Enzymes Flashcards

1
Q

What is an enzyme?

A

Biological catalyst that increases rate of reaction that remains unchanged when the reaction is complete

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2
Q

What is metabolism?

A

Metabolism is the sum of all chemical reactions that occur in living organisms.

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3
Q

What are the roles of enzymes in metabolism?

A
  1. The conversion of food molecules to energy to run cellular processes.
  2. The conversion of food molecules to building blocks for proteins, lipids, nucleic acids, and carbohydrates.
  3. The elimination of nitrogenous wastes.
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4
Q

What do metabolic reactions do?

A

Allow organisms to grow and reproduce, maintain their structures, and respond to their environments.

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5
Q

What are anabolic reactions?

A

A part of metabolism - anabolism. 1. Larger molecules are built up from smaller molecules (condensation). 2. Usually require energy.

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6
Q

What are catabolic reactions?

A

A part of metabolism - catabolism. 1. Larger molecules are broken down into their smaller subunits (hydrolysis). 2. Usually release energy.

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7
Q

What are chemical reactions of metabolism?

A

Organized into linear metabolic chains or cyclic metabolic pathways.

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8
Q

How do chemical reactions occur in nature?

A
  1. Do not occur spontaneously. 2. If they occur, the rate of reaction is very low.
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9
Q

how do enzymes allow metabolic reactions to occur?

A
  1. Rapidly. 2. At a constant rate. 3. Under physiological conditions.
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10
Q

What are intracellular enzymes?

A

Enzymes that catalyze reactions inside cells.

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11
Q

What are extracellular enzymes?

A

Enzymes that are secreted from cells and catalyze reactions outside cells.

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12
Q

What is the specificity of enzymes and what is the cause of this?

A

Enzymes have high specificity due to their active sites.

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13
Q

What is the active site?

A
  1. Made up of specific amino acids. 2. Consists of 2 parts: Binding region and Catalytic region.
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14
Q

How does the active site work?

A
  1. Binds to the substrate with hydrogen bonds, hydrophobic interactions, or ionic bonds. 2. Has a precise 3D shape that is complementary to the substrate. 3. An enzyme will catalyze only one reaction.
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15
Q

What is activation energy and what do enzymes do?

A

Activation energy is the amount of kinetic energy needed to start a chemical reaction. Enzymes lower the activation energy.

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16
Q

What is the mode of action for an enzyme?

A

The function of an enzyme primarily depends on its 3D shape. The active site brings the substrates into physical closeness and the correct orientation for the reaction to take place.

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17
Q

How are enzymes globular proteins?

A

Non-polar hydrophobic R groups point into the center of the molecule, while polar hydrophilic R groups are located on the outside.

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18
Q

How are each protein structure in the enzyme involved in specificity?

A
  1. Primary - Sequence of amino acids determines the active site. 2. Secondary - Alpha and Beta pleated sheets position R groups. 3. Tertiary - Folding orients R groups for bonding. 4. Quaternary - Links between polypeptide chains alter enzyme properties.
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19
Q

What does a chemical reaction need to proceed?

A

The reactant molecules need kinetic energy equal to or greater than the activation energy and an input of energy.

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20
Q

What do enzymes do to a chemical reaction?

A
  1. Lower the activation energy. 2. Causes improbable reactions to occur. 3. Increases the rate of plausible reactions.
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21
Q

What happens to an enzyme after use?

A

It is not consumed or altered by the reaction.

22
Q

What is altered and not by an enzyme in a chemical reaction?

A

Reactant (substrate) energy and product energy remain the same; only activation energy is lowered by the enzyme.

23
Q

Why do we need enzymes?

A

Chemical reactions in nature are normally too slow to maintain life.

24
Q

What is the lock and key hypothesis?

A

The active site is a perfect fit for a specific substance.

25
What happens after enzyme and substrate bind in lock and key hypothesis?
Form the enzyme-substrate complex, the substrate is raised in energy to a transition state.
26
What is the induced fit hypothesis?
The active site and substrate are not exactly complementary.
27
What is the process of the induced fit hypothesis?
1. The arrangement of amino acids matches parts of the substrate. 2. Active site changes shape when the enzyme-substrate complex forms. 3. Amino acids in the catalytic region place stresses on the substrate.
28
How can the rate of an enzyme catalyzed reaction be found?
The rate can be studied by measuring the rate of substrate disappearance or product formation.
29
Why is it possible for us to measure the rate of an enzyme-catalyzed reaction?
Enzyme-catalyzed reactions occur at very high rates.
30
How is catalase used in enzyme catalyzed reactions?
Catalase catalyzes the breakdown of hydrogen peroxide into water and oxygen.
31
What is the process of catalase catalyzing hydrogen peroxide?
Reaction begins very quickly, releasing many O2 bubbles.
32
What is the start of an enzyme catalyzed reaction called?
The rate is called the initial rate of reaction.
33
How can a colorimeter be used to measure the progress of enzyme-catalyzed reactions?
1. Obtains a quantitative measurement of color intensity. 2. Measures the amount of light absorbed by a colored liquid.
34
Why use a colorimeter?
Improves the reliability of results in experiments involving color changes.
35
Do enzyme catalyzed reactions vary with temperature?
Yes, low temperatures slow movement and high temperatures increase reaction rates.
36
What is the process of denaturation of an enzyme due to high temps?
Partial denaturation occurs first, followed by complete denaturation where substrates no longer fit.
37
What is pre-incubation?
Using a pre-heated water bath to bring enzyme and substrate solutions to the same temperature.
38
What is pH?
The measure of the concentration of H+ ions in solution.
39
How does pH affect enzyme catalyzed reactions?
Hydrogen ions can disrupt ionic bonds and change enzyme structure, affecting substrate binding.
40
Can denaturation by pH be reversed?
Denaturation by changes in pH is normally reversible if the optimum pH is restored.
41
What does amylase do?
Breaks down starch into maltose, found in saliva with a pH of 7.
42
What does trypsin do?
Trypsin is a protease found in the small intestine where the optimum pH is 7.5-8.
43
What are buffer solutions?
Buffer solutions maintain a particular pH during reactions.
44
What is a competitive inhibitor and what does it do?
Molecules that resemble the substrate and block the active site.
45
What are non-competitive inhibitors and what does it do?
Inhibitors that bind to an allosteric site, causing a conformational change in the active site.
46
Why are enzymes inhibited?
To control chemical reactions and keep metabolic pathways balanced.
47
What is end-product inhibition?
The final product of a metabolic pathway acts as an inhibitor.
48
Can denaturation by temperature be reversed?
Denaturation by temperature is irreversible.
49
What is the temperature coefficient Q10 of a reaction?
The rate of reaction approximately doubles for every 10 degrees increase in temperature.
50
What is the optimum temperature?
The temperature at which an enzyme catalyzes a reaction at the maximum rate.
51
How does substrate concentration and enzyme activity work?
Initially low rates of reaction increase with substrate concentration until all active sites are full.
52
How does enzyme concentration and enzyme activity work?
The reaction rate increases with increased enzyme concentrations.