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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?

A

Slow

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…

A

Function

25
Q

What is an enzyme?

A

A large molecule, made up of one or more polypeptide chains, folded into specific 3D shapes, determined by the sequence of amino acids

26
Q

What is an Active Site?

A
  • 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
Q

What is the Induced Fit Model

A
  • 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
Q

What influences how fast a cell can convert reactants to products (rate of enzyme kinetics)?

A

Temperature, concentration of substrate, enzyme concentration, pH

29
Q

How do cells control/regulate enzyme kinetics?

A

Enzyme concentration, increase the concentration of substrate, inhibitors/activators

30
Q

What happens to the reaction rate when the enzyme concentration increases?

A

The rate of reaction increases

31
Q

What happens to the enzyme as substrate concentration increases?

A

The enzyme becomes saturated, and plateaus because it is working at max capacity

32
Q

What does denaturation mean?

A
  • Loss of protein structure
  • Partial or complete
  • Irreversible or reversible
  • Caused by heat or pH
33
Q

What does inactivation mean?

A
  • Loss of protein activity
  • Often a result of denaturation
  • Can be reversible or irreversible
34
Q

What is a reversible competitive inhibitor?

A
  • 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
Q

How does a molecule outcompete the other for a reversible competitive inhibitor?

A
  • The molecule with the highest concentration
36
Q

What does the graph of a reversible competitive inhibitor look like?

A
  • The one with the inhibitor rate of reaction is slower, but eventually plateaus at the same point as the one without the inhibitor
37
Q

What is a reversible non-competitive inhibitor?

A
  • 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
Q

How can you outcompete a noncompetitive inhibitor?

A

You can’t, raising the concentrations of the substrate will not outcompete the inhibitor

39
Q

What does the graph of a reversible noncompetitive inhibitor look like?

A

The reaction rate with the enzyme is lower and never reaches the maximum rate of reaction.

40
Q

What is a regulatory (allosteric) enzyme?

A
  • 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
Q

What does an allosteric activator do?

A

Binds to the enzyme, which will change the shape to a more active form

42
Q

What does an allosteric inhibitor do?

A

Binds to the enzyme which will change the shape to a less active form.

43
Q

What is feedback inhibition?

A
  • The final product of a pathway inhibits an enzyme early in the pathway

BIOL 241 (6 decks)

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