Lecture 4 Flashcards

1
Q

Define enzymes

A

• Enzymes - globular proteins of high molecular weight that act as catalysts (RNA is exception)
• Enzymes are specific - most cellular reactions catalysed by enzymes
Faster reaction rate

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2
Q

What is the nomenclature for enzymes?

A

Named by adding -ase to end of substrate it catalyses , e.g. lactase, or to catalysed reaction e.g. polymerase

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3
Q

What do some protein enzymes require for their activity?

A

• Some protein enzymes require non-protein group for their activity
• Haloenzymes - contains non-protein group = co-factor (non protein group), apoenzyme (protein)
Isoenzymes - occurs in different molecular form but catalyse same reaction

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4
Q

Give an example of basic enzyme classification

A

e.g. oxidoreductases = oxidation-reduction reactions,

isomerases - isomerization reactions

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5
Q

How do enzymes work?

A

• Lowers EA by forming enzyme-substrate complex

- Free energy change and equilibrium constant unaffected by enzymes

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6
Q

What are the four steps in a catalytic reaction?

A
  1. enzyme and substrate are available, 2. substrate binds to enzyme,
  2. substrate converted to products,
  3. products are released
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7
Q

Describe the problems with the lock and key model

A
  • Assume enzymes are rigid - they are flexible molecules
  • Over and undersized molecules are observed to bond but not react
  • Some reactions occur in fixed sequence
  • Mechanism for reaction rate enhancement not clear
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8
Q

Describe the induced fit model

A
  • Enzyme partially flexible, substrate influence enzyme final shape
  • Some compounds bind to enzyme but not react as enzyme distorted too much
  • Some molecules too small to induce proper alignment, therefore cant react
  • Only right substrate capable of inducing proper alignment of active site
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9
Q

What is the Michaelis-Mentin equation?

A

v=(v_max [S])/(K_M+[S])

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10
Q

Describe the saturation kinetics

A
  • reversible step: enzyme substrate(ES) complex formed

- Dissociation step: ES complex dissociates to give product and free enzyme

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11
Q

What assumptions are made in the MM equation?

A

Assumptions - high substrate conc. so enzyme saturated, ES complex established rapidly, negligible reverse reaction (2nd step)

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12
Q

Describe the Rapid equilibrium approach

A

Occurs in first step, product formation step slower than first step= ES complex always at equilibrium conc.

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13
Q

Describe the Quasi-steady state approach -

A

Initial substrate conc. > enzyme conc.

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14
Q

What is an enzyme inhibitor?

A

Compounds other than substrate that may bind to enzymes and reduce their activity
Can be either reversible or irreversible - irreversible form stable complex, reversible easily dissociate

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15
Q

Describe the three major classes on inhibitor mechanisms

A
  • Competitive - inhibitor usually substrate analog, compete with substrate for enzyme active site => Vmax same, Km increases
  • Non-competitive - not substrate analogs, bind on sites other than active sites and reduce enzyme affinity => Vmax decreases, Km same
  • Un-competitive - inhibitors bind only to ES complex, no affinity towards free enzyme => Vmax decrease, Km decrease
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