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GU MCP Lectures 7,8,9 Stats
Can you name the GU MCP Lectures 7,8,9?
By
Northface
20m
114 Questions
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Question
Answer
% Correct
_
_
_
_
∆H = enthalpically favored
negative
54.5%
the X intercept is _
_
_
_
_
1|Km
45.5%
U P V (denoted by uppercase letters) represent _
_
_
_
_
_
_
_
_
_
_
_
_
_
_
_
_
which mean they are independent of _
_
_
_
_
_
_
state functions path
36.4%
∆U=
q-w
36.4%
large Keq, ∆G is _
_
_
_
_
_
_
negative
36.4%
_
_
_
_
∆G is only achieved if the surroundings do work on the reaction
positive
36.4%
Catalyst does not change _
_
Keq
36.4%
_
_
_
_
_
kcat means more efficient enzyme
higher
36.4%
“missing a component,” polypeptide part of the enzyme without its co-
factor
apoenzyme
36.4%
_
_
_
_
∆S = entropically opposed
negative
27.3%
Enzymes do not alter _
_
_
_
_
_
_
_
_
_
_
equilibrium
27.3%
high-
energy molecules (glucose), which would otherwise rapidly break down into their simpler, low-
energy constituents (e.g. _
_
_
_
_
and _
_
_
_
_
).
CO2 H2O
27.3%
_
_
_
_
_
_
_
is a measure of catalytic efficiency.
kcat|Km
27.3%
Formula for Km
(k-1+ k2)|k1
27.3%
The initial velocity (v0) is defined as the velocity that is achieved when less than _
_
_
_
% of the _
_
_
_
_
_
_
_
have been consumed.
10 substrates
27.3%
_
_
_
_
= k2 [E]T
Vmax
27.3%
The Y intercept is _
_
_
_
_
_
1|Vmax
27.3%
_
_
_
_
_
_
_
_
_
_
_
_
_
_
_
_
_
_
_
_
_
_
chemical compounds with a chemical structure that resembles the transition state of a substrate molecule in an enzyme-
catalyzed chemical reaction
transition state analogs
27.3%
at very low [S], the effects of a _
_
_
_
_
_
_
_
_
_
inhibitor become negligible
uncompetitive
27.3%
_
_
_
_
_
_
_
_
_
_
_
inhibitor decreases the catalytic activity of the enzyme without affecting its affinity for substrate
uncompetitive
27.3%
The diagnostic Lineweaver-
Burk plot for uncompetitive inhibition consists of a series _
_
_
_
_
_
_
lines
parallel
27.3%
H= _
_
_
+ _
_
_
U PV
27.3%
The universe tends towards maximum disorder: _
_
_
_
_
_
law of Thermodynamics
2nd
27.3%
Primary structure of a protein has low entropy because it is forcing _
_
_
_
_
_
_
to be more _
_
_
_
_
_
_
_
_
water ordered
27.3%
dissolving urea is an _
_
_
_
_
_
_
reaction
endothermic
27.3%
K_
D indicates _
_
_
_
_
_
_
_
_
_
and is part of _
_
_
_
affinity Km
27.3%
Competitive inhibitor _
_
_
_
_
_
_
_
_
_
_
apparent Km
increases
27.3%
“ready to go,” (apoenzyme + cofactor)
holoenzyme
27.3%
Mixed inhibition always decreases _
_
_
_
_
_
but may increase or decrease _
_
_
_
_
_
vmax km
27.3%
q is heat absorbed by the _
_
_
_
_
_
_
from the _
_
_
_
_
_
_
_
_
_
_
system surroundings
18.2%
An otherwise endergonic reaction can be coupled to an exergonic reaction such as _
_
_
_
_
_
_
_
_
_
_
_
_
_
ATP hydrolysis
18.2%
Spontaneous only at T>∆H/
∆S, _
_
_
_
∆H and _
_
_
_
∆S
+ +
18.2%
when Keq < 1, ∆G is _
_
_
_
_
_
_
_
_
_
positive
18.2%
Spontaneous reactions go in the direction of _
_
_
_
_
_
free energy
lower
18.2%
A‡(rate k1) is of higher energy than I‡ (rate k2) , making k_
the slower step
1
18.2%
The experimental advantage of measuring _
_
_
_
is that product inhibition and the reverse reaction are less likely to complicate measurements.
v0
18.2%
_
_
_
_
is expected to occur when the enzyme is completely saturated with substrate ([E]T = [ES]).
Vmax
18.2%
_
_
_
_
_
_
_
_
_
_
_
concentration = [E]T
total enzyme
18.2%
Question
Answer
% Correct
Lineweaver-
Burk is also called a _
_
_
_
_
_
_
_
_
_
_
_
plot
double reciprocal
18.2%
competitive inhibitor is a substance that competes with the substrate for binding to the _
_
_
_
_
_
_
binding site on the enzyme.
substrate
18.2%
Some transition state analogs bind _
_
_
_
_
_
_
_
_
_
_
than actual transition state meaning they bind at a _
_
_
_
_
Km
more tightly lower
18.2%
An uncompetitive inhibitor binds ONLY to the_
_
_
_
_
_
_
_
_
ES complex
18.2%
_
_
_
_
∆G will do work on the surroundings
negative
18.2%
_
_
_
_
_
km = more efficient enzyme
lower
18.2%
number of times per sec an enzyme makes a product
kcat
18.2%
Km has units of _
_
_
_
_
_
_
_
concentration
18.2%
_
_
_
_
_
_
_
kcat/
km= greater catalytic efficiency
higher
18.2%
Binds ES complex and free enzyme
mixed
18.2%
Enzymes are good for reactions in physiological conditions because they allow for _
_
_
_
_
reaction conditions
milder
18.2%
_
_
_
_
_
inhibitors generate a complex pattern on a Lineweaver-
Burk plot, with the _
_
_
_
_
_
_
_
_
component affecting apparent KM and the _
_
_
_
_
_
_
_
_
component affecting both KM and Vmax
mixed competitive uncompetitive
18.2%
The high specificity of enzymes for their substrates, described by their KMs, means that enzyme catalyzed reactions rarely have non-
productive _
_
_
_
_
_
_
_
_
_
_
_
_
_
side products
18.2%
Move group to another location on the same molecule to yield isomeric forms
isomerases
18.2%
_
_
_
_
_
_
_
_
_
_
_
is actually a transferase
ubiquitin ligase
18.2%
w is work done by the _
_
_
_
_
_
_
on its _
_
_
_
_
_
_
_
_
_
system surroundings
9.1%
When ∆U=0, ΔS > or =
q|T
9.1%
A system may attain order at the expense of _
_
_
_
_
_
_
_
_
_
_
_
its _
_
_
_
_
_
_
_
_
_
_
_
_
disordering surroundings
9.1%
_
_
_
_
_
_
_
_
_
temperature = greater contribution of entropy
higher
9.1%
_
_
_
_
∆S = entropically favored
positive
9.1%
when ∆U=0,
q=w
9.1%
The relationship between ΔG‡ and the reaction rate (k) is _
_
_
_
_
_
and _
_
_
_
_
_
_
_
_
_
_
_
(i.e. the higher ΔG‡, the _
_
_
_
_
_
_
the rate (_
_
)).
inverse exponential slower k
9.1%
k_
cat represents _
_
_
_
_
_
_
_
_
_
_
_
_
_
turnover number
9.1%
Living systems are _
_
_
_
_
_
_
systems
open
9.1%
energy barrier between the reactants and products
activation energy
9.1%
The magnitude of lowering activation energy, ΔΔG‡, is proportional to the degree of rate _
_
_
_
_
_
_
_
_
_
_
enhancement
9.1%
Enzymes include _
_
_
_
_
_
_
binding sites or pockets which overlap with their _
_
_
_
_
sites, where the chemistry of catalysis occurs. In some cases this overlap may be 100%
substrate active
9.1%
The _
_
_
_
_
_
_
_
_
_
_
_
_
_
_
_
_
puts forth that after a rapid transient phase of the reaction, [_
_
] remains essentially unchanged until nearly all of the reactants are consumed.
steady state assumption ES
9.1%
A plot of 1/
_
_
_
versus 1/
[_
_
] yields a straight line with the slope _
_
_
_
_
_
_
_
v0 S KM|Vmax
9.1%
Energy (U) cannot be created nor can it be destroyed: _
_
_
_
_
_
law of Thermodynamics
1st
9.1%
equation for entropy with Boltzmann's
S=kblnW
9.1%
A protein folds into secondary and tertiary structures in order to maximize the _
_
_
_
_
_
_
_
_
of _
_
_
_
_
_
_
_
_
randomness water
9.1%
If a catalyst decreases the activation energy by a factor of 2, it increases the reaction rate by a factor of _
_
_
_
4
9.1%
When V_
0=1/
2Vmax, Km= [_
_
]
S
9.1%
Molecules that react with an enzyme irreversibly and decrease its activity are called _
_
_
_
_
_
_
_
_
_
_
inactivators
9.1%
although uncompetitive inhib. lower KM, the overall effect is_
_
_
_
_
_
_
_
(Vmax decreases), since the ES complex is subsequently being “sopped up” by the uncompetitive inhibitor.
inhibitory
9.1%
_
_
_
_
_
_
_
_
_
: Group-
transfer reactions to another _
_
_
_
_
_
. Examples: methyl-
transferase or phosphoryl-
transferases (a.k.a._
_
_
_
_
_
)
transferases substrate kinases
9.1%
_
_
_
_
_
_
_
_
_
: Transfer of functional groups to water – enzymes that hydrolyze bonds by using water as the _
_
_
_
_
_
_
hydrolases nucleophile
9.1%
Question
Answer
% Correct
_
_
_
_
_
_
_
_
_
: Addition of groups to double bonds, or formation of double bonds by group removal (_
_
_
_
or _
_
_
_
_
double bonds)
lyases make break
9.1%
_
_
_
_
_
_
_
_
_
catalyze the formation of C-
C, C-
S, C-
O, and C-
N bonds that never existed before by _
_
_
_
_
_
_
_
reactions coupled to ATP cleavage (Condensation opposite of _
_
_
_
_
_
_
_
)
ligases condensation hydrolysis
9.1%
inactive precursor that needs to be activated by a proteolytic step ex. zymogen
proenzyme
9.1%
inorganic ions, complex organic, metalloorganic molecules (ex. heme group)
coenzyme
9.1%
_
_
_
_
_
_
regulation is distinct from inhibitory regulation -
-
refers to a non-
substrate regulator binding to a location distant from the active site of the enzyme.
Allosteric
9.1%
Tense: less active state; higher affinity for the _
_
_
_
_
_
_
_
_
inhibitor
9.1%
kcat, or the _
_
_
_
_
_
_
number, which is the number of times the enzyme turns over and does its job again per unit time
turnover
9.1%
Although the reaction will never actually reach Vmax, it will get close enough where the _
_
_
_
_
_
_
_
_
_
_
_
extend beyond the Vmax line. At this point it is impossible to tell if the ve
error bars
9.1%
Slope (m) Lineweaver-
Burk Plot=
Km|Vmax
9.1%
Km = [S] when _
_
_
_
= ½ Vmax.
v0
9.1%
In uncompetitive, the enzyme and _
_
_
_
_
_
_
_
can create the ES complex without a problem, but I binds to ES and creates an _
_
_
_
_
_
_
_
_
_
_
_
complex with a rate KI’
substrate inactive ESI
9.1%
For mixed inhibition, the inhibitor does not necessarily have the same KD for each type so it may have a higher affinity for binding to either the_
_
_
_
_
_
_
_
_
_
_
or the_
_
_
_
_
_
_
_
_
_
free enzyme ES complex
9.1%
α (or α’) combines _
_
_
_
_
_
_
of the inhibitor and its _
_
_
_
_
_
for the enzyme
concentration affinity
9.1%
The lines of a competitive inhibitor plot meet at the _
_
_
_
_
_
_
_
y intercept
9.1%
For mixed inhibition plot, when α =α’ lines meet at _
_
_
_
_
_
_
_
_
x intercept
9.1%
A catalyst lowers activation energy but more specifically, it does this by lowering the_
_
_
_
_
_
_
_
_
_
of the _
_
_
_
_
_
_
_
_
_
free energy transition state
9.1%
_
_
_
_
_
_
_
_
energy, ΔG‡, which represents the energy of a fleeting “_
_
_
_
_
_
state” between the substrate and products.
activation transition
0%
All _
_
_
_
_
_
_
_
systems must reach equilibrium
isolated
0%
_
_
_
_
_
_
_
_
_
_
_
inhibitor lowers both the apparent KM and Vmax, but KM/
Vmax, the slope of the lines, remains _
_
_
_
_
_
uncompetitive unchanged
0%
The rate of _
_
_
_
_
_
_
_
_
_
_
is inversely proportional to the change in _
_
_
_
_
_
_
_
_
energy (ΔG‡) and is exponential
enhancement activation
0%
Formula for K_
D =
k-1|k1
0%
Two steps: _
_
_
_
_
_
_
_
substrate binding to enzyme and _
_
_
_
_
_
_
_
_
_
formation of products from ES complex
reversible irreversible
0%
A substrate-
analog that binds irreversibly to amino acids, usually the catalytic amino acid, thereby blocking the active site of the enzyme to other molecules and effectively 'kil
suicide substrate
0%
The complexity of enzymes allows for multiple additional layers of _
_
_
_
_
_
_
_
regulation
0%
_
_
_
_
_
_
_
_
_
: Transfer of electrons or protons (hydride ions or H atoms)
oxidoreductases
0%
_
_
_
_
_
_
_
_
regulation will always have a “negative” effect on the reaction rate (slow the kinetics), _
_
_
_
_
_
_
_
regulation can result in both positive and negative effects
inhibitory allosteric
0%
Relaxed: more active state; higher affinity for the _
_
_
_
_
_
_
_
activator
0%
Proenzymes, Coenzymes, Apoenzymes and Holoenzymes
Enzyme activity
0%
a _
_
_
_
_
_
Km and a _
_
_
_
_
kcat are each associated with a more efficient enzyme.
lower higher
0%
The _
_
_
_
_
_
_
_
_
of the Michaelis-
Menineton _
_
_
_
_
_
_
_
is a line known as the Double-
Reciprocal or Lineweaver-
Burk Plot
inverse hyperbola
0%
They are supposed to be as efficient as _
_
_
_
_
_
_
_
to correctly do their job in an organism.
appropriate
0%
Efficient enzymes are described as approaching the_
_
_
_
_
_
_
-
_
_
_
_
_
_
_
limit because the rate of the enzyme bumping into the substrate is controlled by diffusion, which affects the chan
diffusion-controlled colliding
0%
The primary goal of many drugs that target enzymes is to _
_
_
_
_
_
_
or _
_
_
_
_
_
_
the activity of enzymes.
inhibit change
0%
the presence of an _
_
_
_
_
_
_
is accounted for by α which is calculated by with the equation α = 1 + [I]/
KI.
inhibitor
0%
For uncompetitive inhib., apparent Km is _
_
_
_
_
_
_
_
_
because _
_
_
_
_
_
_
is _
_
_
_
_
_
_
_
, but it is inactive so it does NOT indicate that the enzyme is more efficient.
lower ESI stabilized
0%
For uncompetitive inhib, Vmax is also _
_
_
_
_
_
_
_
because the _
_
_
_
_
_
_
_
_
_
_
concentration available is decreased.
decreased total enzyme
0%
catalysts accelerate the process of reaching Keq, but do not _
_
_
_
Keq.
alter
0%
∆G˚=∆G_
f˚_
_
_
_
_
of _
_
_
_
_
_
_
-
∆G_
f˚_
_
_
_
_
of _
_
_
_
_
_
_
sum products sum reactants
0%
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