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Bio 1113 > Chapter 8: Energy and Enzymes for Exam 2 > Flashcards

Chapter 8: Energy and Enzymes for Exam 2 Flashcards

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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
Q

Three things that work with enzymes

A

Cofactors, coenzymes, and prosthetic groups

26
Q

Optimal pH for enzymes in stomach?

A

1-3

27
Q

Are enzymes consumed in rxns?

A

No

28
Q

How are metabolic pathways regulated?

A

Feedback inhibition

29
Q

What happens as you inc temp?

A

Inc rxn rate until a certain temp and then the enzymes will begin to denature

30
Q

These are usually proteins but can also be RNA

A

Enzymes

31
Q

What happens to enzymes at the end of a rxn?

A

They are not consumed and can catalyze again

32
Q

How do enzymes work?

A

They lower the activation energy (Ea)

33
Q

How does the enzyme shape change during induced fit?

A

The enzyme shape changes to wrap the substrate

34
Q

Regulatory molecules resembles the substrate and binds to the active site to block the actual substrate

A

Competitive inhibition

35
Q

Examples of prosthetic groups

A

Retinal (vitamin A), metal ions, and vitamins

36
Q

Which group is basically part of the enzyme?

A

Prosthetic groups

37
Q

What is feedback inhibition?

A

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
Q

Is regulatory binding usually reversible?

A

yes

39
Q

Optimal pH for enzymes in blood?

A

Around 7

40
Q

What are cofactors?

A

Inorganic ions like Fe, Zn, Mg that work with enzymes in order to make them function properly

41
Q

Where is activation energy required in the progress of a rxn

A

Transition state

42
Q

What does changing the shape of the enzyme during induced fit do?

A

Brings chemical groups of active site into optimal position to catalyze rxns

43
Q

Examples of coenzymes

A

NAD, B vitamins, CoQ, folic acid

44
Q

What is activation energy?

A

Reactants absorb energy from their surroundings to reach state where bonds can change

45
Q

What is optimal temp for enzymes?

A

Depends on where the enzyme will function. 98.6F in humans, etc.

46
Q

When do proteins function best?

A

Under specific conditions

47
Q

What does it mean for a rxn to be spontaneous?

A

It occurs without the need of energy input

48
Q

Regulatory molecules can leave the enzyme to turn it off and on

A

Allosteric regulation

49
Q

How do starting molecules need to change for a rxn to occur?

A

They usually need to be contorted into an unstable form

50
Q

Steps in the progress of a rxn?

A

Reactants to transition state to products

51
Q

Examples of cofactors

A

Fe, Zn, Mg

52
Q

How do enzymes lower activation energy?

A

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

Bio 1113 (22 decks)

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