Chapter 8: Energy and Enzymes for Exam 2 Flashcards

1
Q

The reactant acted on by the enzyme

A

Substrate

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2
Q

Are prosthetic groups organic or inorganic?

A

Both

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3
Q

Regulation that can either activate or inhibit activity

A

Allosteric regulation

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4
Q

Does being spontaneous mean the rxn occurs quickly?

A

No

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5
Q

How is enzyme function regulated?

A

Tightly regulated through competitive inhibition and allosteric regulation

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6
Q

What often act as enzyme inhibitors and can have irreversible binding?

A

Toxins and poisons

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7
Q

What 3 things would enzymes not function without?

A

Cofactors, coenzymes, and prosthetic groups

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8
Q

How do enzymes catalyze rxns?

A

By lowering activation energy

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9
Q

What types of drugs inhibit enzymes?

A

HIV medications, ACE inhibitors (HBP), Prilosec (H+/K+ ATPase), penicillin

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10
Q

What are enzymes?

A

Proteins or sometimes RNA which act as catalysts and speed up rxns

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11
Q

Factors that affect enzyme activity

A

Temp and pH

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12
Q

What is induced fit?

A

When the binding of the substrate causes the enzyme to slightly change shape

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13
Q

How specific do substrates need to be to fit an active site?

A

Very specific. Only very specific ones can fit the active site

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14
Q

What is the optimal pH for enzymes in humans?

A

Depends on where they are found

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15
Q

What do enzymes often do?

A

Catalyze a series of related rxns

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16
Q

Regulatory molecule binds away from the active site and causes change in shape

A

Allosteric regulation

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17
Q

What does sarin gas do?

A

Binds to the active site of acetylcholinesterase and acts as a competitive inhibitor that causes ACh to stay in synapse and continue to signal eventually causing death

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18
Q

Six steps of an enzyme catalyzing a rxn

A
  1. ) Substrates enter active sites
  2. ) Substrates are held in active site by weak interactions
  3. ) Active site can lower activation energy and speed up a rxn
  4. ) Substrates are converted to products
  5. ) Products are released
  6. ) Active site is available for new substrate molecules
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19
Q

Region of the enzyme that actually binds the substrate

A

Active site

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20
Q

What are coenzymes?

A

Organic molecules like NAD, B vitamins, CoQ, folic acid that work with enzymes to make them function properly

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21
Q

How does penicillin work?

A

Blocks the active site of enzyme necessary for cell wall formation in bacteria. Humans don’t need or have that enzyme so it doesn’t effect us

22
Q

How specific is the rxn catalyzed by a particular enzyme?

A

Enzymes are very specific

23
Q

What are prosthetic groups?

A

Molecules tightly bound to enzymes like retinal (vitamin A), metal ions, and vitamins that work with enzymes to make them function properly

24
Q

What does feedback inhibition prevent the cell from doing?

A

Prevents the cell from wasting energy to make excess product

25
Three things that work with enzymes
Cofactors, coenzymes, and prosthetic groups
26
Optimal pH for enzymes in stomach?
1-3
27
Are enzymes consumed in rxns?
No
28
How are metabolic pathways regulated?
Feedback inhibition
29
What happens as you inc temp?
Inc rxn rate until a certain temp and then the enzymes will begin to denature
30
These are usually proteins but can also be RNA
Enzymes
31
What happens to enzymes at the end of a rxn?
They are not consumed and can catalyze again
32
How do enzymes work?
They lower the activation energy (Ea)
33
How does the enzyme shape change during induced fit?
The enzyme shape changes to wrap the substrate
34
Regulatory molecules resembles the substrate and binds to the active site to block the actual substrate
Competitive inhibition
35
Examples of prosthetic groups
Retinal (vitamin A), metal ions, and vitamins
36
Which group is basically part of the enzyme?
Prosthetic groups
37
What is feedback inhibition?
End product of a pathway can bind to an enzyme that acts earlier in the pathway to inhibit it so it doesn't waste energy making excess product
38
Is regulatory binding usually reversible?
yes
39
Optimal pH for enzymes in blood?
Around 7
40
What are cofactors?
Inorganic ions like Fe, Zn, Mg that work with enzymes in order to make them function properly
41
Where is activation energy required in the progress of a rxn
Transition state
42
What does changing the shape of the enzyme during induced fit do?
Brings chemical groups of active site into optimal position to catalyze rxns
43
Examples of coenzymes
NAD, B vitamins, CoQ, folic acid
44
What is activation energy?
Reactants absorb energy from their surroundings to reach state where bonds can change
45
What is optimal temp for enzymes?
Depends on where the enzyme will function. 98.6F in humans, etc.
46
When do proteins function best?
Under specific conditions
47
What does it mean for a rxn to be spontaneous?
It occurs without the need of energy input
48
Regulatory molecules can leave the enzyme to turn it off and on
Allosteric regulation
49
How do starting molecules need to change for a rxn to occur?
They usually need to be contorted into an unstable form
50
Steps in the progress of a rxn?
Reactants to transition state to products
51
Examples of cofactors
Fe, Zn, Mg
52
How do enzymes lower activation energy?
Act as a docking site to bring reactants together in proper orientation (bring substrates to correct positioning), stretch reactants toward transition-state form stressing and bending chemical bonds, provide a microenvironment more favorable to a particular rxn, and participate directly in the chemical rxn