Chapter 7 Flashcards

1
Q

Zero order reaction

A

rate does not depend on concentration of substrate

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2
Q

Velocity or rate of reaction is determined by measuring

A

how much A disappears as a function of time and how much B appears as a functionof time

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3
Q

First order concentration

A

Rate depends on concentration of substrate

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4
Q

When the substrate concentration is low, an enzyme
reaction
* a. will display zero-order kinetics.
* b. will display first-order kinetics.
* c. will display second-order kinetics.
* d. will denature and cease to function

A

b. will display first-order kinetics.

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5
Q

initial velocity (V0) for each substrate concentration is determined from the slope of the curve at …

A

the beginning of a reaction

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6
Q

Km is the substrate concentration that yields

A

1/2 Vmax

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7
Q

Low Km indicates

A

high affinity between enzyme and substrate

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8
Q

Michaelis constant KM is related to the

A

rate constants of individual steps in catalytic scheme

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9
Q

Wehn V==1/2 Vmax, the Km =

A

[S]

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10
Q

Hexokinase catalyzes the phosphorylation of glucose and fructose by ATP. Km for glucose is 0.15mmol/L, whereas that for fructose is 1.5mmol/L. Assume V max is the same for both glucose and fructose and the enzyme displays hyperbolic kinetics.

For which substrate does hexokinase have the great affinity?

Also, the comparison of the two sugars for hexokinase indicates which sugar is preferred as a nutrient?

fructose, fructose
glucose, fructose
fructose, glucose
glucose, glucose

A

glucose, glucose

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11
Q

Michaelis Menten equation manipulated into one that yields ________ by equation called

A

straight line
Lineweaver Burk equation

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12
Q

Advantages for lineweaver burkplot

A
  1. Straight line so easier to determine how well points fit in straight line than to a curve
  2. effects of inhibitors on reaction can be analyzed more easily
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13
Q

KM value is approximately the substrate concentration of the enzyme in _____

A

vivo

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14
Q

k2/kcat

A

turnover number of enzyme
number of substrate molecules converted into production per second

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15
Q

What is the measure of maximum catalytic efficiency?

A

k2/kcat

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16
Q

_____ Kcat/KM indicates more efficient enzyme

A

higher

17
Q

A –> B -> C –> D –> E –> F
what is the key committed step

A

A –> B
so B is committed to being converted into F

18
Q

Allosteric enzymes

A

Quaternary structure
Response to environmental signal
Sigmoidal curve (cooperativity)
Threshold effect
K 0.5

19
Q
A
20
Q

Michaelis Menten enzymes

A

Tertiary structure
Not regulated in the cell
Hyperbolic shape
Km

21
Q
A