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Biology 1 > Chapter 8: An Introduction to Metabolism > Flashcards

Chapter 8: An Introduction to Metabolism Flashcards

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AP® Biology flashcards
1
Q

is a miniature chemical factory where
thousands of reactions occur

A

the living cell

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2
Q

extracts energy stored in sugars
and other fuels

A

cellular respiration

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3
Q

Cells apply this energy to perform work

A

the energy produced for cellular respiration

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4
Q

is the totality of an organism’s chemical reactions

A

metabolism

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5
Q

is an emergent property of life that arises from orderly interactions between molecules

A

metabolism

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6
Q

begins with a specific molecule and ends with a product

A

metabolic pathway

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7
Q

release energy by breaking down complex molecules into simpler compounds

A

catabolic pathways

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8
Q

an example of catabolic pathways is

A

Cellular respiration, the breakdown of glucose
in the presence of oxygen,

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9
Q

consume energy to build
complex molecules from simpler ones

A

anabolic pathways

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10
Q

example of anabolic pathways

A

the synthesis of protein from amino
acids

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11
Q

is the study of how energy flows
through living organisms

A

bioenergetics

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12
Q

is the capacity to cause change

A

energy

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13
Q

Energy associated with motion

A

kinetic energy

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14
Q

is the kinetic energy associated with
random movement of atoms or molecules

A

thermal energy

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15
Q

is thermal energy in transfer between objects

A

heat

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16
Q

is energy that matter possesses
because of its location or structure

A

potential energy

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17
Q

is potential energy available for release in a chemical reaction

A

chemical energy

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18
Q

is the study of energy
transformations

A

thermodynamics

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19
Q

is unable to exchange energy or
matter with its surroundings

A

isolated system

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20
Q

energy and matter can be
transferred between the system and its surroundings

A

open system

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21
Q

what kind of systems are organisms

A

open

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22
Q

proceeds with a net release of free energy and is spontaneous

A

exergonic reaction

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23
Q

absorbs free energy from its surroundings and is non spontaneous

A

endergonic reactions

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24
Q

what happens to reactions in closed systems

A

eventually reach equilibrium and can then do no work

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25
Q

what is special ab metabolism in life

A

it is never at equilibrium

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26
Q

three main kinds of work

A

chemical
transport
mechanical

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27
Q

pushing endergonic reactions

A

chemical work

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28
Q

pumping substances against the direction of spontaneous movement

A

transport work

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29
Q

contraction of muscle cells

A

mechanical work

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30
Q

how cell manage energy resources

A

energy coupling

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31
Q

the use of an exergonic process
to drive an endergonic one

A

energy coupling

32
Q

most energy coupling is meditated by what

A

ATP

33
Q

the chemical breakdown of a compound due to reaction with water.

A

hydrolysis

34
Q

how is cellular work powered?

A

hydrolysis of ATP

35
Q

what can be used to drive an endergonic reaction

A

the energy from the exergonic reaction of ATP hydrolysis

36
Q

transferring a phosphate group to some other
molecule, such as a reactant

A

phosphorylation

37
Q

how does ATP drive endergonic reactions?

A

phosphorylation

38
Q

the molecule that receives the phosphate group is called

A

phosphorylated intermediate

39
Q

is a renewable resource that is regenerated by
addition of a phosphate group to adenosine
diphosphate ()

A

ATP

40
Q

what regenerates ATP?

A

addition of a phosphate group to adenosine
diphosphate (ADP) (phosphorylate - ing the ATP)

41
Q

where does the energy come to phosphorylate ATP come from

A

catabolic reactions

42
Q

is a chemical agent that speeds up a
reaction without being consumed by the reaction

A

catalyst

43
Q

is a catalytic protein

A

enzyme

44
Q

Every chemical reaction between molecules involves what

A

bond breaking and bond forming

45
Q

The initial energy needed to start a chemical
reaction is called the free energy of activation, or

A

activation energy (EA)

46
Q

often supplied in the form of
thermal energy that the reactant molecules absorb
from their surroundings

A

activation energy (EA)

47
Q

speed up specific reactions by lowering the EA barrier

A

catalysis

48
Q

hasten reactions that would occur
eventually

A

enzymes

49
Q

The reactant that an enzyme acts on is called the enzyme’s

A

substrate

50
Q

The enzyme binds to its substrate, forming an

A

enzyme-substrate complex

51
Q

example of a enzyme

A

sucrase

52
Q

how is activation energy often supplied

A

thermal energy

53
Q

how do catalysis speed up specific reactions

A

by lowering the activation energy barrier

54
Q

is the region on the enzyme where
the substrate binds

A

active site

55
Q

brings chemical groups of
the active site into positions that enhance their ability
to catalyze the reaction

A

induced fit of a substrate

56
Q

The active site can lower an EA barrier by what

A

orienting substrates correctly
straining substrate bonds
providing a favorable microenvironment
covalently bonding to the substrate

57
Q

how can the rate of enzyme-catalyzed reaction can be sped up

A

increasing substrate

58
Q

When all enzyme molecules have their active sites engaged, the enzyme is what

A

saturated

59
Q

how do you speed up a saturated reaction rate

A

adding more enzyme

60
Q

An enzyme’s activity can be affected by

A
  • general environmental factors, such as
    temperature and pH
  • chemicals that specifically influence the
    enzyme
61
Q

are nonprotein enzyme helpers

A

cofactors

62
Q

An organic cofactor is called a

A

coenzyme

63
Q

bind to the active site
of an enzyme, competing with the substrate

A

Competitive inhibitors

64
Q

bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective

A

Noncompetitive inhibitors

65
Q

examples of inhibitors

A

toxins, poisons,
pesticides, and antibiotics

66
Q

Chemical chaos would result if what

A

a cell’s metabolic pathways were not tightly regulated

67
Q

may either inhibit or stimulate an enzyme’s activity

A

Allosteric regulation

68
Q

occurs when a regulatory molecule binds to a protein at one site other than the enzyme’s active site and affects the protein’s
function at another site

A

Allosteric regulation

69
Q

most allosterically regulated enzymes are made from

A

polypeptide subunits

70
Q

stabilizes the active form of the enzyme

A

The binding of an activator

71
Q

stabilizes the inactive form of the enzyme

A

The binding of an inhibitor

72
Q

is a form of allosteric regulation that
can amplify enzyme activity

A

cooperativity

73
Q

what is the exception for cooperativity

A

the substrate itself is the regulator and regulation is induced by binding in one of the
active sites

74
Q

how is cooperativity allosteric

A

because binding by a substrate to one active site affects catalysis in a different active site

75
Q

the end product of a
metabolic pathway shuts down the pathway

A

feedback inhibition

76
Q

prevents a cell from wasting chemical resources by synthesizing more product
than is needed

A

Feedback inhibition

Biology 1 (18 decks)

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