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Biology Olympiad > Chapter 8: Metabolism > Flashcards

Chapter 8: Metabolism Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Metabolism

A

all of an organism’s chemical reactions

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2
Q

metabolic pathway

A

specific molecule is altered in a series of defined steps to form a specific product. each step is catalyzed by a specific enzyme

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3
Q

catabolic pathway

A

metabolic pathway that breaks down molecules and releases energy

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4
Q

anabolic pathway

A

metabolic pathway that builds complex molecules and consumes energy

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5
Q

kinetic energy

A

energy of motion

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6
Q

thermal energy

A

energy associated with random movement of atoms/molecules

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7
Q

potential energy

A

energy due to location or structure

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8
Q

chemical energy

A

potential energy available for release in a chemical reaction

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9
Q

thermodynamics

A

study of energy transformations in a collection of matter

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10
Q

isolated system

A

unable to exchange matter/energy with surroundings

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11
Q

open system

A

energy and matter can be exchanged with surroundings (ex: organisms)

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12
Q

first law of thermodynamics

A

energy can be transferred and transformed, but it cannot be created or destroyed (principle of conservation of energy)

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13
Q

entropy

A

measure of disorder/randomness

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14
Q

heat

A

thermal energy. can be used for work only when heat flows from a warm to a cold location.

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15
Q

second law of thermodynamics

A

every energy transfer or transformation increases the entropy of the universe

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16
Q

spontaneous process

A

process that occurs without input of energy and approaches equilibrium. ∆G must be negative (not 0).

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17
Q

free energy

A

portion of system’s energy that can perform work when temperature and pressure are uniform throughout the system (like a cell). also a measure of instability

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18
Q

∆G equation

A

∆G = ∆H - T∆S

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19
Q

equilibrium

A

state of maximum stability. free energy decreases as systems approach equilibrium.

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20
Q

exergonic reaction

A

spontaneous; proceeds with net release of free energy (-∆G)

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21
Q

endergonic reaction

A

nonspontaneous; absorbs free energy from surroundings

22
Q

energy coupling

A

use of exergonic reaction to drive endergonic reaction

23
Q

ATP

A

3 phosphate groups (negative charge), ribose sugar, and adenine.

24
Q

ATP hydrolysis

A

terminal phosphate bond of ATP is broken with water, resulting in inorganic phosphate, ADP, and energy. releases energy because reactants have higher energy than products. (due to the repulsion of negatively charged phosphate groups that causes high instability).

25
Q

glutamic acid -> glutamine

A

ATP phosphorylates glutamic acid to form an instable compound. ammonia replaces the phosphate group to form glutamine. (∆G = -3.9 kcal)

26
Q

phosphorylated intermediate

A

molecule with phosphate group covalently bound to it, making it more reactive than original molecule. important for energy coupling.

27
Q

ATP cycle

A
  1. ATP hydrolysis to ADP + P yields energy for cellular work (∆G = - 7.3 kcal/mole)
  2. ATP synthesis from ADP + P requires energy from catabolism
28
Q

enzyme

A

macromolecule that acts as a catalyst. lowers activation energy for a reaction, but does not change ∆G.

29
Q

catalyst

A

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

30
Q

activation energy

A

amount of energy required to start a reaction (contorts reactant molecules so the bonds can break)

31
Q

transition state

A

unstable state of reactants that have absorbed enough energy for its bonds to break

32
Q

substrate

A

reactant an enzyme acts on. held in place by weak interactions (hydrogen bonds, ionic bonds)

33
Q

enzyme substrate complex

A

enzyme bound to its substrate

34
Q

sucrase

A

enzyme that catalyzes hydrolysis of sucrose (disaccharide) into glucose + fructose (monosaccharides)

35
Q

active site

A

region of enzyme that binds to substrate

36
Q

induced fit

A

change in active site of enzyme to bind more snugly with substrate

37
Q

enzyme catalysis

A

Catalysis carried out by R groups of amino acids in active site. It catalyzes either the forward or reverse reaction (to approach equilibrium).

38
Q

enzyme mechanisms to lower activation energy/speed up reaction

A
  1. active site acts as template to arrange substrates in proper orientation
  2. stretches substrate molecules towards transition state (stresses/bends chemical bonds)
  3. active site provides proper microenvironment (ex: lower pH)
  4. direct participation of active site in chemical reaction
39
Q

saturated

A

substrate concentration where all enzymes have their active sites engaged, so the rate of reaction is determined by the speed of reactant-product conversion.

40
Q

effect of temperature

A

substrates collide with active sites more frequently at higher temperatures. Too high temperatures can cause protein to denature

41
Q

optimal conditions

A

optimal pH and temperature

42
Q

cofactors

A

nonprotein helpers for enzymes

43
Q

coenzyme

A

cofactors that are organic molecules

44
Q

competitive inhibitors

A

competes with substrate to bind with active site

45
Q

noncompetitive inhibitors

A

binds to protein (not at the active site) and causes a shape change that makes active site less effective

46
Q

β-galactosidase

A

breaks lactose into glucose and galactose

47
Q

allosteric regulation

A

protein’s function at one site is affected by binding of regulatory molecule at another site

48
Q

allosteric site

A

site on protein where activating/inhibitory regulatory molecule binds

49
Q

allosteric activator

A

stabilizes active form of enzyme (ex: ADP activates catabolic enzymes)

50
Q

allosteric inhibitor

A

stabilizes inactive form of enzyme (ex: ATP inhibits catabolic enzymes)

51
Q

cooperativity

A

substrate molecule binds to an active site, triggering shape change in the other subunits of the enzyme that increases their catalytic activity

52
Q

feedback inhibition

A

metabolic pathway switched off by inhibitory binding of its end product to an enzyme in the beginning of the pathway

Biology Olympiad (18 decks)

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