AH L1 - The Origins of Enzyme Catalytic Rate Enhancement Flashcards

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1
Q

What are enzymes made of and what do they do?

A

Proteins.
Catalyses nearly all chemical reactions in living organisms.

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2
Q

Are all enzymes made of proteins?

A

No - catalytic RNA eg hammerhead ribozyme

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3
Q

How much do enzymes accelerate reactions by factors of?

A

10^6 to 10^7

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4
Q

How have the 3D structures of enzymes been solved ?

A

X-ray crystallography & cryoelectron microscopy.

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5
Q

Why is it important to study enzymes?

A
  1. Essential for cellular function.
  2. Targets for drug action.
  3. Used in biotech industries.
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6
Q

What are some enzyme drug targets?

A
  • G - protein-coupled receptors.
  • Ligand-gated ion channels
  • Voltage-gates ion channels
  • Nuclear hormone receptors.
  • **Catalytic Receptors
  • Kinases
  • Proteases**
  • Transporters
  • Other enzymes
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7
Q

What is this symbol ‡? What does it mean?

A

Double Dagger.
Preferential stabilization of the transition state.

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8
Q

What is the equation for the non-catalysed reaction?

A

S <-> P
S= ground state at start = substrate
P = ground state at end = product

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9
Q

What is the formula for an enzyme catalysed reaction?

A

E + S <-> E.S <-> E.P <-> E + P

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10
Q

What does delta G mean?

A

the change in free energy

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11
Q

What do enzymes do to ∆G^‡?

A

It reduces it so that effects the rate at which chemical equilibrium is obtained.

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12
Q

What is ∆G⌄B?

A

Intrinsic binding energy - refers to the total interaction energy btwn the transition state and enzyme functional groups.

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13
Q

What is a major source of free energy used by enzymes?

A

Intrinsic binding energy.

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14
Q

What does ∆G⌄B show between the enzyme and transition state?

A

Favourable interactions i.e. favourable intrinsic binding energy.

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15
Q

What thermodynamic factors does intrinsic binding energy (∆G⌄B) need to overcome?

A
  1. Loss of entropy of molecules in solution.
  2. Desolvation (removal of solvent from a material in solution) on binding of substrate(s).
  3. Distortion of substrates that occurs in many reactions.
  4. Alignment of catalytic functional groups on the enzyme.
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16
Q

Are enzymes inefficient?

A

No they are highly efficient. can increase activity by several 10-folds.

17
Q

What happens with every 10-fold increase in relative rate enhancement (kcat/kuncat)?

A

The transition state of the reaction (‡) must be stabilised by 5.7 kJ/mol relative to ‡ of the uncatalyzed reaction.

18
Q

What chemical mechanisms are there for catalysis? (They do this to achieve satbilisation)

A
  1. The proximity (Approximation) effect
  2. Electrostatic catalysis
  3. Acid-base catalysis
  4. Covalent (nucleophilic) catalysis
19
Q

What is the proximity/ approximation effect?

A

Proximity effect, is to organize the substrates within the active site of the enzyme such that the reactants are much closer together than they would be in a typical solution. Enhancing the proximity of reactants increases their collision frequency, thus causing the reaction to proceed at a faster rate.

20
Q

What is the effective concentration (effective molarity)?

A

The ratio of the 1st-order rate constant of an intramolecular reaction involving two functional groups w/in the same molecular entity to the 2nd-order rate constant of an analogous intramolecular elementary reaction.
This ratio has the dimensions of concentration.

21
Q

What happens are you decrease the rotational and translational entropy of a molecule?

A

The relative rate (kcat) and effective molarity (M) increase.

22
Q

What is electrostatic catalysis?

A

Electrostatic catalysis occurs when the enzyme active site stabilizes the transition state of the reaction by forming electrostatic interactions with the substrate. The electrostatic interactions can be ionic, ionic-dipole, dipole-dipole, or hydrophobic interactions.

23
Q
A