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ZOO 241 > Lecture 4/5 > Flashcards

Lecture 4/5 Flashcards

1
Q

What is Lineweaver-Burke Plot equation?

A

y=ax+b

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2
Q

What is Y in the Lineweaver-Burke Plot equation?

A

Y = 1/vo

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3
Q

What is A in the Lineweaver-Burke Plot equation?

A

Slope:

Km/Vmax

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4
Q

What is X in the Lineweaver-Burke Plot equation?

A

1/[S]

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5
Q

What is B in the Lineweaver-Burke Plot equation?

A

Y intercept

1/Vmax

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6
Q

What is Competitive inhibition?

A

It is when an inhibitor blocks the substrate from binding to the active site of the enzyme.

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7
Q

When dealing with a competitive inhibitor, will the binding affinity of the enzyme change?

A

No, it will only appear to change due to the inhibitor binding to the active site of enzymes.

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8
Q

What is the structural shape of a competitive inhibitor?

A

It is generally the same shape as the solute it is competing with.

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9
Q

How can you detect a Competitive inhibitor?

A

You will see an increase in Km.

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10
Q

What causes non-competitive inhibitor?

A

Caused by allosteric inhibition of active site distal to the substrate

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11
Q

How does a non-competitive inhibitor work?

A

An agent bound at an allosteric site causes decreased functionality of the enzyme.

Evokes a conformation change that slows the reaction rate.

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12
Q

Is binding reversible in non-competitive inhibitors?

A

Yes

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13
Q

Does the non-competitive inhibitor affect the substrates ability to bind to the active site?

A

Nope

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14
Q

How can you detect a Non-competitive inhibitor?

A

Decrease in Vmax

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15
Q

What is mixed inhibition?

A

When an agent binds to a allosteric site causing a decreased level of functionality in the enzyme

  • Slows reaction rate and binding affinity
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16
Q

How can you detect a mixed inhibitor?

A

You will see a decrease in Vmax and an increase in Km

17
Q

What happens in allosteric activation?

A

It is a up-regulator

You will see a decrease in Km

18
Q

What happens in a covalent activation?

A

It is a up-regulator

You will a increase in Vmax. But no change in Km

19
Q

What two major roles do enzymes play in the regulation of pathways.

A

They can speed up reactions or they can limit them.

20
Q

true or false:
Enzymes that catalyzes rate-limiting reactions and branch point reactions are well positioned to extert control over metabolism?

A

True.

21
Q

What is a branching metabolic pathway?

A

It is where an enzyme can change between two or more streams for what should be produced

22
Q

How do you slow down a reaction rate?

A

With a rate limiting reaction Enzyme.

It can be due to a high Km, or Low Vmax

23
Q

What is the principle of mass action?

A

The more of solute you have determines that reaction rate.

24
Q

True or false:

Allosteric modulators do NOT follow the principle of mass action.

A

False,

they do.

25
Q

Why are explosive reactions casued by mass action important?

A

They allow for measurable physiological changes at a faster rate.

26
Q

How can you arrange enzymes and other proteins on a family tree?

A

Through the examination of their amino acids.

27
Q

What is conserved as enzymes evolve and change due to mutation?

A

The active site gouge.

28
Q

What would casue alleles to differ in frequency from warmer weather to colder weather?

A
  • Selective pressure
  • The temperature affects the bonds within the enzyme. The greater the bonds the better it can hold up in warmer weather. Inversely true for the cold.
29
Q

What enzyme is SUPER important for the regulation of glycolysis?

A

Phosphofructokinase -

Allosterically modulated enzyme.

30
Q

What two molecules regulate Phosphofructokinase?

A

Citrate and AMP

31
Q

What does Citrate do?

A

When citrate is combined, according to mass action with its regulatory site, it decreases the catalytic activity. IE - lowers Km

32
Q

What does AMP do?

A

AMP increase the catalytic activity when it combines with its active site.

IE increases Km

ZOO 241 (17 decks)

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