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Advanced Biology > Unit Three - Enzymes > Flashcards

Unit Three - Enzymes Flashcards

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1
Q

What is the function of an enzyme? (2)

A
  1. Speed up the rate of a chemical reaction
  2. By lowering the activation energy
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2
Q

Why can enzymes be reused over and over again? (2)

A

AFTER A CHEMICAL REACTION

  1. Enzymes are not changed or used up
  2. Only a small amount is needed to catalyze numerous rxns
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3
Q

Are enzymes organic and why?

A

Yes, contain C - H bonds

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4
Q

Are enzymes specific? (3)

A

Yes
1. Each enzyme can only catalyze 1 substance
2. Isomers aren’t interchangeable
3. b/c SHAPE of active site is unique

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5
Q

What do enzymes normally end in?

A
  • ase
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6
Q

What is another word for reactant in enzyme reactions?

A

Substrate

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7
Q

How can an enzymatic rxn be anabolic? (3)

A
  1. Endergonic & Synthesis Rxn
  2. Substrate is the Raw Material
  3. Bonds & larger molecules are formed

Ex: Dehydration Synthesis, Photosynthesis

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8
Q

What is the enzymatic reaction called when it is endothermic?

A

Anabolic

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9
Q

What makes an enzymatic reaction catabolic? (2)

A
  1. Exergonic & Breakdown Rxn
  2. Bonds & large molecules are broken down (into smaller building blocks)

Ex: Cellular Respiration & Hydrolysis

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10
Q

What is the enzymatic reaction called when it is exothermic?

A

Catabolic

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11
Q

Definition of Optimum Temperature

A

Temp. at which enzymes function at max. rate
(37°C)

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12
Q

Definition of Active Site (3)

A
  1. Site where substrate & enzyme touch
  2. Activates to create unstable bonds that need to be stabilized
  3. Enabling the catabolic & anabolic reactions
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13
Q

What are the three factors that determines whether the enzyme and substrate is compatible?

A
  1. Opposite Charges
  2. Shape
  3. Active Site Configuration
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14
Q

Definition of Induced Fit (2)

A
  1. When substrate binds to the activation site
  2. Enzyme slightly changes shape to fit substrate
    (Like a handshake!)
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15
Q

Definition of Competitive Inhibition (4)

How, Competes For, Result

A
  1. Substance mimics substrate’s shape
  2. Competes for binding site
  3. Blocks substrate from binding to AS
  4. Decreases enzyme activity & reaction
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16
Q

Definition of Noncompetitive Inhibition (3)

Definition, effect

A
  1. Inhibitor binds to allosteric site
  2. Enzyme’s shape is changed due to induced fit
  3. Substrate cannot bind w/ altered activation site
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17
Q

Noncompetitive Inhibition Analogy

Read Through

A

Someone (noncompetitive inhibitor) comes along and bends the keyhole out of shape. A key (substrate) might still fit in, but it can’t turn to unlock the door (catalyze the reaction).

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18
Q

Definition of the ES Complex

A

Substrate is binded to Enzyme

19
Q

What is Acidic?

PH Level & Contains

A

pH Level: 1 - 6.9
Contains more H+
Contains less OH -

20
Q

What’s Basic?

PH Level & Contains

A

pH Level: 7.1- 14
Contains less H+
Contains more OH -

21
Q

What’s Neutral?

PH Level & Contains

A

pH Level: 7
H+ = OH -

22
Q

What happens to the enzyme when the temperature increases past optimum temperature and decreases past optimum temperature? (5)

Decrease, Increase, Paragraph

A

Decreases: Metabolic Reactions Slow Down
Increases: Enzyme Denatures, Ceasing Function

  1. Changed Shape = Changed Function
  2. In secondary structure, breaks H - Bonds
  3. In tertiary structure, breaks H - Bonds, Disulfide Bonds, Ionic Bonds & Hydrophobic Interactions
  4. In quaternary structure, breaks all bonds as shown above
  5. Enzyme can’t combine w/ substrate
23
Q

What happens to the enzyme when the pH level increases past the optimum pH level and decreases past the the optimum pH level?

A

It denatures, so it will not perform its enzymatic reactions

  1. Changed Shape = Changed Function
  2. In secondary structure, breaks H - Bonds
  3. In tertiary structure, breaks H - Bonds, Disulfide Bonds, Ionic Bonds & Hydrophobic Interactions
  4. In quaternary structure, breaks all bonds as shown above
  5. Enzyme can’t combine w/ substrate
24
Q

Why can’t the enzyme function well when it the pH level and temperature changes?

(HINT: EXPLAIN HOW SHAPE CHANGES AND HOW IT CHANGES THE FUNCTION) (5)

A
  1. Changed Shape = Changed Function
  2. In secondary structure, breaks H - Bonds
  3. In tertiary structure, breaks H - Bonds, Disulfide Bonds, Ionic Bonds & Hydrophobic Interactions
  4. In quaternary structure, breaks all bonds as shown above
  5. Enzyme can’t combine w/ substrate
25
Q

How do you know where to locate the optimum temperature in a “function” graph and a “substrate concentration” graph?

A

Function: Peak
SC: Right before the line flattens

26
Q

Definition of Substrate Concentration (5)

Definition, Result, Explain

A
  1. Fixed amount of enzyme but increasing amount of substrate
  2. Rxn rate increases as SC increases
  3. Enzyme will be saturated with substrates (more production of products)
  4. Fully saturated enzymes don’t need more substrates
  5. Rate will no longer inrease & and level off
27
Q

Definition of Enzyme Concentration and Explain What Happens (3)

Definition, Result, Explain

A
  1. Fixed amount of substrate but increasing amount of enzymes
  2. Increases rxn rate as EC increase
  3. If all substrates are already binded to an enzyme, increasing enzyme won’t increase rate
28
Q

What’s an analogy about why increasing substrate and enzyme concentration will not speed up the reaction if it’s already fully saturated?

Read Through

A

When you first add more raw goods (substrates), the machines (enzymes) can process them faster and produce more products because there’s more work to be done. However, if you keep adding raw goods but don’t increase the number of machines, the machines will eventually reach their maximum capacity.

At this point, each machine is working as fast as it can, so adding more raw goods doesn’t increase production—there aren’t enough machines to process the extra material. Similarly, if you add more machines (enzymes) but don’t have enough raw goods (substrates), some machines will sit idle, and the reaction won’t speed up.

The production rate levels off when all machines are fully occupied, and no additional raw goods or machines can increase the output without increasing the other.

29
Q

Definition of Coenzymes (3)

Structure, Function

A
  1. Organic molecule attatches to an enzyme
  2. Required for enzyme function
  3. Allows Substrate to bind & necessary for rxn to occur
30
Q

Definition of Cofactors (3)

A
  1. Metal Ions attatch to enzyme (non - protein helpers)
  2. Attach to Enzyme
  3. Allows Substrate to Bind & Rxn to occur

Ex: Hemoglobin allows oxygen to attach to the blood

31
Q

Function of Inhibitors

A

Slow the rate of enzyme catalyzed reactions

32
Q

Definition of Irreversible Inhibitors (3)

Definition & Result

A
  1. Forms a covalent bond at active site
  2. Permanently blocks the substrate
  3. ENDS reaction
33
Q

Definition of Reversible Inhibitor (3)

Definition, Result, How to Overcome

A
  1. Forms a temporary bond at active site
  2. Slows reaction rate
  3. Effects can be overcome by increasing substrate concentration
34
Q

Definition of Metabolic Pathways

Read Through

A
  1. A series of enzyme-catalyzed reactions in a cell
  2. Convert substrates to products
35
Q

Definition of the Allosteric Enzyme (3)

A
  1. Enzyme that regulates its own activity
  2. By the binding of non - competitive inhibitors at the allosteric site
  3. Changes shape of the enzyme

(effectively allowing the enzyme to “self-regulate” in response to the cellular environment)
Enzymes that have shapes that can be altered by the binding of “signal” molecules to their surfaces

36
Q

Definition of Feedback Inhibition (4)

Definition, How & Why

A
  1. End product of metabolic pathway acts as an inhibitor
  2. Turns the reaction on/off
  3. Inhibits enzyme involved in initial stages
  4. Maintain sbalance by preventing overproduction & waste of resources
37
Q

Why does enzyme activity increase when pH increases? (4)

Read Through

A
  1. PH can change charge of the active site
  2. b/c AA can lose or gain H+ based on the pH
  3. When pH is at optimal value
  4. Active Site will be correctly ionized
38
Q

Why does enzyme activity increase when temperature increases? (3)

A
  1. Increase in molecule speed
  2. Increase in molecule collisions, overcoming activation energy
  3. More ES complex will form
39
Q

Is exergonic or endergonic reaction spontaneous? Why? (2)

A
  1. Exergonic
  2. No need for an input of energy, occurs naturally
40
Q

Definition of Activator and Inhibitor in terms of an allosterically regulated enzyme

A

Activator: Turns on the reaction (still binds to the non - active site)
Inhibitor: Turns off the reaction

41
Q

HOW do coenzymes and cofactors assist enzyme function? (3)

A
  1. Stabilizes 3D shape
  2. Maintains Active Sites
  3. Assists in the binding of ES
42
Q

Definition of Hydrolase

A

Enzyme that splits molecules through usage of water

43
Q

In data, how do competitive inhibitors affect chemical reactions?

A

Data shows it reduces the concentration of the enzyme

44
Q

What’s the lock and key theory for enzymes?

Read Through

A

Enzyme = Lock: The enzyme has a specific active site (like a lock).

Substrate = Key: The substrate has a shape that fits perfectly into the enzyme’s active site (like a key).

Advanced Biology (16 decks)

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