Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers Flashcards

1
Q

is a macromolecule that acts as a catalyst

A

enzyme

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2
Q

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

A

catalyst

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3
Q

Every chemical reaction between molecules involves both bond breaking and .

A

bond forming

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4
Q

To reach the contorted state where bonds can change, reactant molecules must absorb

A

energy from their surroundings.

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5
Q

When the new bonds of the product molecules form, energy is released as heat, and the molecules return to stable shapes with lower

A

energy than the contorted state.

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6
Q

The initial investment of energy for starting a reaction—the energy required to contort the reactant molecules so the bonds can break—is known as the

A

free energy of activation, or activation energy abbreviated Eᴀ

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7
Q

We can think of activation energy as the amount of energy needed to push the reactants to the top of an energy barrier, or uphill, so that the

A

“downhill” part of the reaction can begin.

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8
Q

Activation energy is often supplied by heat in the form of

A

thermal energy that the reactant molecules absorb from the surroundings

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9
Q

The absorption of thermal energy accelerates the reactant molecules, so they

A

collide more often and more forcefully.

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10
Q

When the molecules have absorbed enough energy for the bonds to break, the reactants are in an unstable condition known as the

A

transition state

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11
Q

learn Figure 8.13 Energy profile of an exergonic reaction.

A
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12
Q

Proteins, DNA, and other complex cellular molecules are rich in free energy and have the potential to

A

decompose spontaneously; that is, the laws of thermodynamics favor their breakdown

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13
Q

high temperature denatures proteins and

A

kills cells.

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14
Q

a process by which a catalyst (for example, an enzyme) selectively speeds up a reaction without itself being consumed.

A

catalysis

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15
Q

an enzyme cannot change the ∆G for a reaction; it cannot make an endergonic reaction

A

exergonic.

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16
Q

for any reaction to occur, even a downhill reaction, some energy must be

A

added to get the reaction going

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17
Q

this energy is needed to break bonds in the

A

reactant molecules

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18
Q

the energy needed to start a chemical reaction is called the

A

energy of activation (E sub A)

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19
Q

this required energy input represents a barrier that prevents even energy-releasing exergonic reactions from occurring without

A

some added energy

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20
Q

serves as a biological catalyst, increasing the rate of a reaction without being changed into a different molecule

A

an enzyme

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21
Q

an enzyme does not add energy to a reaction: it

A

speeds up a reaction by lowering the energy barrier

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22
Q

an enzyme is very selective, its three-dimensional shape allows it to act on specific molecules, referred to as the

A

enzyme’s substrates

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23
Q

as the substrates bind to the enzyme’s active site they are held in a position that facilitates the

A

reaction

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24
Q

this takes less activation energy than the

A

unaided reaction

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25
Q

product form and are

A

released

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26
Q

the enzyme emerges

A

unchanged from the reaction

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27
Q

because of the specific fit between enzyme and substrate, each enzyme can catalyze

A

one kind of reaction involving specific substrates

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28
Q

thousands of different enzymes may be required to carry out all of a

A

cells metabolic processes

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29
Q

The reactant an enzyme acts on is referred to as the

A

enzyme’s substrate

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30
Q

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

A

enzyme-substrate complex

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31
Q

While enzyme and substrate are joined, the catalytic action of the enzyme converts the substrate to the

A

product (or products) of the reaction

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32
Q

Most enzyme names end in

A

-ase.

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33
Q

most enzymes are proteins, and proteins are macromolecules with unique

A

three-dimensional configurations

34
Q

The specificity of an enzyme results from its shape, which is a consequence of its

A

amino acid sequence.

35
Q

is typically a pocket or groove on the surface of the enzyme where catalysis occurs

A

active site

36
Q

Usually, the active site is formed by only a few of the enzyme’s amino acids, with the rest of the protein molecule providing a framework that determines the

A

shape of the active site.

37
Q

The specificity of an enzyme is attributed to a complementary fit between the shape of its active site and the shape of the

A

substrate.

38
Q

enzymes (and other proteins) seem to “dance” between subtly different shapes in a

A

dynamic equilibrium, with slight differences in free energy for each “pose.

39
Q

As the substrate enters the active site, the enzyme changes shape slightly due to interactions between the substrate’s chemical groups and

A

chemical groups on the side chains of the amino acids that form the active site.

40
Q

The tightening of the binding after initial contact—called

A

induced fit

41
Q

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

A

chemical reaction.

42
Q

In most enzymatic reactions, the substrate is held in the active site by so-called weak interactions, such as

A

hydrogen bonds and ionic bonds.

43
Q

The R groups of a few of the amino acids that make up the active site catalyze the conversion of substrate to product, and the

A

product departs from the active site.

44
Q

The entire cycle happens so fast that a single enzyme molecule typically acts on about

A

1,000 substrate molecules per second

45
Q

although every enzyme performs a different reaction on different substrates they all go through the same general steps in accomplishing their reaction. these general steps include

A

substrate binding, formation of the enzyme-substrate complex, product formation and dissociation, and enzyme recovery

46
Q

like all catalysts, enzymes are unchanged by the

A

overall reaction

47
Q

first step in any enzymatic reaction is the

A

binding of the substrates by the enzyme

48
Q

the enzyme includes an active site that can accommodate the

A

size, shape, and electron configuration of its substrate or substrates

49
Q

according to the induced-fit model of enzyme-substrate interaction, a perfect fit does not form until the

A

enzymes and substrates bind to form an enzyme-substrate complex

50
Q

after the substrate has bound in the active site, the

A

enzyme-substrate complex is formed

51
Q

the shape of the enzyme may change to allow for an efficient chemical reaction, and amino acids may accept or donate protons or electrons to facilitate the

A

chemical reaction

52
Q

once the enzyme-substrate complex has formed and any reactive groups have moved to the right position, the reaction proceeds and products are

A

formed

53
Q

the product dissociate rapidly, leaving an empty

A

active site

54
Q

after the products leave the active site, the enzyme

A

returns to its original configuration

55
Q

any groups that donated or accepted protons or electrons are also

A

returned to their original state

56
Q

like all catalysts, the enzyme is unchanged by the

A

overall reaction

57
Q

Most metabolic reactions are reversible, and an enzyme can catalyze either the forward or the reverse reaction, depending on which direction has a negative

A

∆G

58
Q

This in turn depends mainly on the

A

relative concentrations of reactants and products

59
Q

The net effect is always in the direction of

A

equilibrium.

60
Q

Enzymes use a variety of mechanisms that

A

lower activation energy and speed up a reaction

61
Q

When there are two or more reactants, the active site provides a template on which the .

A

substrates can come together in the proper orientation for a reaction to occur between them

62
Q

The more substrate molecules that are available, the more frequently they access the active sites of the .

A

enzyme molecules

63
Q

there is a _______ to how fast the reaction can be pushed by adding more substrate to a fixed concentration of enzyme

A

limit

64
Q

As soon as the product exits an active site, another

A

substrate molecule enters

65
Q

At this substrate concentration, the enzyme is said to be ____________, and the rate of the reaction is determined by the speed at which the active site converts substrate to product.

A

saturated

66
Q

When an enzyme population is saturated, the only way to increase the rate of product formation is to

A

add more enzyme.

67
Q

Cells often increase the rate of a reaction by producing more

A

enzyme molecules.

68
Q

learn scientific skills exercise

A
69
Q

The activity of an enzyme—how efficiently the enzyme functions—is affected by general environmental factors, such as

A

temperature and pH.

70
Q

the rate of an enzymatic reaction increases with increasing temperature, partly because substrates collide with active sites more frequently when the

A

molecules move rapidly

71
Q

Above that temperature, however, the speed of the enzymatic reaction

A

drops sharply.

72
Q

Most human enzymes have optimal temperatures of about

A

35–40°C

73
Q

The thermophilic bacteria that live in hot springs contain enzymes with optimal temperatures of

A

70°C or higher

74
Q

The optimal pH values for most enzymes fall in the range of

A

pH 6–8, but there are exceptions.

75
Q

Many enzymes require nonprotein helpers for catalytic activity, often for chemical processes like electron transfers that cannot easily be carried out by the amino acids in proteins. These adjuncts, called _________ may be bound tightly to the enzyme as permanent residents, or they may bind loosely and reversibly along with the substrate.

A

cofactors

76
Q

The cofactors of some enzymes are inorganic, such as the metal

A

atoms zinc, iron, and copper in ionic form.

77
Q

If the cofactor is an organic molecule, it is referred to, more specifically, as a

A

coenzyme

78
Q

reduce the productivity of enzymes by blocking substrates from entering active sites.

A

competitive inhibitors

79
Q

watch and learn animation enzymes: competitive inhibition and animation enzymes: noncompetitive inhibition

A
80
Q

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

A

noncompetitive inhibitors

81
Q

they impede enzymatic reactions by binding to another part of the

A

enzyme