Enzymes Kinetics, Inhibition, and Control Ch.12 Flashcards

(54 cards)

1
Q

What will reduce the amount of cholesterol that we make?

A

Atorvastatin (Lipitor)

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2
Q

What does kinetics refer to?

A

Rates

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3
Q

What doe enzyme kinetic rates refer to?

A

Reaction rates

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4
Q

What do reaction rates refer to?

A

the formation of product as a function of time.

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5
Q

What is the job of an enzyme?

A

To enhance the rate of the reaction.

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6
Q

If the Michaelis-Menten Equation for Enzyme Kineticas is determined early in its course what is considered?

A

products is considered to be low and K-2 ( rate constants) drops out of the equation. Back reaction is negligible.

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7
Q

What is KM?

A

A constant describing the affinity of an enzyme for its substrate.

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8
Q

In KM, the lower the constant what can be determined?

A

The higher the affinity for the substrate.

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9
Q

What gives half maximal VMAX?

A

KM is the S.

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10
Q

What is KM unique for?

A

each substrate of a given enzyme.

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11
Q

What is Kcat?

A

take the Vmax/ total enzyme concentration and it gives you the value of the turnover number.

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12
Q

What is the turnover number?

A

how fast the enzyme will come to a state that it can do it again.

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13
Q

What doe the most efficient reactions reflect a need for?

A

speed

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14
Q

KM should be what in vivo concentrations?

A

10^-2

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15
Q

Ethyl Ester is not something that happens in the cell normally what?

A

The 10^-1 is too big of a concentration to exist inside the cell naturally.

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16
Q

Why do enzyme inhibitors react reversably or irreversably with an enzyme?

A

to alter its Km and or Vmax values.

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17
Q

What alters the KM or Vmas values?

A

Enzymes inhibitors that interact reversibly or irreversibly with an enzyme

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18
Q

What does a competitive inhibitor bind to?

A

the enzymes active site

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19
Q

What does a competitive inhibitor increase?

A

the apparent Km for the reaction

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20
Q

What does an uncompetitive enzyme inhibitor affect?

A

catalytic activity such that both the apparent KM and the apparent Vmax decreases.

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21
Q

A mixed enzyme inhibitor alters both what?

A

catalytic activity and substrate binding.

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22
Q

What will occur with a mixed enzyme inhibitor?

A

Apparent Vmax decreases and the apparent KM may increase or decrease.

23
Q

What occurs in competitive inhibition?

A

The inhibitor binds to the enzyme’s substrate binding site.

24
Q

What does the inhibitor resemble in competitive inhibition?

A

the inhibitor structurally resembles the substrate but not always obvious to the eye.

25
What is pyrazole?
a competitive inhibitor of alcohol dehydrogenase.
26
What is tamiflu (oseltamivir)?
it is a competitive inhibitor of influenze neurominidase.
27
What does Oseltamivir do?
Hydrolizes sialic acid.
28
What is Adenosine Deaminase?
Transition State Analog Inhibitor.
29
What two enzymes does HIV make?
reverse transcriptase and a protease.
30
What is the reverse transcriptase that HIV makes do?
Replicate genome
31
What does the protease that HIV makes do?
cleaves its polyprotein precursor into functional proteins.
32
What is the most important point in regards to competitive enzyme inhibition?
inhibition can be overcome at high substrate concentration.
33
What occurs in the uncompetitve enzyme inhibition?
inhibitor binds to the ES complex.
34
What do allosteric effectors bind to?
multisubunit enzymes
35
What are multisubunit enzymes?
aspartate transcarbamoylase
36
What does the binding of allosteric effectors to multisubunit induce?
cooperative conformational changes that alter the enzyme's catalytic activity.
37
What can phosphorylation and dephosphorylation of an enzyme such as glycogen phosphorylase control?
its activity by shifting the equilibrium between more active and less active conformations.
38
What is the first committed step in the biosynthesis of pyrimidines?
aspartate transcarbamoylase reaction.
39
What is significant of the allosteric effectors: ATCase reaction graphs?
the curves are sigmoidal because the substrates bind cooperatively.
40
Why does the pyrimidine biosynthesis ATCase feedback inhibition is activated by ATP?
To coordinate purine and pyrimidine biosynthesis (need equal amounts for RNA and DNA)
41
What is the important point of ATCase: T-State vs R-state?
the regulatory subunits impose coopertivity on the catalytic subunits.
42
What do regulatory subunits repress?
the catalytic subunits' activity.
43
Allosteric effects of a different molecule binds to an enzyme to what?
modify its activity
44
CTP binds to what?
regulatory subunits to cause substrate binding site to close.
45
Why does CTP cause substrate binding site to close?
inhibit enzyme activity
46
What does CTP undergo this feedback inhibition?
it is the endproduct of the pathway
47
What does ATP bind to in allosteric effect of enzyme activity?
To regulatory subunits to cause the substrate binding site to open and enhances activity.
48
ATP is the product of what?
a parallel pathway.
49
What does the parallel pathways mean when the ATP is the product of parallel pathways?
purine and pyrimidine nucleotides need to be present in nearly in equal amounts.
50
Why do purines and pyrimidine nucleotides needs to be present in nearly equal amounts?
this serves to balance the levels of nucleotides in the cell.
51
How is phosphorylation controlled?
by covalent modification.
52
What is G1P a product of?
Glycogen phosphorylase
53
Rabbit muscle glycogen phosphorylase causes a masking loop to do what?
move out of the way of the active site.
54
What is atorvastatin (lipitor)?
inhibitor of HMG CoA reductase-rate limiting step in cholesterol synthesis.