Exam 2 M6 Flashcards

(95 cards)

1
Q

T/F: biological rxns require catalysts

A

T

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2
Q

what serves as enzymes

A

proteins and RNA molecules

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3
Q

T/F: catalysts are not enzymes

A

F

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4
Q

enzymes catalyze rns under ____ conditions

A

mild

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5
Q

enzymes allow for high degrees of rxn ____

A

specificty

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6
Q

enzymes catalyze 1 or a few ___

A

closely related rxns

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7
Q

T/F: enzymes can’t distinguish btwn stereoisomers

A

False

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8
Q

T/F: enzymes inc rxn rates

A

T

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9
Q

how much do enzymes inc rxn rates

A

10^6 to 10^12

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10
Q

enzymes enable ___

A

regulation

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11
Q

how to regulate enzyme

A

1)control amount of enzyme in cell via txn (control rate at which RNA is produced that will code for that enzyme) or tsln (control how fast RNA–> protein) mechs

2)control activity of enzyme (different small molecules can act as effector molecules that can speed up an enzyme or slow down an enzyme –> activators vs inhibitors)

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12
Q

some enzymes require additional molecules called ____ for their functions

A

coenzymes

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13
Q

Cofactors

A
  1. Cations (ions that stabilize enzyme structure like Zn fingers; can also participate directly in chemical rxns)
  2. coenzymes (organic molecules that associate transiently w enzyme; can also participate in chemical rxn and need to be converted back to their initial state for next round of rxn)
  3. prosthetic groups (e.g. heme, organic molecules permanently covalently associated w enzyme)
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14
Q

active sites are meant to be complementary in ____ to substrate

A

shape and chemical properties

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15
Q

enzymes are HIGHLY

A

specific

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16
Q

enzymes are not ____

A

rigid

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17
Q

enzymes do not alter ____

A

thermodynamics

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18
Q

define transition state

A

point of highest free energy

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19
Q

rate of rxn is directly proportional to

A

delta G dagger

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20
Q

enzymes don’t affect the ____ of equilibrium

A

position

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21
Q

T/F: If a rxn is +deltaG but an enzyme can catalyze it, it will occur

A

F

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22
Q

how do enzymes speed up rxns

A

by stabilizing TS by reducing deltaG associated w TS, make substrates that resemble TS, or change the pathway to go through a diff TS

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23
Q

what causes high delta G

A

lots of breaking and forming bonds at the same time

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24
Q

what is delta delta G dagger

A

reduction in deltaG dagger by the catalyst; helps determine how much enzyme speeds up rxn

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25
enyme does not change overall ___ of a rxn
deltaG
26
enzymes do change ____ of a rxn by lowering delta G associated w TS
kinetics
27
all chem rxns exhibit___
kinetics
28
zero order
rate = k1 A--> B k1 independent of concentration and only depends on rate constant, k1
29
first order
rate = k1[A] A--> B k1 depends on rate constant and also on conc of reactants
30
second order
rate = k1[A][B] A+B --> C k2 depends on rate constant and conc of reactants
31
dissociation constant for ES
Kd = [E][S]/[ES]
32
what does Kd for ES assume
K-1 >> K2
33
which molecules can't you measure in lab
[E], [ES]
34
which molecules can you measure in lab
[P], [E]tot
35
what enzyme did M-M base their model off of
invertase
36
what are the 3 assumptions of M-M's model
1. product does not convert back into substrate (irreversible rxn) 2. rxn is at a steady-state; [ES] remains constant during whole rxn 3. [S] is infinitely large
37
product formation depends on _____ and ___
[ES] and K2
38
M-M equation
v0 = vmax [ S] / (Km + [S])
39
a low [S], line is almost linear but as we inc [S], v inc in a ___ fashion
linear
40
Km = [S] it takes to get to
1/2 Vmax
41
vmax occurs
at high [S] when enzyme is sat vmax = k2 [E]tot
42
Kcat =
Vmax / [E]tot
43
Kcat also known as
turnover number
44
large Kcat =
fast conversion and high turnover #
45
for enzymes that obey M-M kinetics, Kcat =
K2
46
highly efficient enzymes are ___ limited
diffusion
47
overall efficiency of an enzyme depends on both ___ and ____
Kcat and Km
48
Kcat/Km must be less than or equal to
K1
49
efficiency is directly proportional to
Kcat
50
efficiency is indireclty proportional to
Km
51
on LW-B plot: slope =
Km/Vmax
52
on LW-B plot: x-intercept =
-1/Km
53
on LW-B plot: y-intercept =
1/Vmax
54
competitive inhibition blocks the
active site (direclty or allosterically) *block's enzyme's ability to bind substrate*
55
T/F: comp inhibition binds enzymes reversibly or irreversibly
T
56
comp inhibitors often resemble
substrate in structure
57
comp inhibitors best resemble
TS analog
58
product inhibition is an ex of ____ inhibition
competitive
59
inhibitors change the ___
kinetics
60
comp inhibitors bind to
free enzyme
61
KI =
[E][I]/[EI]
62
M-M equation for comp inhibition
V0 = Vmax [ S] / aKm + [S]
63
For comp inhbition, as inc [I], the line shifts to the ___ which means rxn is slower
right
64
65
66
67
68
alpha depends on
[I] and affinity of E for I
69
Km app =
alpha Km
70
for comp inhibition, alpha only affects
Km
71
slope for comp inhib
alpha Km / Vmax
72
in comp inhib, Vmax
doesnt change
73
if inhibitor binds very tightly, KI ___ and alpha ___
dec; inc
74
uncomp inhibitors bind to
ES complex
75
uncomp inhibitors interfere with
catalysis
76
uncomp inhibitors don't necessarily need to resemble
substrate bc doesn't bind to active site
77
KI' =
[ES][I]/[ESI]
78
uncomp inhib graph looks like
parallel lines
79
why are the parallel lines parallel
bc Vmax and Km are changing proportionally as we inc [I]
80
a' is_____ to [I]
directly proportional
81
a' is _____ to KI
indireclty proprtional
82
uncomp inhibitor effects both ___
Vmax and Km
83
as we add more uncomp inhibitor, Km___and Vmax __
inc; dec
84
new y-int for uncomp inhib
a'/vmax
85
new x-int for uncomp inhib
-a'/Km
86
M-M equation for uncomp inhib
V0 =(vmax/a')[S] / (Km/a') +[S]
87
Km app for uncomp inhib
Km / a'
88
vmax app for uncomp inhib
vmax / a'
89
both vmax and Km is affected by
a'
90
mixed inhib affects both
binding (comp) and catalysis (uncomp)
91
M-M equation for mixed
V0 = (vmax/a')[S] / (aKm/a') + [S]
92
Km app for mixed =
aKm/a'
93
Vmax app for mixed
Vmax/a'
94
in mixed, both a and a' affects
Km
95