Science Quiz / GU MCP Lectures 7,8,9

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QUIZ: Can you name the GU MCP Lectures 7,8,9?

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An uncompetitive inhibitor binds ONLY to the___ ______
kcat, or the _______ number, which is the number of times the enzyme turns over and does its job again per unit time
Primary structure of a protein has low entropy because it is forcing _______ to be more _________
inactive precursor that needs to be activated by a proteolytic step ex. zymogen
If a catalyst decreases the activation energy by a factor of 2, it increases the reaction rate by a factor of ____
_________: Group-transfer reactions to another ______. Examples: methyl-transferase or phosphoryl-transferases (a.k.a.______)
The primary goal of many drugs that target enzymes is to _______ or _______ the activity of enzymes.
Formula for K_D =
Km has units of ________
when ∆U=0,
Km = [S] when ____ = ½ Vmax.
The initial velocity (v0) is defined as the velocity that is achieved when less than ____% of the ________ have been consumed.
Spontaneous only at T>∆H/∆S, ____∆H and ____ ∆S
Move group to another location on the same molecule to yield isomeric forms
Lineweaver-Burk is also called a ______ ______ plot
The _________ of the Michaelis-Menineton ________ is a line known as the Double-Reciprocal or Lineweaver-Burk Plot
Slope (m) Lineweaver-Burk Plot=
___________ inhibitor lowers both the apparent KM and Vmax, but KM/Vmax, the slope of the lines, remains ______
All ________ systems must reach equilibrium
The lines of a competitive inhibitor plot meet at the ___ _____
A protein folds into secondary and tertiary structures in order to maximize the _________ of _________
_______ ________ _______ chemical compounds with a chemical structure that resembles the transition state of a substrate molecule in an enzyme-catalyzed chemical reaction
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___ _______
Two steps: ________ substrate binding to enzyme and __________ formation of products from ES complex
Relaxed: more active state; higher affinity for the ________
The _____ ______ ______ puts forth that after a rapid transient phase of the reaction, [__] remains essentially unchanged until nearly all of the reactants are consumed.
The diagnostic Lineweaver-Burk plot for uncompetitive inhibition consists of a series _______ lines
A‡(rate k1) is of higher energy than I‡ (rate k2) , making k_ the slower step
_____km = more efficient enzyme
w is work done by the _______ on its __________
Catalyst does not change __
inorganic ions, complex organic, metalloorganic molecules (ex. heme group)
H= ___ + ___
competitive inhibitor is a substance that competes with the substrate for binding to the _______ binding site on the enzyme.
Spontaneous reactions go in the direction of ______ free energy
_________ temperature = greater contribution of entropy
________ regulation will always have a “negative” effect on the reaction rate (slow the kinetics), ________ regulation can result in both positive and negative effects
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’
For uncompetitive inhib., apparent Km is _________ because _______ is ________, but it is inactive so it does NOT indicate that the enzyme is more efficient.
“ready to go,” (apoenzyme + cofactor)
_________ 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 ________)
although uncompetitive inhib. lower KM, the overall effect is________ (Vmax decreases), since the ES complex is subsequently being “sopped up” by the uncompetitive inhibitor.
An otherwise endergonic reaction can be coupled to an exergonic reaction such as ______ ________
∆G˚=∆G_f˚_____ of _______ - ∆G_f˚_____ of _______
high-energy molecules (glucose), which would otherwise rapidly break down into their simpler, low-energy constituents (e.g. _____ and _____).
_____ ______ is actually a transferase
Enzymes are good for reactions in physiological conditions because they allow for _____ reaction conditions
For mixed inhibition plot, when α =α’ lines meet at ___ ______
The universe tends towards maximum disorder: ______ law of Thermodynamics
____∆G will do work on the surroundings
They are supposed to be as efficient as ________ to correctly do their job in an organism.
____∆S = entropically opposed
Mixed inhibition always decreases ______ but may increase or decrease ______
U P V (denoted by uppercase letters) represent ________ _________ which mean they are independent of _______
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%
A catalyst lowers activation energy but more specifically, it does this by lowering the_____ _____ of the _____ _____
A plot of 1/ ___ versus 1/[__] yields a straight line with the slope ________
The magnitude of lowering activation energy, ΔΔG‡, is proportional to the degree of rate ___________
_____ inhibitors generate a complex pattern on a Lineweaver- Burk plot, with the _________ component affecting apparent KM and the _________ component affecting both KM and Vmax
Molecules that react with an enzyme irreversibly and decrease its activity are called ___________
“missing a component,” polypeptide part of the enzyme without its co-factor
Proenzymes, Coenzymes, Apoenzymes and Holoenzymes
The Y intercept is ______
dissolving urea is an _______ reaction
the presence of an _______ is accounted for by α which is calculated by with the equation α = 1 + [I]/KI.
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
large Keq, ∆G is _______
_________: Transfer of electrons or protons (hydride ions or H atoms)
The experimental advantage of measuring ____ is that product inhibition and the reverse reaction are less likely to complicate measurements.
_______ is a measure of catalytic efficiency.
α (or α’) combines _______ of the inhibitor and its ______ for the enzyme
____∆G is only achieved if the surroundings do work on the reaction
q is heat absorbed by the _______ from the ___________
The high specificity of enzymes for their substrates, described by their KMs, means that enzyme catalyzed reactions rarely have non-productive _______ _______
______ regulation is distinct from inhibitory regulation -- refers to a non-substrate regulator binding to a location distant from the active site of the enzyme.
energy barrier between the reactants and products
_____ ______ concentration = [E]T
k_cat represents _______ _______
Competitive inhibitor ___________ apparent Km
A system may attain order at the expense of ____________ its _____________
____ ∆S = entropically favored
For uncompetitive inhib, Vmax is also ________ because the _____ ______ concentration available is decreased.
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
____ is expected to occur when the enzyme is completely saturated with substrate ([E]T = [ES]).
When ∆U=0, ΔS > or =
The relationship between ΔG‡ and the reaction rate (k) is ______and ____________ (i.e. the higher ΔG‡, the _______ the rate (__)).
K_D indicates __________ and is part of ____
____ = k2 [E]T
_______ kcat/km= greater catalytic efficiency
Formula for Km
Enzymes do not alter ___________
Binds ES complex and free enzyme
_____kcat means more efficient enzyme
number of times per sec an enzyme makes a product
____∆H = enthalpically favored
Energy (U) cannot be created nor can it be destroyed: ______ law of Thermodynamics
_________: Addition of groups to double bonds, or formation of double bonds by group removal (____ or _____ double bonds)
Living systems are _______ systems
When V_0=1/2Vmax, Km= [__]
catalysts accelerate the process of reaching Keq, but do not ____ Keq.
___________ inhibitor decreases the catalytic activity of the enzyme without affecting its affinity for substrate
a ______ Km and a _____ kcat are each associated with a more efficient enzyme.
Tense: less active state; higher affinity for the _________
The rate of ___________ is inversely proportional to the change in _________ energy (ΔG‡) and is exponential
at very low [S], the effects of a __________ inhibitor become negligible
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
equation for entropy with Boltzmann's
Some transition state analogs bind _____ ______ than actual transition state meaning they bind at a _____ Km
________ energy, ΔG‡, which represents the energy of a fleeting “______ state” between the substrate and products.
when Keq < 1, ∆G is __________
the X intercept is _____
_________: Transfer of functional groups to water – enzymes that hydrolyze bonds by using water as the _______
The complexity of enzymes allows for multiple additional layers of ________

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