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BIO 1200 > Chapter 6: Energy And Enzymes > Flashcards

Chapter 6: Energy And Enzymes Flashcards

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Biology 101 flashcards
1
Q

what are the types of energy in the cell?

A

chemical energy, ion gradients, and solar energy

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2
Q

what molecules have chemical energy?

A

organic (ATP, NADH)

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3
Q

what types of chemical energy are there?

A

ATP/GTP, NADH/FADH2, other high energy molecules

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4
Q

what provided energy for enzyme reactions?

A

NADH/ FADH2

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5
Q

What is ATP’s bonding?

A

high energy bonds between the P groups

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6
Q

How does ATP energy work?

A

when the P-P bonds are broken the energy released can be used in enzyme reactions

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7
Q

what does ATP hydrolysis produce?

A

ADP + P + energy

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8
Q

what is redox reaction?

A

oxidation-reduction reaction

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9
Q

which form normally has the H?

A

reduced

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10
Q

in a redox reaction, where are the reduced and oxidized form?

A

both sides

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11
Q

what is the reduced form?

A

High energy form
Has accepted a pair of electrons

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12
Q

what is the oxidized form?

A

low energy form
has lost a pair of electrons

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13
Q

reduced compounds transformation

A

loses electrons and become oxidized

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14
Q

oxidized compounds transformation

A

gains electrons and becomes reduced

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15
Q

when a compound gains an electron what else does it sometimes pick up?

A

H- it neutralizes the charge

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16
Q

OILRIG

A

oxidation is loss of electrons
reduction is gain of electrons

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17
Q

What is an ion gradient?

A

when the concentration of the ion is higher on one side of the membrane

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18
Q

in an ion gradient, as ions flow across the membrane down their concentration gradient, energy is

A

released to move some other substance or make ATP

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19
Q

what is solar energy?

A

energy from sunlight can be used for electron transport during photosynthesis

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20
Q

what are the parts of photosynthesis?

A

light reactions, sunlight, electron transport =H+ gradient, ATP/NADPH =chemical energy

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21
Q

what is thermal energy

A

heat

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22
Q

what is chemical energy?

A

stored in the bonds of molecules

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23
Q

what is the first law of thermodynamics?

A

energy cannot be created or destroyed- energy can be converted from one type of energy to another type of energy

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24
Q

what law says energy can only change form?

A

1st

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25
Q

what is the 2nd law of thermodynamics?

A

any energy transformation increases the disorder of a system; entropy

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26
Q

what is entropy

A

A measure of disorder or randomness

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27
Q

reactions are a part of a

A

pathway

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28
Q

each reaction is catalyzed by a

A

enzyme

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29
Q

is all enzymes in a reaction needed?

A

yes- to get to the final product

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30
Q

what is the reactant?

A

sunbstrate

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31
Q

what is a substrate?

A

the starting compound in a reaction

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32
Q

what is the product?

A

compound made at the end of a reaction

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33
Q

-ace is normally a

A

enzyme

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34
Q

what is a chemical equilibrium?

A

when the rate of formation of products equals the rate of formation of reactants

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35
Q

chemical reactions will reach a

A

equilibrium

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36
Q

Keq>1 means

A

the formation of products is favored
the reaction is mainly going left to right

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37
Q

what is the equation for Keq?

A

(C)c(D)d
————
(A)a(B)b

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38
Q

what does a larger Keq mean?

A

the more of a product is made relative to reactant at equilibrium

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39
Q

the more products you get is by

A

A bigger Keq

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40
Q

what is free energy?

A

The energy that can be used to do work

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41
Q

what way do reactions tend to proceed in?

A

the direction that causes a decrease in the free energy of the system (^G=negative)

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42
Q

what are exergonic reactions?

A

where energy is released and ^G is negative

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43
Q

what reactions are spontaneous?

A

exergonic

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44
Q

what are endergonic reactions?

A

are reactions where energy must be input in order to occur (^G is positive

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45
Q

what is the name of more than one reaction occurring at the same time?

A

coupled

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46
Q

when will couples reactions not go?

A

when the overall ^G is positive

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47
Q

when will a coupled reaction go?

A

when the overall ^G is negative

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48
Q

exergonics energy is coming _
endergonic energy is coming _

A

out
in

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49
Q

what are coupled reactions?
spontaneous or not?

A

spontaneous

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50
Q

what are catalysts?

A

increase the rate of reaction

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51
Q

what are not used up in the reaction?

A

catalysts (they are reusable)

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52
Q

Catalysts _ reactant

A

don’t equal

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53
Q

do catalysts alter the equilibrium of a reaction?

A

no

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54
Q

what decreases the amount of time required to reach equilibrium?

A

catalyst

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55
Q

what are the special features of enzymes?

A

specific, efficient, and regulated

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56
Q

what is specific?

A

enzymes perform one reaction or type of reaction

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57
Q

Kinase adds a phosphate group to a certain enzyme or protein. It won’t add a group to every single enzyme or protein so which feature is it?

A

specific

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58
Q

what is efficient?

A

enzymes increase the rate of reaction dramatically

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59
Q

what is regulated?

A

enzymes can be turned on and off

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60
Q

why are enzymes regulated?

A

they take a long time to build so you don’t want rebuild each time so you turn on and off

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61
Q

enzymes work in

A

pathways

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62
Q

what is interconnected

A

pathways

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63
Q

flow through a pathway can be

A

regulated

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64
Q

catabolic is
Anabolic is

A

breakdown
synthesis

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65
Q

what state do substrates go though?

A

activated transition state

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66
Q

what is a transition state?

A

intermediate whose free energy is higher that that of the reactants

67
Q

formula for transition state

A

enzyme+ substrate -> enzyme-substrate complex -> enzyme + product

68
Q

are substrate and molecules stable during transition state?

A

yes

69
Q

what is activation energy?

A

the amount of energy that must be added for a reaction to proceed

70
Q

how do enzymes speed up a reaction?

A

they lower the activation energy of a reaction

71
Q

what type of energy could be activation?

A

heat or kinetic energy

72
Q

enzymes catalyzed reactions go through a ____ whose free energy is ____ than the intermediate if the _______

A

transition state
lower
uncatalyzed reaction

73
Q

how do enzymes lower the activation energy?

A

enzymes can interact with the substrate and provide an alternate transition state

74
Q

what is an alternate transition state?

A

different intermediate

75
Q

what is Ea

A

activation energy

76
Q

what do enzymes do for the reaction to occur?

A

hold the substrates in the proper orientation

77
Q

what is enzyme specificity determined by?

A

the shape of the active site

78
Q

what is an active site?

A

location in the enzyme where reactions take place and where substrates have to bond to

79
Q

what is the lock and key model?

A

only the right substrate (key) will fit in the active site (keyhole) of the enzyme (lock)

80
Q

when are molecules substrates?

A

only when molecules can fit into the active site of an enzyme are substrates for the reaction

81
Q

why are substrates oriented?

A

so the bond to be cleaved is in a certain position

82
Q

what is a variation of the lock and key model?

A

induced fit model

83
Q

anytime something bonds, what happens to the activity?

A

it can become more or less active and it will change its shape

84
Q

what is the induced fit model?

A

when substrates bind to enzyme the shape of the enzyme changes slightly to improve catalytic activity of the enzyme

85
Q

what does the lock and key model help enzymes be?

A

very efficient

86
Q

how are substrates held?

A

in close proximity and proper orientation

87
Q

what do active sites contain?

A

functional groups that temporarily donate H+s or e-s

88
Q

what happens during binding of substrate to enzyme?

A

it induces strain on the substrate molecule and makes it more reactive

89
Q

what is covalent intermediates?

A

has a slightly higher energy level and are temporary

90
Q

catalytic efficiency is the formation of

A

covalent intermediates

91
Q

list the steps of catalytic reaction

A

the active site lowers the activation energy
acts as a template for the reaction
stresses the substrate
stabilizes the transition state
participates in catalytic reaction

92
Q

what is more likely when a intermediate is stabilized?

A

it is more likely to go through

93
Q

how do enzymes compare to themselves in the beginning of a reaction

A

they look exactly the same

94
Q

what does a small change in ph do? (<1 ph unit)

A

change the charge on the substrate
change the charge on the enzyme (active site)
the substrate may no longer be able to bind to enzyme or not bind as well so the enzyme will be less active

95
Q

what is a proteins shape essential for?

A

its function

96
Q

what is a denatured protein?

A

it loses its 3d shape and becomes an unfolded chain of amino acids
it will not function properly

97
Q

what happens during denaturing?

A

the ionic, H bonds, and disulfide bonds that hold the protein in its 3d shape are broken and the enzymes unfolds

98
Q

what is the formation of amino acids while denatured?

A

still connected in a chain by peptide bonds

99
Q

What causes protein denaturation?

A

large change in ph
acidic
basic
high temps

100
Q

Is denaturing temporary or permanent?

A

permanent

101
Q

What happens when an enzyme reaches past its optimal temp or ph?

A

denaturation

102
Q

are some enzymes more sensitive to ph than others?

A

yes

103
Q

what is ph optimum

A

the ph at which the enzyme performs the reaction at the maximum rate

104
Q

when does an enzyme become denatured with the ph optimum?

A

when it is above or below it- it becomes less active

105
Q

How is an enzymes ph optimum chosen?

A

depends on where they work

106
Q

what ph optimum do most enzymes have?

A

one that matches the ph of the environment the enzyme is designed to work for

107
Q

what happens with a large change in ph (>1 ph unit)

A

breaks ionic and H bonds that hold protein in its 3d shape
enzymes may partially unfold and become less active
Enzyme may completely unfold (denature) and become totally inactive

108
Q

a relative change in ph will ____ and as it goes farther it will ____

A

slightly unfold
more unfolded and it will unravel

109
Q

what is the stomach enzyme?
what is it ph optimum?

A

pepsin
2

110
Q

what is the intestinal enzyme?
what is the ph optimum?

A

trypsin
8

111
Q

what is the ph optimum of most enzymes? why?

A

7 because most ph of cells is 7

112
Q

what do most enzymes have a temp optimum of?

A

equal to the body temp of the organism they are from

113
Q

what does a high temp do?

A

breaks ionic and h bonds that holds the enzyme into its 3d shape

114
Q

what is the human enzymes temp?

A

37c

115
Q

what happens with cold temps?

A

the exams will not be denatured. It is less active because molecules have less kinetic energy at low temps

116
Q

what to do if you want to preserve enzymes?

A

put it on ice-cold

117
Q

what is kinetic energy?

A

energy associated with movement

118
Q

How does kinetic energy affect the reaction rate?

A

more kinetics energy, more collisions between molecules, faster reaction rate

119
Q

how does cold temps affect kinetic energy?

A

the colder the temp, the less kinetic energy a molecule has, so there will be feeer collisions between molecules, lower and slower reaction rate

120
Q

___ temp= ___ kinetic energy = ____ reaction rate

A

low, low, low

121
Q

what are the factors for maximal enzyme activity?

A

prosthetic group
coenzymes
cofactors

122
Q

what is a prosthetic group?

A

small organic molecule permanently (covalently) bound to enzyme; Heme

123
Q

what are coenzymes?

A

small organic molecule (volume derivatives) bind temporarily (ionic or h bonds) to enzyme

124
Q

what does a coenzyme need for?

A

to function right

125
Q

what are cofactors?

A

metal ions: fe, Mg

126
Q

what is required for proper 3d shape of protein and active site?

A

prosthetic group
coenzyme

127
Q

what is directly involved in chemical reaction?

A

cofactor and coenzymes

128
Q

what may change the shape of the active site?

A

coenzymes

129
Q

what makes temporary bond between 2 substrates?

A

coenzymes

130
Q

what is an inhibitor?

A

molecule or ion that binds to enzyme and decreases its activity

131
Q

what happens when an inhibitor is present?

A

it changes the shape so the substrate can’t bind to it, it makes it less active or completely

132
Q

how can an inhibitor bind to the active site?
what type?

A

It must resemble the substrate
competitive

133
Q

if the competitive inhibitor binds to the active site, the substrate ___ so ___ reaction

A

can’t
no

134
Q

a competitive inhibitor is called this because

A

they are both competing for the active site

135
Q

the more inhibitor is added the ____ reaction is inhibited

A

more

136
Q

how many enzyme molecules are in a cell?

A

100s or thousands

137
Q

the more inhibitor binds to the active to ___ the reaction rate

A

lower

138
Q

what are noncompetitive inhibitors?

A

binds to enzyme noncovalently at the allosteric site- won’t bind to the active site

139
Q

do some proteins have more than one subunit?

A

yes

140
Q

what is the catalytic subunit?

A

contains the active site and performs the reaction

141
Q

what are regulatory sununits?

A

contains the allosteric site and regulates enzyme sctivity

142
Q

noncompetitive inhibitors bind to ___ on ___ subunits

A

allosteric
regulatory

143
Q

what does noncompetitive inhibitors change shape of?

A

regulatory and catalytic subunits

144
Q

control of enzyme activity is

A

allosteric regulation and noncompetitive inhibitors

145
Q

how many subunits do allosteric enzymes have?

A

more than one

146
Q

what is a catalytic subunit?

A

binds substrate at the active site, performs enzyme reaction

147
Q

what is a regulatory subunit?

A

binds an effector at the allosteric site, controls activity of the enzymes

148
Q

what are effectors and where do they bind to?

A

small organic molecule that controls the activity of the enzyme and bind to the allosteric site

149
Q

what two things can effectors be?

A

inhibitors or activators

150
Q

what two forms do allosteric enzymes have?

A

active- form of the enzyme that performs its function (on)
inactive - nonfunctional form of enzyme (off)

151
Q

what do effectors control?

A

Activity of enzyme

152
Q

what do regulatory molecules/effectors bond to?

A

regulatory subunit and causes it to change shape

153
Q

what does a change in shape of the regulatory subunit cause?

A

catalytic subunit to change shape- turns it in inactive form, off

154
Q

what may regulatory subunits bound to?

A

catalytic subunits but they both change shape
it can either be bound or released but either way it will change shape

155
Q

What is allosteric inhibition?

A

an inhibitor (effector) binds to the regulatory subunit which causes the subunit to change shape.

156
Q

change of shape of regulatory subunit cause catalytic subunit to change ____

A

shape from active form to inactive form

157
Q

what is feedback inhibition?

A

accumulation of the product of a metabolic pathway inhibits one of the enzymes at the beginning of the pathway

158
Q

what is feedback inhibition a kind of?

A

allosteric inhibition

159
Q

process of feedback inhibition

A

Inhibitor binds to allosteric site on regulatory subunit of enzyme 1, regulatory subunit changes shape, catalytic subunit changes shape (inactive form)

160
Q

when a product made at the end of a pathway binds to one of the enzymes near the beginning of pathway and inactivates the enzyme

A

feedback inhibition

161
Q

allosteric regulation is a kind of

A

noncompetitive inhibition

162
Q

what is allosteric regulation used for?

A

regulate enzymes in pathway

163
Q

what is an allosteric inhibitor?

A

chemical binding of the effects makes enzyme less active
active enzyme-> inactive off

164
Q

what is an allosteric activator?

A

chemical binding of the effects makes enzyme more active
inactive enzyme -> active, on

BIO 1200 (14 decks)

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