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BIOL 241 > Topic 3: Enzymes > Flashcards

Topic 3: Enzymes Flashcards

1
Q

Most enzymes are…

A

Proteins

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2
Q

What is a protein?

A

Polypeptides folded into a 3D shapes

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3
Q

What does an Amino Acid have?

A
  • Amino group
  • Alpha/Central Carbon
  • R group (functional group)
  • Carboxyl Group
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4
Q

When Amino Acids are linked together they form?

A

Peptides

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5
Q

What is a Peptide Bond?

A
  • Forms through a dehydration reaction between 2 amino acids (H2O is formed from a Carboxyl and Amino group)
    O H
    || |
    C - N - ~
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6
Q

What is a Hydrophobic R-Groups

A
  • Water hating groups
  • When the R-group consists of non-polar bonds
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7
Q

What is a Hydrophilic R-Group?

A
  • Water-loving groups
    When the R-group consists of polar bonds
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8
Q

What is a peptide?

A

Polymer of amino acids

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9
Q

What is a Polypeptide?

A

Greater than 10 amino acids joined together

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10
Q

What is 1⁰ Primary Structure?

A

Polypeptide

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11
Q

What is a polypeptide in the 1⁰ Primary Structure?

A

A sequence of amino acids in the polypeptide

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12
Q

What is in the 2⁰ Secondary Structure:

A

Helices and Sheets

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13
Q

What do Helices do?

A
  • It is a part of the 2⁰ Secondary Structure
  • A regular repeat of H-bonds to stabilize the helix
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14
Q

What do sheets do?

A
  • It is a part of the 2⁰ Secondary Structure
  • The main chain stabilized into sheets through H-bonds
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15
Q

What is the 3⁰ Secondary Structure:

A

Hexokinase’s tertiary structure, the overall folded 3D shape of the protein which results from the organization of secondary structural regions relative to one another

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16
Q

What occurs in the 3⁰ Tertiary Structure:

A

The secondary structure is folded into the 3D shape of a single protein due to multiple levels of interaction between R-groups

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17
Q

What is the 4⁰ Quaternary Structure:

A

Multiple polypeptides folded into 3D shapes (sub-units) that interact with each other
e.g.
Homotrimer and Heterotrimer

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18
Q

What is the speed of most biological reactions?

19
Q

Why do glucose and ATP take a long time to produce a measurable product?

A
  • Bonds in both substrate molecules are stable
  • Energy is need to break the bonds
20
Q

What is Activation Energy (Ea)?

A
  • The energy required to get a reaction going
21
Q

What to label on an Energy by Reaction Pathway graph…

A
  • Reactants, transition state (maximum), and products, activation energy, and change in free energy
22
Q

What are the 3 ways to speed up a Chemical Reaction?

A
  • Increase temperature (more energy when colliding)
  • Increase concentrations (more often collisions)
  • Add a catalyst (enzyme or ribozyme)
23
Q

What does adding an enzyme to a reaction do?

A
  • Lowers the activation energy
  • Does not change the change in free energy
24
Q

Enzyme structure determines their…

25
What is an enzyme?
A large molecule, made up of one or more polypeptide chains, folded into specific 3D shapes, determined by the sequence of amino acids
26
What is an Active Site?
- A region that interacts (binds) with a specific substrate (reactant) (this changes the shape of the enzyme) - Some can bind more than one substrate
27
What is the Induced Fit Model
- Suggests that when a substrate binds to an enzyme, the enzyme changes shape to better fit the substrate, forming an enzyme-substrate complex. - This helps force the reactants into the transition state and lower the activation energy of the reaction
28
What influences how fast a cell can convert reactants to products (rate of enzyme kinetics)?
Temperature, concentration of substrate, enzyme concentration, pH
29
How do cells control/regulate enzyme kinetics?
Enzyme concentration, increase the concentration of substrate, inhibitors/activators
30
What happens to the reaction rate when the enzyme concentration increases?
The rate of reaction increases
31
What happens to the enzyme as substrate concentration increases?
The enzyme becomes saturated, and plateaus because it is working at max capacity
32
What does denaturation mean?
- Loss of protein structure - Partial or complete - Irreversible or reversible - Caused by heat or pH
33
What does inactivation mean?
- Loss of protein activity - Often a result of denaturation - Can be reversible or irreversible
34
What is a reversible competitive inhibitor?
- An inhibitor that is chemically like the substrate - Noncovalently binds to the enzyme at the active site (competes with the substrate for binding to the active site)
35
How does a molecule outcompete the other for a reversible competitive inhibitor?
- The molecule with the highest concentration
36
What does the graph of a reversible competitive inhibitor look like?
- The one with the inhibitor rate of reaction is slower, but eventually plateaus at the same point as the one without the inhibitor
37
What is a reversible non-competitive inhibitor?
- An inhibitor that is not chemically like the substrate - Inhibitor that noncovalently binds the enzyme at some other site on the enzyme (away from the active site)
38
How can you outcompete a noncompetitive inhibitor?
You can't, raising the concentrations of the substrate will not outcompete the inhibitor
39
What does the graph of a reversible noncompetitive inhibitor look like?
The reaction rate with the enzyme is lower and never reaches the maximum rate of reaction.
40
What is a regulatory (allosteric) enzyme?
- A regulatory allosteric enzyme is an enzyme with multiple parts and active sites that can change shape and activity when certain molecules bind to it. - More than one active site - Have a quaternary structure (subunits)
41
What does an allosteric activator do?
Binds to the enzyme, which will change the shape to a more active form
42
What does an allosteric inhibitor do?
Binds to the enzyme which will change the shape to a less active form.
43
What is feedback inhibition?
- The final product of a pathway inhibits an enzyme early in the pathway

BIOL 241 (6 decks)

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