy is released from the system
Negative- Energy is added to the system
0- Closed system

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7
Q

How can we speed up a reaction

A

Raise the temperature

Stabilize the transition state (using enzyme)

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8
Q

Induced fit model of catalysis

A

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

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9
Q

Catalysis is achieved through

A

Substrate orientation
Straining substrate bonds
Creating favorable microenvironment
Covalent/noncovalent interactions b/w substrate and enzyme

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10
Q

Covalent catalysis

A

Enzyme covalently binds the transition state (electrons transfer)

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11
Q

Acid-base catalysis

A

Partial proton transfer to the substrate

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12
Q

Approximation catalysis/Entropy reduction

A

Proper spatial orientation and close contact of the reactant molecules must occur for reaction to proceed I
-If both pieces of puzzle can be captured and held in proper orientation (by enzyme) reaction is more likely to occur

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13
Q

Electrostatic catalysis

A

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

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14
Q

What type of enzymes are chymotrypsin and carbonic anhydrase

A

Hydrolases

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15
Q

What is the problem with the reactions the catalyze

A

Chymotrypsin- reaction is too slow without it

Carbonic anhydrase- reaction isn’t fast enough without it

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16
Q

The active site of chymotrypsin contains what AAs

A

Serine- nucleophile
Histidine- base
Aspartic acid- acid

17
Q

Oxyanion hole of chymotrypsin function and AAs

A

Stabilizes the tetrahedral intermediate (transition state), using H-bond interactions (first) then enthalpic interactions (second)

  • Serine
  • Glycine
18
Q

Active site of carbonic anhydrase contains

A

Zn+ atom coordinated to 3 histidines and a water

19
Q

Carbonic anhydrase transition state

A

Facilitated by H2O which is deprotonated

Approximation catalysis strategy is used

20
Q

Reaction mechanism of carbonic anhydrase

A

Water binds Zn, lowering its pKa. Water loses proton at physiological pH
Catalytic strategy of approximation used as substrate enters active site
Nucleophilic addition (functional group added to CO2)
Release of product and regeneration of enzyme (using histidine proton shuffle)