Enzymes Flashcards

1
Q

ΔG = ?, ΔG<0 vs. ΔG>0

A

ΔG = ΔH - TΔS (difference of energy between the reactants and products)
ΔG<0 spontaneous
ΔG>0 non-spontaneous

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

large Ea vs. small Ea

A

large = slow reaction
small = fast reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is activation energy?

A

the energy required to produce the transition state

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is the purpose of catalysts?

A
  1. lower Ea
  2. stabilizes T.S.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Name 2 ways that enzymes are regulated and the results that occur from regulation.

A
  1. phosphorylation of enzyme
  2. allosteric modulation
    Result of regulation:
    -negative feedback or positive feedback, product made inhibits or promotes enzyme activity, respectively
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Define Vmax, Km and their relationship

A

Vmax: the max rate of product formation
Km: affinity the enzyme has for the substrate
-Large Km value: weak affinity
-small Km value: strong affinity
Km is the substrate concentration required to reach 1/2 of Vmax.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

True or False? Vmax depends on substrate and enzyme concentration.

A

FALSE!!!!!
it only depends on enzyme concentration :0

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

State the changes to Km and Vmax during competitive, noncompetitive, and uncompetitive inhibition

A

Competitive: binds at active site
-Km increases, Vmax stays the same
Noncompetitive: binds to allosteric site of enzyme alone
-Km stays the same, Vmax decreases
Uncompetitive: binds to allosteric site of enzyme-substrate complex
-Km decreases, Vmax decreases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Know the linweaver burk plots, shape, slopes…
-getting closer to the origin means Km or Vmax has increased
-x-intercept: Km
-y-intercept: Vmax

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Should you use a V vs. S plot or lineweaver burk plot when estimating reaction kinetics? Why?

A

Lineweaver burk plots because they are more accurate, linear graph vs hyperbolic graph

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what is cooperative binding, what is the prerequisite for an enzyme to be able to cooperatively bind, and what does a graph of an enzyme that undergoes cooperative binding look like?

A

cooperative binding is when the binding of some substrate facilitates the binding of more substrate until saturation is reached, the enzyme must be made up of more than one subunit, the graph is a sigmoidal curve

How well did you know this?
1
Not at all
2
3
4
5
Perfectly