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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?

A

Speed up the rate of a chemical reaction by lowering the activation energy

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2
Q

Why can enzymes be reused over and over again? (4)

A
  1. After a chemical reaction
  2. Enzymes are not changed
  3. Enzymes are not used up
  4. Small amount can catalyze many reactions
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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? (4)

A
  1. Yes
  2. Each enzyme can only catalyze one substance
  3. Isomers’ enzymes are not interchangeable
  4. This is because the SHAPE of the active site varies
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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

What makes an enzymatic reaction anabolic? (6)

A
  1. Endergonic/Endothermic Reaction
  2. Synthesis Reactions
  3. Substrate - Raw Material
  4. Forms bonds
  5. Makes larger molecules
  6. 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? (4)

A
  1. Exergonic/Exothermic Reaction
  2. Breakdown Reactions
  3. Takes large molecules and breaks it down into smaller building blocks
  4. 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 (2)

A
  1. The temperature at which enzymes function at its maximum rate
  2. 37 degrees celsius
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12
Q

Definition of Active Site (3)

A
  1. Where the substrate touches the enzyme
  2. Activates to create unstable bonds
  3. Performs 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 (3)

A
  1. When a substrate binds to an enzyme’s activation site
  2. Enzyme will slightly changes shape to fit the substrate
  3. Like a handshake!
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15
Q

Definition of Competitive Inhibition (4)

Definition, effect

A
  1. A substance mimics the substrate (shape)
  2. Competes for the binding of a. site
  3. Inhibitor blocks substrate from binding
  4. Decreases enzyme activity
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16
Q

Definition of Noncompetitive Inhibition (3)

Definition, effect

A
  1. Inhibitor binds to enzyme other than the active site
  2. Due to induced fit, enzyme’s shape is changed
  3. Substrate cannot bind with activation site and start the reaction
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17
Q

Noncompetitive Inhibition Analogy

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

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19
Q

What is Acidic?

A

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

20
Q

What’s Basic?

A

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

21
Q

What’s Neutral?

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?

A

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

  1. Changes Shape, which Changes Function
  2. In secondary structure, breaks H - Bonds
  3. In tertiary structure, breaks H - Bonds, Disulfide Bonds, Ionic Bonds and Hydrophobic Interactions
  4. In quaternary structure, breaks all bonds as shown above
  5. So, enzyme cannot combine with the 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. Changes Shape, which Changes Function
  2. In secondary structure, breaks H - Bonds
  3. In tertiary structure, breaks H - Bonds, Disulfide Bonds, Ionic Bonds and Hydrophobic Interactions
  4. In quaternary structure, breaks all bonds as shown above
  5. So, enzyme cannot combine with the 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. Changes Shape, which Changes Function
  2. In secondary structure, breaks H - Bonds
  3. In tertiary structure, breaks H - Bonds, Disulfide Bonds, Ionic Bonds and Hydrophobic Interactions
  4. In quaternary structure, breaks all bonds as shown above
  5. So, enzyme cannot combine with the 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 after the lines builds up and right before the line flattens

26
Q

Definition of Substrate Concentration and Explain What Happens (4)

A
  1. Fixed amount of enzyme but increasing amount of substrate
  2. Increase in rate of reaction (more production of products) as substrate concentration increases
  3. Enzyme will become saturated with substrates
  4. If there’s fully saturated enzymes, increasing substrate won’t increase rate and level off
27
Q

Definition of Enzyme Concentration and Explain What Happens (3)

A
  1. Fixed amount of substrate but increasing amount of enzymes
  2. Increases rate of reaction (more production of products) as enzymes 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?

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 (5)

Function, Characteristic, How

A
  1. Increases rate of enzyme reactions
  2. Organic molecule
  3. Required for enzyme to work
  4. Attach to Enzyme
  5. Allows Substrate to Bind & Rxn to occur
30
Q

Definition of Cofactors (4)

A
  1. Metal Ion Substances
  2. Non - Protein Helpers
  3. Attach to Enzyme
  4. Allows Substrate to Bind & Rxn to occur

Ex: Hemoglobin allows oxygen to attach to the blood

31
Q

Definition of Inhibitors

A

Slow the rate of enzyme catalyzed reactions

32
Q

Definition of Irreversible Inhibitors (3)

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

Definition of Reversible Inhibitor (3)

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

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

Does adding H+ ions increase or decrease the rate of reaction?

A

Decrease, because ph will be lowered

36
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
    Enzymes that have shapes that can be altered by the binding of “signal” molecules to their surfaces
37
Q

Definition of Feedback Inhibition (5)

A
  1. Product acts as the inhibitor
  2. For enzyme in the beg. of metabolic pathway
  3. Maintains the balance metabolic pathways
  4. By avoiding overproduction and waste
  5. Turns reactions on/off
38
Q

Why does enzyme activity increase when pH increases?

A
  1. Because it is getting closer to the enzyme’s optimal range
  2. PH can also change the charge, because AA can lose or gain H+ based on the pH
  3. This affects the active site’s charge
  4. Closer the pH is to the optimal value
  5. AS will be correctly ionized
  6. Allowing the Substrate to bind
39
Q

Why does enzyme activity increase when temperature increases?

A
  1. Increase in molecule speed
  2. Increase in molecule collisions, overcoming Act. Energy
  3. More ES complex will form
40
Q

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

A
  1. Exergonic
  2. No need for an input of energy, occurs naturally
41
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

42
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
43
Q

Definition of Hydrolase

A

Enzyme that splits a molecule using h2o

44
Q

HOW do competitive inhibitors affect chemical reactions?

A

It SEEMS like it reduces the concentration of the enzyme

45
Q

What’s the lock and key theory for enzymes?

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 (15 decks)

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