5 - Enzymes Flashcards

1
Q

What is the transition state?

A
  • High energy intermediate between S and P
  • E-S COMPLEX
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2
Q

How do enzymes increase the reaction rate?

A
  • Lower activation energy
  • Facilitate production of transition state
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3
Q

What are the important features of an enzyme?

A
  • Highly specific
  • Unchanged after reaction
  • Do not affect equlibrium
  • Increase rate of reaction
  • Proteins
  • May require cofactors
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4
Q

What is the active site?

A

A small part of the enzyme where the substrate binds, rest of the enzyme acts as scaffolding. Active site has clefts that exclude water to allow the reaction to occur

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5
Q

What is the induced fit model?

A
  • Substrate not complementary to active site
  • Binding of substrate causes conformational change and an induced fit
  • Non covalent interactions between substrate and active site, e.g h bonds and electrostatic attractions
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6
Q

What is Km and what is Vmax?

A

Km - Substrate concentration that gives half Vmax

Vmax - Maximum rate of reaction if all active sites were saturated by substrate

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7
Q

What is the Michaelis-Menten Model?

A

A specific complex between enzyme and substrate is essential for catalysis

Predicts that the plot of Vo vs [S] will be rectangular parabola

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8
Q

What does a low Km mean?

A

HIGH AFFINITY FOR SUBSTRATE

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9
Q

How do you work out the rate of reaction using Michaelis-Menten?

A
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10
Q

What is the rate of reaction UNIT?

A

The amount of enzyme required to convert 1um of substrate into product per minute under standard conditions

Expressed per litre or gram

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11
Q

What is the Lineweaver-Burk Plot?

A

A way of rearranging the Michaelis-Menten so it is linear and Km and Vmax can be calculated

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12
Q

What is an irreversible and reversible inhibitor?

A

Irreversible: Binds tightly and forms covalent bonds

Reversible: Non-covalent. Competitive and non-competitive

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13
Q

How does competitive and non-competitive inhibition affect Km and Vmax?

A

Competitive: Vmax same, Km increases

Non-competitive: Vmax decreases, Km same

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14
Q

How would a Lineweaver Burk plot be affected by competitive and non-competitive inhibition?

A
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15
Q

What are the units for Km and Vmax?

A

Km (conc) = M

Vmax (rate) = M/min

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16
Q

What can a deficiency of vitamin B3 do?

A
  • Vitamin B3 is niacin
  • Niacin a precursor for NAD and NADP
  • NAD and NADP are coenzymes so without them other enzymes can’t work
  • Lower aerobic respiration rate
17
Q

What would these graphs look like if substrate was infinite?

A