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S2 E2 KCU COB Andersen Courses > Biochemistry E2 > Flashcards

Biochemistry E2 Flashcards

1
Q

What is the fractional saturation of binding?

A

Y= [S] ÷ (KD + [S])

The concentration of bound ligand divided by the total amount of protein/enzyme

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2
Q

What is KD

A

The dissociation constant or the [S] at half the saturation

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3
Q

What is KD related to when the protein is enzymatic/catalytic?

A

KD=KM

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4
Q

In a Sctchard plot graph, when n=1,
Slope
x-intercept
y-intercept

A

Slope: -1/KD
x-intercept = [E]T
y-intercept = 1/KD

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5
Q

In a Sctchard plot graph, when n>1,
Slope
x-intercept
y-intercept

A

Slope: -1/KD
x-intercept = n
y-intercept = n/KD

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6
Q

What is the Hill Equation?

A

Log(ø ÷ (1-ø)) = Log (1/KD) + nLog[S]

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7
Q

What type of graphs are Hill Plots usually?

A

Sigmoidal

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8
Q

What does the slope of the Hill plot tell us?

A

Slope= n
n>1 = Positive cooperativity
0

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9
Q

What is the y-intercept of the Hill plot?

A

log(1/KD) = log(1/Km)

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10
Q

Michaelis-Menten Kinetics follow what order of enzymes?

A

First Order Enzymes

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11
Q

What does the graph of Zero-order kinetics look like?

A

If [S] vs time is linear, the reaction is 0-order

v=k

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12
Q

What does the graph of First-order kinetics look like?

A

If ln[S] vs time is linear, the reaction is 1st order

v=k[S]

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13
Q

What does the graph of Second-order kinetics look like?

A

If 1/[S] vs time is linear, the reaction is 2nd order

v=k[S][S] or v=k[S1][S2]

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14
Q

What is the initial reaction rate equation?

A

V0 = Vmax • [S] ÷ ([S] + Ks)

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15
Q

What are the three assumptions for Michaelis-Menten Kinetics?

A
  1. Binding of the substrate to the enzyme is at equilibrium
    (Ks = K-1/K1)
  2. Since we are measuring initial rate, not enough product is present for the reverse reaction to occur
    (Secon step is irreversible)
  3. Stead State Assumption
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16
Q

What is the steady state assumption?

A
  • When [S] is very large, ∆[S] = 0

- Formation of E•S complex occurs at the same rate that its loss either by dissociation or by product formation

17
Q

Define Km

A

Michaelis Menten constant
When [S] where half the active sites are full
OR
When [S] where the reaction is half maximal

18
Q

What is the equation for the Michaelis Menten Kinetics?

A

V0= Vmax • [S] ÷ ([S]+Km)

19
Q

Define Vmax

A

How fast the reaction can take place

Vmax = Kcat[E]

20
Q

Kcat is the same as

A

K2
Movement from E•S complex to E•P complex
(Changing Substrate to Product)

21
Q

What happens when [S]<

A

V0 = (vmax÷Km) * [S]

Less than half the binding sites are occupied

22
Q

What happens when [S]=Km

A

V0 = Vmax/2

Half the binding sites are occupied

23
Q

What happens when [S]»Km

A

V0 = Vmax

All the binding sites are occupied

24
Q

What is the specificity constant?

A

Kcat ÷ Km = (Kcat ÷ (K-1 +Kcat)) •K1
Used to determine catalytic efficiency
Measures what happens when to E•S complex

25
Q

A good enzyme vs a poor enzyme

A

Good enzymes: Kcat»K-1
(More production of product)

Poor Enzymes: Kcat<

26
Q

Lineweaver-burk plots are used for

A

reversible inhibitors

27
Q

What is vmax and Km with a competitive inhibitor?

A

Vmax is constant and Km is variable

Inhibitor binds at the enzyme

28
Q

What is vmax and Km with a Noncompetitive inhibitor?

A

Vmax is variable and Km is constant

Inhibitor binds at Enzyme or E•S complex

29
Q

What is vmax and Km with an uncompetitive inhibitor?

A

Vmax is variable and Km is variable

Binds at E•S complex

30
Q

Constitutional Isomers

A

Changes orders of atoms

Also called Tautomers

31
Q

Stereoisomers have the

A

same connectivity, but different spatial organization

32
Q

Configurational Isomers are

A

Stereoisomers that have chiral carbons

33
Q

Enantiomers are

A

mirror images at ALL CHIRAL centers

34
Q

Diastereomers have

A

multiple chiral centers, but not all chiral centers are mirror images

35
Q

The anomeric carbon decides

A

Whether it is an alpha or beta carbohydrate in the ring form
Beta is up
Alpha is down

36
Q

When converting from fischer to hawthorn projections, What goes up and what goes down?

A

Right side is down

Left side is up

37
Q

Anomers vis epimers

A

Anomers differ at the anomeric carbon

Epimers differ at locations other than the anomeric carbon

S2 E2 KCU COB Andersen Courses (14 decks)

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