Enzymes Flashcards

1
Q

How do enzymes reduce activation energy

A

Correctly orients substrates
Strains substrate bonds
Proved a favorable micro environment (R groups)
Brief covalent bonds with substrate

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2
Q

What is an enzyme

A

Helps to lower Ea allowing reactions to proceed more efficiently

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3
Q

What is activation energy

A

Initial amount of energy needed for the reaction to proceed

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4
Q

What is the allosteric site

A

Site located away from the active duty where the non competitive inhibitor can fit

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5
Q

Where is the energy of ATP stored

A

In bonds between its terminal phosphate groups

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6
Q

Where are enzymes located

A

It can either be free in the cytoskeleton or be bound to membranes and organelles

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7
Q

What does free energy look like as the reaction progresses on a graph

A

Reactions without and enzyme have a higher Vmax than reactions with an enzyme, but they both meet at y=0

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8
Q

What does the graph of concentration substrate look like with and without inhibitors

A

Without an inhibitor the rate has a higher Km than with an inhibitor but they both have the same 1/2 Vmax and Vmax

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9
Q

What is the product of a reaction used for in feedback inhibition

A

The product directly inhibits the enzyme that made it

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10
Q

What happens when the acidity increases (H+)

A

The H+ is attracted to O, OH becomes an ion dipole (weak) and the molecule becomes more basic

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11
Q

What happens to enzymes when the temperature is decreased

A

The bonds are unable to move and are inflexible

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12
Q

What happens to enzymes when you increase the temperature

A

The energy increases causing the molecules to fall apart

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13
Q

During the catalytic cycle what happens to thermodynamics

A

The thermodynamics are unchanged throughout the catalytic cycle

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14
Q

How does feedback inhibition regulate enzymatic activity in the biochemical pathway

A

It can shut down the pathway if something goes wrong

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15
Q

What is feedback inhibition

A

A way to regulate enzymatic activity in the biochemical pathway

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16
Q

What is an example of a biochemical pathway

A

Glycolysis

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17
Q

What is a biochemical pathway

A

The product of a reaction becomes the substrate for the next reaction

18
Q

What is the 1/2 Vmax

A

Half of the Vmax value

19
Q

What is Km

A

The concentration substrate it takes to reach 1/2 Vmax

20
Q

Is the reaction rate higher or lower without the inhibitor? With the inhibitor?

A

Without: the reaction rate is higher
With: the reaction rate is lower

21
Q

How would you get rid of the competitive inhibitor

A

Add more substrate

22
Q

What is the Vmax

A

The maximum reaction rate that can happen within that system

23
Q

Does Ea have an effect on delta g

A

No matter what Ea is, delta G doesn’t change

24
Q

What happens when substrate concentration increases

A

Reaction rate increases and eventually levels off

25
What is a michaelis menten plot
Shows substrate concentration vs reaction rates
26
What is a non competitive inhibitor
Bonds to the allosteric site which changed the shape of the active site
27
What is a competitive inhibitor
Mimics substrate and competes with the substrate for access to active site
28
What are inhibitors
Controls enzyme activity
29
What is normal binding
A substrate can normally bind to the active site of an enzyme
30
Why is Mg2+ essential for ATP hydrolysis
It brings substrates together which stabilized molecules
31
What are organic cofactors
Small, non-protein organic molecules (vitamins)
32
What are inorganic cofactors
Metallic ions that can move electrons from covalent bonds (Mg, zinc, copper, etc.)
33
Enzymes are…
Substrate specific, meaning they only react with specific substances
34
What is the 1st step of the catalytic cycle
Substrates enter the active site
35
What is the second step of the catalytic cycle
Substrates are held in the active site by weak interactions
36
What is the third step of the catalytic cycle
The active site lowers the Ea
37
What is the 4th step of the catalytic cycle
Substrates are converted into products
38
What is the 5th step of the catalytic cycle
The products are released
39
What stage of protein structure is the active site in
Quaternary structure
40
What does an increase of G cause during the catalytic cycle
Unstable transition state Bonds break and new ones form Free energy is released (spontaneous)