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AP Biology > Enzymes > Flashcards

Enzymes Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Define enzyme?

A

A protein biological catalyst that speeds up reactions,

  • Breaks down macromolecules,
  • Combines micromolecules
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2
Q

What is an active site?

A

The area is an enzyme that binds to a substrate

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3
Q

What is denaturing?

A

When an enzyme loses its shape from heat or PH change,
- This can be reversed by changing the environment back to optimum conditions because the shape of the enzyme is coded into the primary structure

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4
Q

What is induced fit?

A

The dynamic fit between the substrate and enzyme, both components modify their structure for ideal binding

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5
Q

What is a substrate?

A

The molecule on which the enzyme acts binds to the active site of an enzyme

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6
Q

What is kinetic energy?

A

The energy present in an object in motion

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7
Q

What is the lock and key method?

A

The model that shows the substrate fitting perfectly into an enzyme

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8
Q

Why does the rate of reaction increase in enzymes that are heated, but then reduce after a certain point?

A

With an increase in temperature, molecules move faster because there is more energy,

  • Increases the number of collisions between molecules and enzymes
  • Increases the amount of energy each molecule has so they have the required activation energy for the reaction,
  • Until temp rises too much and the enzyme denatures
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9
Q

What is the optimum PH in the stomach and small intestine?

A

Stomach - PH 2

Small Intestine - PH 7-8

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10
Q

What is the biochemical pathway?

A

A specific sequence of reactions where the product of one enzyme-catalyzed reaction becomes the substrate of the next enzyme-catalyzed reaction.

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11
Q

Why is it beneficial to stop a biochemical pathway?

A

AS a product becomes available in the environment, it is wasteful and unnecessary to continue making the product through enzyme catalyzing reactions.

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12
Q

How are biochemical pathways inhibited?

A
  • After the final stage of the pathway, the product goes back to the first enzyme in the biochemical pathway,
  • It then binds to the enzyme’s allosteric site, the enzyme undergoes a conformational change,
  • The change in shape causes a change in function, and the enzyme can no longer be used
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13
Q

What is allosteric inhibition?
Al-lost-eric
FMAB, Al literally lost his whole body lol

A

When a biochemical pathway is stopped by a final product binding to an allosteric site on the first enzyme, changing its conformation and preventing enzyme activity

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14
Q

What does anabolic mean? (anabolism in an enzyme)

A

Pathways that require an input of energy to synthesize complex molecules from simpler ones

  • Making up molecules, using inputted energy
  • Remember anabolic steroids build those PHAT arms
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15
Q

What is bioenergetics?

A

The study of energy flowing through living systems

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16
Q

What does catabolic mean? (Catabolism in an enzyme)

A

Pathways in which complex molecules are broken down into simpler ones

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17
Q

What is a coenzyme?

A

An organic molecule that helps the enzyme,

  • They can add or remove chemical groups from the substrate
  • Participate in many different reactions
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18
Q

What is a cofactor?

A

An inorganic ion that help enzymes

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19
Q

What is competitive inhibition?

A

A type of inhibition in which the inhibitor competes with the substrate molecule by binding to the active site of the enzyme,
- The active site is physically blocked and cannot be accessed by the substrate

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20
Q

What is feedback inhibition?

A

Allosteric inhibition,
- Using the product of a reaction sequence to inhibit the first enzyme by binding to it and changing the conformation of the enzyme, resulting in no function

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21
Q

What is metabolism?

A

The sum of chemical reactions that take place inside cells, including anabolism and catabolism

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22
Q

What is activation energy?

A

Necessary energy for reactions to occur

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23
Q

What is chemical energy?

A

Energy stored in chemical bonds and released when broken

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24
Q

What does endergonic mean?

A

Chemical reactions that require an input of energy

- Endothermic reactions but with energy not heat

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25
Q

What does enthalpy mean?

A

The total energy of a system

26
Q

What is entropy (S)?

A

The measure of randomness or disorder within a system

27
Q

What does exergonic mean?

A

Chemical reactions that release free energy

- Exothermic reactions but with energy

28
Q

What is free energy?

A

Energy available to do work

29
Q

What is heat energy?

A

Energy transferred from one system to another that is not work, energy of the motion of molecules or particles,

30
Q

What is potential energy?

A

Energy that has the potential to do work,

- Stored energy

31
Q

What is thermodynamics?

A

The study of energy and energy transfer involving physical matter

32
Q

What is the transition state?

A

High energy in an unstable state,

  • A form between the substrate and product,
  • Occurs during a chemical reaction, at the peak of the energy transfer
33
Q

For reactions to occur, what must happen to the potential energy?

A

It will decrease

34
Q

What is an example of work in biology?

A

Biosynthesis, molecules need energy to be built up

35
Q

What happens to energy change when heat is added to the system?

A
  • Increases
  • Less activation energy is required b/c the molecules are moving faster
  • More energy means a high rate of reaction, so an increased number of reactants can create products.
36
Q

What causes the activation energy barrier?

A

The transition state,

  • When the enzyme-substrate complex is held together in a strained manner,
  • The enzyme-substrate complex becomes unstable,
  • Energy is needed to break this strain and allow the reactants to become products easily after
37
Q

How do catalysts increase the rate of reaction?

A

Decreases the activation energy by creating another pathway for the reaction

38
Q

Why do enzymes not affect the energy of the products or the reactants?

A

Only a new pathway is created for the reaction so that it requires less energy, meaning more reactants can create more products with equal energy,
- This works in both directions of the reaction

39
Q

What are oxidation and reduction?

A
  • Oxidation is the loss of hydrogen
  • Reduction is gaining a hydrogen
    OILRIG
40
Q

How does an enzyme assist oxidation and reduction in NAD+?

A
  • A substrate and the NAD+ molecule enter binding sites of an enzyme,
  • The enzyme assists the substrate in transferring the hydrogen to the NAD+
  • The substrate is oxidized, the NAD is reduced to NADH
41
Q

What factors denature proteins?

A
  • Temperature
  • Concentration of H+ (PH)
  • High concentration of polar substances
  • Nonpolar substances
42
Q

What are the two biological catalysts in the human body?

A
  • Enzymes

- Ribozymes

43
Q

What is an enzyme-substrate complex?

A

The combination of a substrate and an enzyme due to the substrate binding to the enzymes active site

44
Q

What holds together the enzyme-substrate complex?

A
  • Hydrogen bonds
  • Electrical attratcion
  • Or temporary covenant bonding
45
Q

How is the reaction between an enzyme and a substrate written?

A 
E + S → ES → E + P
E = Enzyme
S = Substrate
ES = Enzyme-substrate complex
P = Product
46
Q

With what two methods do enzymes catalyze reactions?

A
  • Strain

- Substrate orientation

47
Q

How do enzymes “strain” substrates to catalyze reactions?

A

Bonds of the substrate are stretched, putting it in an unstable transitional state, which allows the bonds to be broken

48
Q

How does an enzyme use substrate orientation to catalyze reactions?

A

Substrates are brought together so that bonds can form

49
Q

How does an enzyme use chemical groups to catalyze a reaction?

A

The enzyme could replace or add R-groups to a substrate

50
Q

What is the induced fit model?

A

When an enzyme changes the shape of its binding site to accommodate a substrate

51
Q

What are prosthetic groups?

A

Non-Amino acid groups that permanently bind to their enzyme so can affect the function of the enzyme

52
Q

What does it mean for an enzyme to be saturated?

A

The enzyme is bound to a substrate

53
Q

When is the maximum rate of reaction in the presence of an enzyme?

A

When all enzymes are saturated

54
Q

How can we measure the rate of reaction in an enzyme?

A
  • Rate at which products are formed
  • Rate at which substrates disappeared
  • The reaction rate of the enzyme is taken by measuring the slope of the steepest part of the graph
55
Q

What is non-competitive inhibition?

A

When the substrate cannot access the active site because another substrate is bound to an allosteric site, changing the shape of the enzyme and its function

56
Q

Describe the process of glucose decomposition in aerobic respiration?

A
  • Glucose is the first substrate and is broken down into the final product of pyruvate,
  • The intermediate substrates between glucose (including glucose) and Pyruvate are oxidized, while NAD+ is reduced,
  • An electron and hydrogen are transferred from the substrate to NAD+ with the assistance of an enzyme to create a new substrate and NADH,
  • The NADH is then oxidized by transferring an electron to an O2 molecule which gets reduced to water, as it collects hydrogen floating around in the cell
  • The NADH reverts back to NAD+
  • The cycle restarts with the next substrate, which is the product of the last enzyme reaction.
57
Q

What is chemical potential energy?

A

Energy stored in the bonds in molecules

58
Q

What is the final electron acceptor?

A

The last molecule to be reduced in a sequence of enzyme reactions

59
Q

What type of reaction is aerobic respiration?

A
  • Exergonic

- Catabolic

60
Q

What is the coenzyme of aerobic respiration?

A

NAD+

AP Biology (19 decks)

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