bio chapter 6

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metabolism

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Biology

59 Terms

1

metabolism

all of an organism’s metabolic pathways; anabolic and catabolic

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2

catabolic pathways

release energy; break down complex molecules into simpler ones

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3

ex of catabolic pathways

cellular respiration breaking glucose down into CO2 and H2O providing cell with energy

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4

anabolic pathways

consume energy; build complex molecules from simpler ones

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5

ex of anabolic pathways

photosynthesis making glucose molecules from CO2 and H2O; polymerization reactions

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6

energy

capacity to do work

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7

kinetic energy

energy of motion; energy in the process of doing work

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8

kinetic energy ex

a ball at the top of a hill or water behind a dam (due to gravity); chemical energy stored in molecules because of arrangement of nuclei and electrons

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9

ex of transformed energy

in photosynthesis, the kinetic energy of sunlight is transformed into potential energy; when burning gasoline, the potential energy of chemical bonds is transformed into kinetic energy which pushes engine pistons

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10

free energy

amount of energy in a system that is available to do work; designated G

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11

Delta G

change in free energy; change in free energy from the initial state to the final state of a reaction

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12

free energy

indicates whether a reaction will occur spontaneously or not

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13

spontaneous reaction

a reaction that will occur without additional energy; free energy decreases (negative delta G)

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14

spontaneous reaction

as a reaction approached equlibrium, delta G decreases

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15

non-spontaneous reaction

when a reaction is pushed away from equilibrium, delta G increases

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16

no net change in system

when a system reaches equilibrium, delta G = 0

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17

exergonic reaction

proceeds with a net loss of delta G (negative); products have less free energy than reactants; spontaneous reaction

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18

endergonic reaction

proceeds with a net gain of delta G (positive); requires input of energy; products have more free energy than reactants; non-spontaneous reaction

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19

if a chemical process is exergonic, the reverse process must be endergonic

ex:

cellular respiration is an exergonic process

2870 kJ (686 kcal) of energy are released from each mole of glucose in respiration (∆G = -2870 kJ/mol or ∆G = -686 kcal/mol) photosynthesis is an endergonic process 2870 kJ (686 kcal) of energy must be added to produce a mole of glucose in photosynthesis (∆G = + 2870 kJ/mol or ∆G = +686 kcal/mol)

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20

metabolic disequilibrium

necessary for life; if metabolic reactions reach equilibrium, cell dies (delta G = 0, no work can be done); metabolic reactions are “pulled forward” bc their products become reactants for the next reaction in the metabolic pathway

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21

ATP

adenosine triphosphate; immediate source of energy that drives most cellular work; mechanical, transport, and chemical work

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22

mechanical work

cilia beating, muscle contraction, etc.

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23

transport work

pumping substances across membranes

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24

chemical work

endergonic reactions like polymerization

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25

ATP

nucleotide with unstable phosphate bonds; phosphate bonds are hydrolyzed to yield energy for endergonic reactions

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26

components of ATP

adenine (nitrogenous base); ribose (5 carbon sugar); 3 phosphate groups

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27

phosphate bonds

unstable; can be broken (exergonic reaction); when terminal phosphate bond is hydrolyzed, a phosphate group is removed

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28

ADP

exergonic reaction; ATP + water = ADP

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29

exergonic reaction

products more stable than reactants

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30

ATP function

exergonic hydrolysis of ATP is couple with endergonic reactions; a phosphate group is transferred to another molecule; phosphorylated molecule becomes more reactive

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31

regeneration of ATP

endergonic reaction ADP + P = ATP; occurs rapidly (10^7 molecules are used and regenerated in each cell every second; energy required comes from the exergonic process of cellular respiration

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32

catalyst

chemical agent that speeds up a reaction without being permanently changed in the process; can be used over and over

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33

enzymes

biological catalysts made of protein; speed up reactions by lowering energy barriers

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34

activation energy

amount of free energy reactant molecules must absorb to start a reaction (EA); needed to break chemical bonds

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35

exergonic reaction

reactants must absorb enough energy to reach transition state (top of hill); usually involves absorption of thermal energy from surroundings; reaction occurs and energy is released as new bonds form (downhill); delta G for overall reaction is the difference between the free energy products and reactants; free energy of products is less than reactants in an exergonic reactants

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36

breakdown of biological macromolecules

exergonic; cannot absorb enough energy to reach transition state; need enzymes

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37

enzymes

lower EA; transition state can be reached at cellular temperatures; very selective for the reaction will catalyze

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38

substrate

substance an enzyme acts on (made more reactive); catalyzed to product after it binds to active site of enzyme; enzyme +substrate = enzyme-substrate complex = product + enzyme

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39

enzyme

specific for a certain substrate; 3D shape determines specificity

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40

active site

region of enzyme which binds to substrate; formed by a few amino acids; fits compatibly with substrate

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41

catalytic cycle of enzymes

substrate binds to active site and held there by weak interactions; induced fit of active site around substrate, side chains in active site catalyze conversion of substrate to product; product leaves site and enzyme emerges unchanged

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42

ways enzyme lower activation energy to speed up reactions

active site may hold reactions in proper position to react; induced fit may distort substrates chemical bonds making them easier to break; site may provide a microenvironment conducive to particular reaction types; amino acid side chains in active site may participate directly in reaction

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43

substrate concentration

higher substrate concentration = faster reaction (to a point); enzyme can become saturated with substrate if concentration gets high enough; when saturated, reaction rate depends on how fast site can convert substrate to product; when enzyme is saturated, reaction increases with more enzyme

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44

effects of temperature

optimal temp. allows greatest number of molecular collisions without denaturing enzymes; ( temperature =  kinetic energy =  collisions =  reaction rate) beyond optimal temperature, reaction rate slows as enzyme denatures ( thermal energy disrupts weak bonds in enzymes)

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45

effects of pH

optimal range for most enzymes = 6-8; some operate best at more extremes of pH (stomach enzyme = 2)

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cofactors

small, nonprotein molecules needed for proper enzyme function; may bind to active site or substrate

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47

inorganic cofactors

zinc, iron, copper, etc

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48

organic cofactors (coenzymes)

vitamins

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49

effects of enzyme inhibitors

some chemicals may inhibit enzyme activity; irreversible and reversible inhibition

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50

irreversible inhibition

inhibitor attaches by covalent bonds

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51

reversible inhibition

inhibitor attaches by weak bonds

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52

competitive inhibitors

resemble substrate; compete with substrate for active site (block site from substrate); overcome by increasing substrate concentration (if reversible)

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53

noncompetitive inhbitors

bind to another part of enzyme molecule causing it to change shape (active site cant bind substrate); may act as toxins (DDT, antibiotics); increasing substrate WILL NOT overcome this

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54

control of metabolism

allosteric regulation; feedback inhibition; cooperativity

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55

allosteric regulation

controls metabolism

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56

allosteric enzymes

2 shapes; active and inactive conformation

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57

allosteric site

receptor site on some part of enzyme molecule (other than active site); activator binds here stabilizing active conformation of enzyme; noncompetitive inhibitor binds here stabilizing inactive conformation

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58

feedback inhibition

metabolic pathway regulated by its own end product; end product inhibits an enzyme somewhere in the pathway

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59

cooperativity

substrate molecules may enhance enzyme activity; substrate binds to active site of 1 enzyme subunit causing a shape change that enhances substrate binding at active site of other subunits

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