Lecture 13- Kinetics Flashcards

1
Q

Km

A

Michaelis constant; [S] where rxn rate is half maximal OR half of the active sites are full

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2
Q

vmax

A

Maximum velocity; Maximum rate possible for a given concentration of enzyme

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3
Q

Kcat

A

Turnover number; Number of substrate molecules converted per active site per time (first order rate constant)

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4
Q

Ks

A

A dissociation constant for substrate binding

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5
Q

Kcat/Km

A

Specificity constant; Measure of enzyme performance by predicting the fate of ES

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6
Q

-1/Km

A

x-intercept

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7
Q

1/vmax

A

y-intercept

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8
Q

Reversible inhibitors

A
  1. Competitive
  2. Non-competitive (allosteric)
  3. Uncompetitive (allosteric)
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9
Q

Competitive inhibition

A

vmax is constant

Km is a variable

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10
Q

Non-competitive inhibition

A

vmax is variable

Km is constant

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11
Q

Uncompetitive inhibition

A

vmax is variable

Km is variable

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12
Q

Irreversible inhibitors (inactive enzymes)

A
  1. Group-specific
  2. Substrate analogs
  3. Suicide inhibitors
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13
Q

Group-specific

A
  • Targets a specific AA

- Specificity for active site: Low

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14
Q

Substrate analogs

A
  • Substrate mimic, modifies enzyme

- Specificity for active site: High

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15
Q

Suicide inhibitors

A
  • Modified substrate so is unable to form products

- Specificity for active site: Very high

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16
Q

LO#1: Lab conditions to remember**

A
  1. [S]<>Km
17
Q

[S]<

A

vo~ ((vmax/km)([S]))

18
Q

[S]=Km

A

vo= vmax/2

19
Q

[S]»Km

A

vo=vmax

20
Q

Good enzyme

A

kcat»k-1; kcat/Km~ K1*

remember ~k1

21
Q

Bad enzyme

A

kcat<