Test 2 - Enzymes (Corrected) Flashcards

1
Q

Catalysis by proximity

A
  • Substrate molecules are in the active site of enzymes
  • Support:
    • If you can bring enzymes closer to their substrates, then the reaction will move faster.
    • In example C the esthers are already close to each other so they can be catalyzed faster.
  • Role in Substrate Channeling
    • Substrates are channeled that way the concentration of substrates and intermediates is kept high as it moves from one enzyme to the next.
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2
Q

Acid - Base Catalysis

A
  • Side chains and prosthetic groups contribute to catalysis by acting as acids and bases.
    • Presence of Asp, Glu, Lys, Arg, His.
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3
Q

Coenzyme A

A
  • Transfers: Acyl groups
  • Precursor: Pantothenic acid and other compounds.
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4
Q

FAD

A
  • Flavin Adenine dinucleotide
  • Transfer: Electrons
  • Precursor: Riboflavin (Vit. B2)
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5
Q

Lipoate

A
  • Transfers: Electrons and Acyl groups
  • Precursor: No dietary
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6
Q

NAD

A
  • Nicotinamide adenine dinucleotide
  • Transfer: Hydride Ion ( :H -)
  • Precursor: Nicotinic Acid (Niacin)
  • Mobile Universal electron carrier
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7
Q

Thiamine pyrophosphate

A
  • Transfer: Aldehydes
  • Precursor: Thiamine (Vit. B1)
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8
Q

Tetrahydrofolate

A
  • Transfer: One carbon groups.
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9
Q

What type of inhibition does this graph show?

A

Competitive

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10
Q

What type of inhibition is this equation?

A

Competitive

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11
Q

What type of inhibition is this graph

A

Mixed inhibition graph

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12
Q

What type of inhibition is the following graph?

A

Uncompetitive

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13
Q

What does competitive inhibition effect?

A

Negatively impacts Km

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14
Q

What does mixed or noncompetitive inhibition effect?

A

Decreases maximum Velocity.

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15
Q

What does uncompetitive inhibition affect?

A

Decreases both Km and Vmax.

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16
Q

Catalysis by strain

A
  • Enzymes bind substrate in an unfavorable conformation to weaken the bond and promote cleavage.
    • Eg. Stickase model
17
Q

Catalysis by proximity

A
  • Effective concentration and orientation of substrate molecules in the active site speed up efficiency.
    • Eg. Substrate channeling by multi-enzyme complexes.
18
Q

Covalent catalyis

A
  • Formation of a covalent bond between the enzyme and one or more groups or substrates to create a more reactive enzyme
    • Eg. group transfer reactions.
    • Often contain Ser or Tyr
19
Q
A