Chapter 4: Enzyme Kinetics Flashcards

1
Q

Enzyme kinetics

A
  • Investigation of rates of enzyme-catalyzed reactions

- Help determine substrate specificity and reaction mechanisms

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2
Q

Establishes the initial rate of reaction

A
  • Measuring either the disappearance of substrate or the appearance of product per unit time
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3
Q

Progressive curve

A
  • The time course of an enzyme-catalyzed reaction
  • Concentration on y-axis
  • Time on x-axis
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4
Q

Maximum velocity of enzyme (Vmax)

A
  • The point where the enzyme the enzyme is saturated with substrate (all enzyme in ES form) and very little free enzyme exists
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5
Q

Initial reaction rates (Vo)

A
  • Measured by drawing a tangent to the hyperbolic plot of [product] formed vs time when t = 0
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6
Q

Progress cruve (Vo) is at maximum

A
  • Substrate supplies are high and a minimal amount of product has been formed
  • Makes reverse reaction insignificant
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7
Q

High enzyme concentration effect on initial rate

A
  • Initial rate will be higher at high enzyme concentration than at low enzyme concentration
  • More product is formed as time increases for each enzyme when substrate is in excess
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8
Q

Gradient of slope

A
  • Calculates the amount of product formed per unit time
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9
Q

Calculate initial rate (Vo)

A
  • Can be determined by measuring the gradient at t = 0
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10
Q

First order kinetics

A
  • At low concentrations or substrate, a rapid increase in reaction velocity that is proportional to [S] is observed
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11
Q

Zero order kinetics

A
  • At high [S] the curve plateaus at a maximum value (Vmax)

- Reaction velocity is independent of changes in [S]

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12
Q

Temperature

A
  • Reaction rate initially increases when this increases as the enzyme is activated
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13
Q

Denaturation of the enzyme

A
  • Occurs when the non-covalent stabilizing factors of an enzyme are broken
  • Reaction rate declines as the temperature is further increased
  • Native conformation of the enzyme is disrupted
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14
Q

pH

A
  • Measure of [H+] of a solution

- (-) log [H+] = log 1/[H+]

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15
Q

Functional groups

A
  • Side chains of amino acids
  • Can function as weak acids
  • Perform acid/base interactions
  • Degree of ionization changes as pH fluctuates
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16
Q

Interstitial fluid buffer system

A
  • Carbonic acid - Bicarbonate
  • Hydrogen phosphate
  • Proteins
17
Q

Intracellular fluid buffer system

A
  • Carbonic acid - Bicarbonate
  • Hydrogen phosphate
  • Proteins
18
Q

Blood buffer system

A
  • Carbonic acid - Bicarbonate
  • Hemoglobin
  • Hydrogen phosphate
  • Plasma proteins
19
Q

Acidosis

A
  • pH of blood falls

- Common in poorly controlled diabetes mellitus

20
Q

Protects against acidosis

A
  • Carbonic acid - bicarbonate buffer system of the blood
21
Q

Alkalosis

A
  • pH of the blood becomes elevated above 7.4

- May occur with extended periods of vomiting or from hyperventilation

22
Q

Hydrogen phosphate - dihydrogen phosphate buffer system

A
  • Works in the cytoplasm of most cells
23
Q

Gastric pepsin

A
  • Secreted from the chief cells in gastric glands

- Optimal pH of 1.5

24
Q

Michaelis constant (Km)

A
  • The substrate concentration at which the initial velocity is 1/2 Vmax (half the enzyme active sites are occupied)
25
Q

Y-intercept of LWB

A

1/Vmax

26
Q

X-intercept of LWB

A

-1/Km

27
Q

Gradient/slope of LWB

A

Km/Vmax

28
Q

Enzyme Kinetics

A
  • The study of the initial rates (Vo) of enzyme-catalyzed reactions
29
Q

Plotting of Vo vs [S] or an enzyme-catalyzed reaction yields:

A
  • A classic hyperbolic plot for enzymes that exhibit M/M kinetics
30
Q

Michaelis constant (Km)

A
  • The substrate concentration at which the reaction rate is half maximal
31
Q

Lower Km

A
  • Higher enzyme’s affinity for susbtrate
32
Q

Changes in temperature and pH

A
  • Can alter enzyme activity