Basic Concepts of Enzyme Action Flashcards

1
Q

What do enzymes do?

A

Accelerate the rate of rxns, highly specific in both the rxns they catalyze and choice of reactants (substrate)

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2
Q

What are proteolytic enzymes?

A

Catalyze proteolysis, which is hydrolysis of a peptide bond (breakage of bond with H2O), differ greatly in degrees of substrate specificity

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3
Q

What are the six major classes of enzymes?

A
  1. Oxidoreductases
  2. Transferases
  3. Hydrolases
  4. Lyases
  5. Isomerases
  6. Ligases
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4
Q

Oxidoreductases

A

Catalyze redox rxns (transfer e- between molecules)

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5
Q

Transferases

A

Transfer functional groups between molecules

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6
Q

Hydrolases

A

Cleaves molecules by addition of H2O

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7
Q

Lyases

A

Adds atoms or functional groups to a double bond or removes them to form a double bond

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8
Q

Isomerases

A

Move functional groups within a molecule

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9
Q

Ligases

A

Join 2 molecules in rxn powered by ATP hydrolysis

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10
Q

Enzymes often cannot meet the chemical needs required for catalysis to take place, so they depend on

A

the presence of cofactors (small molecules)

  • Enzyme without cofactor = apoenzyme
  • Enzyme with cofactor = holoenzyme
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11
Q

Cofactors are divided into 2 groups:

A
  1. Coenzymes

2. Metals

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12
Q

Coenzymes

A

Small organic molecules derived from vitamins, similar to cosubstrates bc they bind to the enzyme and are released from it, used by variety of enzymes

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13
Q

Metals

A

Bound at the active site and participate in the rxn

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14
Q

Free Energy Change

A

For spon, deltaG = (-)
At equil, deltaG = 0
deltaG is independent of pathwaymechanism of transformation
deltaG tells NOTHING about rate of rxn

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15
Q

For a rxn to be energetically favourable (spon), deltaG must be

A

negative
Spon rxns are NOT instantaneous
Enzymes make a spon rxn kinetically favourable

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16
Q

How do enzymes accelerate rxns?

A

By decreasing the activation energy to overcome the activation energy barrier
Enzymes lower the activation energy by stabilizing the transition state

17
Q

What are the features of enzyme active sites?

A
  1. Residues forming the active site come from different positions in the primary sequence
  2. Small volume of total protein
  3. Unique microenvironment (polar residues on inside when normally outside)
  4. Forms many weak interactions with substrates
  5. Specificity of substrate binding depends on the precise arrangement of atoms in the active site
18
Q

What is binding energy?

A

The free energy that is released when many weak interactions form between the enzyme and substrate and transition state
- Only the correct substrate can maximize the amount of binding energy = specificity

19
Q

When does maximal binding energy occur?

A

During the formation of the transition state