Lecture 5 - Enzymes and Catalysts Flashcards

1
Q

What are Enzymes

A

Biological catalysts that speed up specific enzyme reactions

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2
Q

What causes enzymes to lose their catalytic activity

A

if the enzyme is denatured (dissociated from its subunits)

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3
Q

What is enzyme specificity?

A

The ability of the enzyme to specifically recognise the proper substrate (reactant)

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4
Q

Where do substrates bind to

A

Active Sites

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5
Q

What are the 2 models of substrate active site binding

A
  • lock and key
  • induced fit
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6
Q

What is the lock and key system

A

When the active site and substrate are a perfect fit for each other

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7
Q

What is induced fit

A

When the substrate isn’t a perfect fit to the active site resulting in a conformational change allowing a better fit.

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8
Q

What is the active site composed of

A
  • Substrate Binding Site
  • Catalytic Site
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9
Q

What is the substrate binding site composed of

A

Amino acid side chains interact with the substrate through hydrogen bonding and other electrostatic interactions

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10
Q

What is the activation energy?

A

The minimum amount of energy required to start a reaction

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11
Q

How do enzymes achieve catalysis?

A

By reducing the activation energy of the transition state

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12
Q

Why do proteins lose activity at high temperatures?

A

Denaturation occurs - loss of native folding

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13
Q

What is the pH of enzymes in the intestine?

A

7.5

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14
Q

What is the pH of stomach enzymes

A

1.5

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15
Q

What is the pH for lysosomal enzymes?

A

4-5

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16
Q

What is a steady state?

A

When vMax is reached

17
Q

What is KM

A

The concentration of substrate at which the reaction rate is half-maximal

18
Q

What are enzyme inhibitors?

A

Molecules that interact with enzymes which can cause temporary or permanent block in enzyme activity

19
Q

What are the 2 types of enzyme inhibitors?

A
  • Competitive
  • NonCompetitive
20
Q

What are enzyme cofactors?

A
  • essential ions
  • Coenzymes (organic molecules)
21
Q

What are essential ions composed of

A
  • Activator ions
  • Metal ions for metalloenzymes
22
Q

What are Coenzymes made of

A
  • Cosubstrates
  • Prosthetic Groups
23
Q

What is a Holoenzyme

A

A completely catalytically active enzyme together with its cofactor

24
Q

What is a Holoenzyme

A

A completely catalytically active enzyme together with its cofactor

25
Q

What is an apoenzyme

A

The protein part of the enzyme without its cofactor

26
Q

What are the 7 Classes of enzymes

A

oxidoreducatases
transferases
hydrolases
lyases
isomerases
ligases
translocases