Campbell Biology: Chapter 8

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Chapter 8: An Introduction to Metabolism
updated 4 years ago by Amber_Ares
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1

Which term most precisely describes the cellular process of breaking down large molecules into smaller ones?

Catabolism

2

Which metabolic process can occur without a net influx of energy from some other process?

Cellular Respiration

3

Catabolic Pathway

A metabolic pathway that releases energy by breaking down complex molecules to simpler molecules.

4

Catabolism is to anabolism, as ______ is to ______.

A) exergonic; spontaneous

B) exergonic; endergonic

C) free energy, entropy

D) work; energy

E) entropy, enthalpy

exergonic; endergonic

5

Anabolic Pathway

A metabolic pathway that consumes energy to synthesize a complex molecule from simpler molecules.

6

Kinetic Energy

Energy can be associated with the relative motion of object.

7

Thermal Energy

Kinetic energy associated with the random movement of atoms or molecules.

8

Heat

Thermal energy transferred from one object to another.

9

Potential Energy

Energy that matter possesses because of its location or structure.

10

Chemical Energy

The potential energy available for release in a chemical reaction.

11

First Law of Thermodynamics

Energy can be transferred or transformed but neither can be created or destroyed.

12

Second Law of Thermodynamics

Every Energy transfer or transformation increases the disorder (entropy) of the universe.

13

Thermodynamics

The study of energy transformation that occur in a collection of matter.

14

Entropy

A thermodynamic quantity representing the unavailability of a system's thermal energy for conversion into mechanical work, often interpreted as the degree of disorder or randomness in the system.

15

Spontaneous Process

The time-evolution of a system in which it releases free energy (usually as heat) and moves to a lower, more thermodynamically stable energy state.

16

Consume energy to build up polymers from monomers

Anabolic Pathways

17

Living organisms increase in complexity as they grow, resulting in a decrease in the entropy of an organism. How does this relate to the Second Law of Thermodynamics?

As a consequence, growing organisms cause a greater increase in entropy in their environment than than the decrease in entropy associated with their growth.

18

Whenever energy is transformed, there is always an increase in the...

entropy of the universe

19

Second Law of Thermodynamics

Every chemical reaction must increase the total entropy of the universe

20

Type of reaction that would decrease the entropy within a cell

Anabolic Reaction

21

What is an example of potential energy rather than kinetic?

A molecule of glucose

22

Metabolism consists of all the energy transformation reactions in an organism.

True

23

The energy in a molecule* that is available for conversion to some other form. All molecules* have an inherent free energy.

Free energy

24

The difference in free energy between two molecules or “states.”

Free energy change (DG)

25

A+B→C+D

Example: glucose + fructose --> sucrose and H2O.

Free energy change

26

If DG < 0, chemical reaction is

Exergonic

27

If DG > 0, chemical reaction is

Endergonic

28

Requires input of energy. Cannot occur unless energy from some other source is added.

Endergonic

29

Cells carry out endergonic reactions by _______ them to a more strongly exergonic reaction.

Coupling

30

What is the most common exergonic reaction

ATP hydrolysis

31

An exergonic reaction or process is used to drive an endergonic reaction or process.

Energy coupling

32

Typical nucleotide with 3 phosphates attached

ATP (Adenosine Triphosphate)

33

Terminal phosphate is removed, producing ADP and Pi (inorganic phosphate)

ATP hydrolysis

34
  • Overcoming a barrier to start an exergonic reaction
  • Energy must be added to break bonds before others are formed.
  • A common non‐catalytic way to overcome activation energy (EA) is heat

Activation energy

35
  • A substance that accelerates a chemical reaction without being changed by it.
  • Act by lowering the activation energy, so that it is not a barrier under cellular conditions.

Catalyst

36
  • Accelerate the rates of exergonic chemical reactions by lowering the activation energy.
  • Cannot catalyze endergonic reactions

Ezyme

37

How is cellular metabolism regulated?

Enzymes

38
  • All biochemical reactions are exergonic.
  • Most exergonic reactions require catalysis to overcome the activation energy.

True

39

Breakdown of glucose to make ATP

Catabolic

40

Synthesis of macromolecules from smaller subunits.

Anabolic

41

Usually proteins

Enzymes

42

Cavity where chemical reaction takes place

Active site

43

Change in protein folding tightens fit around substrate after binding

Induced fit

44
  1. substrate(s) bind in active site
  2. enzyme undergoes slight change in 3D structure (induced fit)
  3. chemical reaction takes place
  4. product(s) released

Steps in catalysis

45

Enzymes lower the activation energy by:

  • acting as a template to bring reactive groups into proximity
  • straining bonds & stabilizing transition state
  • providing microenvironment to chemical reaction
  • participating directly in chemical reaction
46

Cofactor

Non‐protein molecule required for catalysis

47

Coenzyme

Organic molecule that acts as cofactor (subset of “cofactor”)

48

Competitive inhibition

A molecule that is similar in shape to the substrate binds to and blocks the active site.

49

Noncompetitive regulation

Molecule binds to a site other than the active site and inhibits or promotes catalysis

50

Allosteric site

Site to which regulator binds. Not the active site.

51

Binding of a molecule...

induces a change in conformation. Change in conformation changes shape of active site.

52

Conformations

Proteins exist in 2 or more alternative, slightly different 3D shapes

53

Can activate (upper) or be inhibitory (lower).

Allosteric regulation

54

Cooperativity

Occurs in enzymes w/ more than one subunit. Binding of one substrate molecule increases the stability of the active conformation.

55

Feedback inhibition

A “downstream” product inhibits an earlier step in a biochemical pathway.

56

Phosphorylated Intermediate

The recipient molecule with the phosphate group covalently bonded to it

57

Substrate

The reactant an enzyme acts on

58

The enzyme binds to its substrate (or substrates, when there are two or more reactants), forming a(n)

Enzyme-substrate complex

59

As the substrate enters the active site...

The enzyme changes shape slightly due to interactions between the substrate's chemical groups and the chemical groups on the side chains of the amino acids hat form the active site.

60

Noncompetitive inhibitors

Do not directly compete with the substrate to bind to the enzyme at the active site.

61

In cells, what is usually the immediate source of energy for an endergonic reaction?

ATP

62

What is the fate of the phosphate group that is removed when ATP is converted to ADP?

It is acquired by a reactant in an endergonic reaction.

63
card image

In this reaction _____.

the products have less potential energy than the reactants

64

How does an enzyme increase the rate of the chemical reaction it catalyzes?

An enzyme reduces the free energy of activation (EA) of the reaction it catalyzes.

65

Sucrose is a disaccharide, composed of the monosaccharides glucose and fructose. The hydrolysis of sucrose by the enzyme sucrase results in

breaking the bond between glucose and fructose and forming new bonds from the atoms of water.

66

Zinc, an essential trace element for most organisms, is present in the active site of the enzyme carboxypeptidase. The zinc most likely functions as a(n)

cofactor necessary for enzyme activity.

67
card image

What best describes this reaction?

The amount of free energy released as a result of the catalyzed reaction is indicated by "d."

68

A series of enzymes catalyze the reaction X→Y→Z→A. Product A binds to the enzyme that converts X to Y at a position remote from its active site. This binding decreases the activity of the enzyme.

Substance A functions as a(n)...

Allosteric inhibitor

69

Some of the drugs used to treat HIV patients are competitive inhibitors of the HIV reverse transcriptase enzyme. Unfortunately, the high mutation rate of HIV means that the virus rapidly acquires mutations with amino acid changes that make them resistant to these competitive inhibitors. Where in the reverse transcriptase enzyme would such amino acid changes most likely occur in drug-resistant viruses?

In or near the active site