Exam 3 Flashcards

1
Q

The two distinct divisions of metabolism

A

Catabolic reactions (catabolism) and anabolic reactions (anabolism)

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2
Q

Catabolic Reactions (characteristics)

A

1) Breaks down complex molecules, makes them simpler. 2) releases energy. 3) DOWNHILL REACTION

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3
Q

Anabolic Reactions (characteristic)

A
  • links simple molecules
  • makes them more complex
  • require energy
  • UPHILL REACTIONS
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4
Q

Metabolic Pathways

A

Series of chemical reactions that happen in a cell

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5
Q

Delta G

A

G (products) - G (reactants)

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6
Q

Delta G in exergonic reactions

A

Negative

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7
Q

Delta G in endergonic reactions

A

Positive

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8
Q

Energy coupling

A

Exergonic reactions are used to drive endergonic ones

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9
Q

ATP

A

Adenosine Triphosphate
“Energy currency” in cells
Powers cellular work through energy coupling

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10
Q

How does the release of energy occur during the hydrolysis of ATP?”

A

The chemical change to a lower state of free energy causes energy to be released

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11
Q

How do enzymes speed up metabolic reactions?

A

By lowering the activation energy barrier, making it so that the reaction to happen at moderate temperatures.

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12
Q

Catalyst

A

Chemical agent that speeds up a reaction without being consumed by the reaction

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13
Q

What is an enzyme?

A

A catalytic protein. (Names often end in -ase)

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14
Q

What is the enzyme’s substrate?

A

The reactant that an enzyme acts on.

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15
Q

What happens when the enzyme binds to its substrate?

A

Enzyme-substrate complex is created

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16
Q

What happens to the enzyme when the substrate enters the active site?

A

Enzyme changes shape slightly, creating an induced fit.

17
Q

What affects enzyme activity?

A

Temperature, pH, cofactors, and inhibitors.

18
Q

Temperature’s effect on enzyme activity

A

As temperature increases, the reaction rate will also increase. Enzymes also have a peak performance at a temperature optimum, they denature beyond that temperature.

19
Q

pH’s effect on enzyme activity.

A

Most enzymes have a pH at which they perform at peak efficiency (pH optimum)

20
Q

What is a cofactor?

A

A nonprotein helper that binds to the enzyme permanently, or reversibly with the substrate

21
Q

What is a coenzyme?

A

Organic cofactors

22
Q

What are inhibitors?

A

Chemicals that selectively inhibit the action of specific enzymes

23
Q

When is inhibition usually irreversible?

A

When the inhibitor covalent bonds with the enzyme

24
Q

When does reversible inhibition happen?

A

When inhibitors bind to the enzyme by weak interactions

25
Competitive inhibitors
Inhibitors that closely resemble the substrate and can bind to the active site
26
How can you overcome competitive inhibition?
By increasing substrate concentration
27
What are noncompetitive inhibitors?
Inhibitors that bind to a part of the enzyme that is away from the active site. This causes the enzyme to change shape (the active site becomes less effective)
28
Allosteric Regulation
- Can inhibit or stimulate the enzyme's activity - Occurs when a regulatory molecule binds to a protein at one site and affects the protein's function at another site
29
What is cellular respiration?
A catabolic pathway that breaks down organic molecules. It uses an electron transfer chain for the production of ATP
30