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AP Bio > Ground Rules of Metabolism > Flashcards

Ground Rules of Metabolism Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Metabolism-

A

all of organism’s chemical processes

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2
Q

Participants in a metabolic reaction:

A

Reactants,Intermediate,Products

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3
Q

Reactants

A

substances that enter a reaction

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4
Q

Intermediate

A

any substance that forms during reaction

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5
Q

Products

A

substances produced or left at the end

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6
Q

Catabolic pathways

A

processes that release energy by breaking down complex substances into simpler substances

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7
Q

ex catabolic pathways

A

o Ex- cellular respiration, in which glucose is broken down toCO2 and water, releasing energy

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8
Q

Anabolic pathways-

A

consume energy to build complex substances from simpler ones

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9
Q

Anabolic pathways- ex

A

Ex- synthesis of proteins from amino acids

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10
Q

Energy

A

capacity to do work

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11
Q

Kinetic energy + ex

A

energy of motion. ex–Water, electrons, leg muscles, light

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12
Q

Potential energy + ex;

A

stored energy. Water behind a dam

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13
Q

measurement chemical energy

A

kcal

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14
Q

Chemical energy-

A

potential energy of molecules stored in bonds

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15
Q

Can energy be converted? Ex?

A

Energy can be converted from one form to another, ex- respiration turns chemical energy into kinetic energy (then glucose is broken down). Organisms secure energy from their environment and use it to perform energy-required processes.

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16
Q

Types of work performed in cell:

A

mechanical, transport, chemical

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17
Q

mechanical work

A

movement–muscle cell contraction, beating of cilia (little hairs in respiratory tract that sweep away dirt and dust caught in mucus)

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18
Q

Transport

A

active transport/electrochemical work. pumping of substances across membranes against the direction of spontaneous movement

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19
Q

Chemical work

A

powering reactions that do not occur spontaneously

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20
Q

Thermodynamics-

A

study of energy transformations that occur in a collection of matter

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21
Q

First Law of Thermodynamics

A

energy can be transferred and transformed, but it cannot be created or destroyed. Also known as law of conservation of energy`

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22
Q

Second Law of Thermodynamics-

A

with every energy transfer, entropy, or disorder increases. Energy tends to flow from concentrated to less concentrated forms.

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23
Q

spontaneous-

A

-reaction that doesn’t require energy

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24
Q

example 1 of SLoT

A

Example- energy in cells mainly comes from breaking the bonds in organic molecules. However, in every energy transfer, some energy is lost to surroundings as heat and can’t be recaptured

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25
Q

Exergonic reactions

A

reactions that have net release of G; spontaneous

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26
Q

Ex exergonic reactions

A

Ex- respiration- breaking down glucose will release energy stored in the sugar molecules (catabolic)

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27
Q

Endergonic reactions-

A

a reaction that has a positive delta G–requires net input of energy; non spontaneous

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28
Q

Ex endergonic reactions

A

Ex- photosynthesis (opposite of respiration)- producing sugar by absorbing energy from the sun (anabolic)

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29
Q

Are reactions reversible?

A

mostly— Most reactions are reversible- can run in forward or reverse direction

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30
Q

equilibrium

A

when forward and backward reactions occur at same rate

31
Q
  • ATP has the same structure as an RNA nucleotide, except…
A

3 phosphate groups, not 1

32
Q

Why is the triphosphate tail unstable (ATP)

A

because each phosphate has a negative charge so they repel each other–short lived energy molecule. Therefore, phosphates can break off by hydrolysis.

33
Q

phosphorylation

A

(ATP) after phosphates break off by hydrolysis, the phosphate group then breaks off and joins another molecule, priming that molecule for a reaction

34
Q

ATP +H2O –>

A

ADP + Pi (adenosine diphosphate, Pi=inorganic phosphate group)

35
Q

∆G of ATP

A

-7.3 kcal/mol

36
Q

When a phosphate group is removed from the ATP…

A

7.3kcal of energy is released. ATP can reform when ADP joins with an inorganic phosphate.

37
Q

Energy coupling

A

using the energy from the exergonic reactions to power endergonic ones; Cells usually use ATP as a coupling agent. By breaking down ATP and releasing energy, that energy can be used to power an endergonic reaction

38
Q

why enzymes are necessary

A

Spontaneous reactions may proceed on their own, but the rate could be very slow

39
Q

enzyme

A

catalyst that can make a reaction happen hundreds to millions of times faster than they would on their own/Protein molecules that bind substrates

40
Q

Activation energy (free energy of activation)-

A

minimum amount of energy that is required to get the reaction to the point that it can run on its own. - Even for exergonic reactions, the activation energy “bump” must be overcome in order for the reaction to occur. Enzymes help lower this activation energy.

41
Q

enzyme characteristics

A

Often end in –ase; named for what they act on; Folded in such a way that they have active sites

42
Q

substrates

A

reactants (enzymes)

43
Q

active sites

A

pockets or crevices (made up of a few amino acids) where the substrates bind and where specific reaction occurs. Each active site will only bind to one particular substrate-enzymes are specific

44
Q

How does an enzyme bonding a substrate lower the activationenergy?

A

In order for a reaction to occur, energy must be put in to put a substrate into a transition state- at this state, bonds can be broken or changes made. An enzyme will bind to a substrate, releasing energy. This energy will stabilize the transition state so that the reaction can occur.

45
Q

o The enzyme may help lower the activationenergy by:

A

Allowing two substrates to find each other Orienting the substrate in a way to favor a reaction Induced fit

46
Q

Induced fit

A

squeezing the substrate into an active site, although it may not be a perfect fit. If it is squeezed next to another molecule, it can move the substrate into the transition state

47
Q

enzyme-substrate complex

A
  • While the enzyme and substrate are temporarily bound together, the resulting structure is called an enzyme-substrate complex.
48
Q

post enzyme reaction

A

After the reaction, the product departs from the active site Enzyme can take another substrate (enzyme remains in original form)o Cycle happens fast- single enzyme converts ~ 1,000 substrate molecules per second enzyme wears out eventually

49
Q

Rate is dependent on…

A

concentration of substrate and enzymes–More substrate, higher rate. At some point, adding substrate won’t help because all the enzymes will be used up –> enzyme is saturated. At enzyme saturation, only way to increase rate is to add more enzyme

50
Q

4 Important Enzyme Features

A

Enzymes can’t change non-spontaneous reactions into spontaneous reactions- they simply speed up reactions that would happen on their own anyway2- Enzymes are not permanently used up in reactions- they can be reused repeatedly3- Same type of enzyme usually catalyzes the forward and reverse directions of reversible reactions4- Enzyme is “picky” about its substrates lock and key model

51
Q

Factors affecting enzyme activity

A

environmental, cofactors, enzyme inhibitors, allosteric reactions, Cooperativity

52
Q

temp (Factors affecting enzyme activity)

A

Usually, reaction rate increases with increasing temperature because the substrates collide with active sites more frequently when the molecules move rapidly At some point- temp is too high and it disrupts H bonds, ionic bonds, weak interactions so the protein/enzyme denatures Each enzyme has optimum temp- humans-37c

53
Q

pH

A

Most enzymes have optimal pH at 7

54
Q

Salt concentration

A

Most enzymes can’t tolerate saline (salty)environments because ions intefere w ionic bonds Exceptions- algae and bacteria inhabit pools with high salt conc

55
Q

cofactors

A

help at the active site or bring electrons or H+ ions or functional groups to the reaction, Are either metal ions or are coenzymes, Can be bound tightly to active sites permanently or diffuse throughout cytoplasm

56
Q

coenzymes

A

organic compounds if helping at active site–metal ions

57
Q

cofactors–ex of being bound tightly to active sites permanently

A

Ex- heme in catalase has an iron atom which speeds up thebreakdown of H2O2

58
Q

cofactors–Others may diffuse throughout the cytoplasm ex

A

NAD+ or NADP+–both bring H+ ions and electrons

59
Q

Enzyme Inhibitors-

A

chemicals can inhibit the action of specific enzymes

60
Q

Competitive inhibitors-

A

resemble the normal substrate molecule and competes for active site, reducing productivity of enzymes bc active site is blocked

61
Q

overcoming competitive inhibitors

A

can be overcome by increasing concentration of substrate

62
Q

Noncompetitive inhibitors-

A

bind to part of enzyme away from active site, causing the enzyme to change shape and making the active site unreceptive to the substrate

63
Q

Enzyme Inhibitors- ex

A

Examples: Pesticides (DDT and parathion) are inhibitors in nervous system Antibiotics are inhibitors of enzymes in bacteria (penicillin is inhibitor in bacteria of enzymes that build cell walls)

64
Q

Allosteric Regulation

A

Some enzymes have allosteric site- receptor site far from the active site.

65
Q

two choices for bonding at allosteric site–

A

either an activator or an inhibitor. Activators and inhibitors attach to enzyme by weak bonds,so activity of enzyme can change from moment to moment.

66
Q

If the allosteric site can accept an activator

A

when the activator binds, the active conformation of the enzyme is stabilized. When the activator leaves, the active site becomes inactive

67
Q

If the allosteric site can accept an inhibitor

A

when the allosteric site is free, the active form of the enzyme exists. When the inhibitor binds, the inactive form of the enzyme is stabilized with a nonfunctional active site

68
Q

goal of cellular respiration-

A

-produce ATP

69
Q

Cooperativity

A

Resembles allosteric activation- substrate molecules bind toenzyme and canstimulate other active sites to bind other substrates

70
Q

Feedback Inhibition

A

when a metabolic pathway is switched off by its end product–end product acts as an inhibitor of the enzyme within a pathway. Prevents cell from wasting chemical resources in synthesizing more than necessary

71
Q

ex Feedback Inhibition

A

Example- 5 steps in changing isoleucine from threonine, another amino acid. As isoleucine accumulates, it switches off its own synthesis by inhibiting the enzyme that catalyzes the first step of the pathway

72
Q

quantity v quality bc of thermodynamics

A

Therefore- quantity of energy in the universe is constant(always the same amount of energy), but quality isn’t. Organisms, however, become more organized because we take in energy to decrease our entropy (make things more ordered)

73
Q

Ex 2 SLoT

A

Other example- car uses chemical energy of gasoline and converts it into mechanical energy to move the car- but only 20 – 30 % is used. Other 70 – 80 % isreleased as heat

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