Science Quiz / GU MCP Lectures 7,8,9

Random Science Quiz

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

 Plays Quiz not verified by Sporcle

Forced Order
Also try: Pop Quiz: Anatomy
Score 0/114 Timer 20:00
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’
U P V (denoted by uppercase letters) represent ________ _________ which mean they are independent of _______
Energy (U) cannot be created nor can it be destroyed: ______ law of Thermodynamics
∆G˚=∆G_f˚_____ of _______ - ∆G_f˚_____ of _______
A‡(rate k1) is of higher energy than I‡ (rate k2) , making k_ the slower step
Formula for Km
The _________ of the Michaelis-Menineton ________ is a line known as the Double-Reciprocal or Lineweaver-Burk Plot
the presence of an _______ is accounted for by α which is calculated by with the equation α = 1 + [I]/KI.
The universe tends towards maximum disorder: ______ law of Thermodynamics
Km has units of ________
An uncompetitive inhibitor binds ONLY to the___ ______
For mixed inhibition plot, when α =α’ lines meet at ___ ______
“missing a component,” polypeptide part of the enzyme without its co-factor
_______ kcat/km= greater catalytic efficiency
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
Spontaneous only at T>∆H/∆S, ____∆H and ____ ∆S
The primary goal of many drugs that target enzymes is to _______ or _______ the activity of enzymes.
They are supposed to be as efficient as ________ to correctly do their job in an organism.
_____ ______ concentration = [E]T
A system may attain order at the expense of ____________ its _____________
When V_0=1/2Vmax, Km= [__]
____ = k2 [E]T
The _____ ______ ______ puts forth that after a rapid transient phase of the reaction, [__] remains essentially unchanged until nearly all of the reactants are consumed.
although uncompetitive inhib. lower KM, the overall effect is________ (Vmax decreases), since the ES complex is subsequently being “sopped up” by the uncompetitive inhibitor.
_______ ________ _______ chemical compounds with a chemical structure that resembles the transition state of a substrate molecule in an enzyme-catalyzed chemical reaction
For uncompetitive inhib, Vmax is also ________ because the _____ ______ concentration available is decreased.
Some transition state analogs bind _____ ______ than actual transition state meaning they bind at a _____ Km
Lineweaver-Burk is also called a ______ ______ plot
high-energy molecules (glucose), which would otherwise rapidly break down into their simpler, low-energy constituents (e.g. _____ and _____).
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
________ regulation will always have a “negative” effect on the reaction rate (slow the kinetics), ________ regulation can result in both positive and negative effects
Catalyst does not change __
Move group to another location on the same molecule to yield isomeric forms
Mixed inhibition always decreases ______ but may increase or decrease ______
A catalyst lowers activation energy but more specifically, it does this by lowering the_____ _____ of the _____ _____
______ regulation is distinct from inhibitory regulation -- refers to a non-substrate regulator binding to a location distant from the active site of the enzyme.
catalysts accelerate the process of reaching Keq, but do not ____ Keq.
The high specificity of enzymes for their substrates, described by their KMs, means that enzyme catalyzed reactions rarely have non-productive _______ _______
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%
K_D indicates __________ and is part of ____
_________ temperature = greater contribution of entropy
_________: Group-transfer reactions to another ______. Examples: methyl-transferase or phosphoryl-transferases (a.k.a.______)
Enzymes do not alter ___________
α (or α’) combines _______ of the inhibitor and its ______ for the enzyme
_____ ______ is actually a transferase
Binds ES complex and free enzyme
The diagnostic Lineweaver-Burk plot for uncompetitive inhibition consists of a series _______ lines
Tense: less active state; higher affinity for the _________
number of times per sec an enzyme makes a product
For uncompetitive inhib., apparent Km is _________ because _______ is ________, but it is inactive so it does NOT indicate that the enzyme is more efficient.
____∆H = enthalpically favored
_____ inhibitors generate a complex pattern on a Lineweaver- Burk plot, with the _________ component affecting apparent KM and the _________ component affecting both KM and Vmax
H= ___ + ___
Relaxed: more active state; higher affinity for the ________
at very low [S], the effects of a __________ inhibitor become negligible
Spontaneous reactions go in the direction of ______ free energy
____∆S = entropically opposed
The complexity of enzymes allows for multiple additional layers of ________
_____km = more efficient enzyme
_________ 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 ________)
The magnitude of lowering activation energy, ΔΔG‡, is proportional to the degree of rate ___________
competitive inhibitor is a substance that competes with the substrate for binding to the _______ binding site on the enzyme.
All ________ systems must reach equilibrium
Slope (m) Lineweaver-Burk Plot=
If a catalyst decreases the activation energy by a factor of 2, it increases the reaction rate by a factor of ____
Km = [S] when ____ = ½ Vmax.
___________ inhibitor lowers both the apparent KM and Vmax, but KM/Vmax, the slope of the lines, remains ______
the X intercept is _____
when Keq < 1, ∆G is __________
The Y intercept is ______
An otherwise endergonic reaction can be coupled to an exergonic reaction such as ______ ________
kcat, or the _______ number, which is the number of times the enzyme turns over and does its job again per unit time
____∆G will do work on the surroundings
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
A plot of 1/ ___ versus 1/[__] yields a straight line with the slope ________
q is heat absorbed by the _______ from the ___________
____ is expected to occur when the enzyme is completely saturated with substrate ([E]T = [ES]).
Formula for K_D =
The rate of ___________ is inversely proportional to the change in _________ energy (ΔG‡) and is exponential
The lines of a competitive inhibitor plot meet at the ___ _____
____ ∆S = entropically favored
energy barrier between the reactants and products
Proenzymes, Coenzymes, Apoenzymes and Holoenzymes
“ready to go,” (apoenzyme + cofactor)
a ______ Km and a _____ kcat are each associated with a more efficient enzyme.
_________: Transfer of electrons or protons (hydride ions or H atoms)
Two steps: ________ substrate binding to enzyme and __________ formation of products from ES complex
The relationship between ΔG‡ and the reaction rate (k) is ______and ____________ (i.e. the higher ΔG‡, the _______ the rate (__)).
Competitive inhibitor ___________ apparent Km
When ∆U=0, ΔS > or =
A protein folds into secondary and tertiary structures in order to maximize the _________ of _________
Molecules that react with an enzyme irreversibly and decrease its activity are called ___________
dissolving urea is an _______ reaction
large Keq, ∆G is _______
The initial velocity (v0) is defined as the velocity that is achieved when less than ____% of the ________ have been consumed.
____∆G is only achieved if the surroundings do work on the reaction
________ energy, ΔG‡, which represents the energy of a fleeting “______ state” between the substrate and products.
___________ inhibitor decreases the catalytic activity of the enzyme without affecting its affinity for substrate
Living systems are _______ systems
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___ _______
equation for entropy with Boltzmann's
inorganic ions, complex organic, metalloorganic molecules (ex. heme group)
_______ is a measure of catalytic efficiency.
_____kcat means more efficient enzyme
_________: Addition of groups to double bonds, or formation of double bonds by group removal (____ or _____ double bonds)
Enzymes are good for reactions in physiological conditions because they allow for _____ reaction conditions
The experimental advantage of measuring ____ is that product inhibition and the reverse reaction are less likely to complicate measurements.
inactive precursor that needs to be activated by a proteolytic step ex. zymogen
_________: Transfer of functional groups to water – enzymes that hydrolyze bonds by using water as the _______
Primary structure of a protein has low entropy because it is forcing _______ to be more _________
w is work done by the _______ on its __________
k_cat represents _______ _______
when ∆U=0,

You're not logged in!

Compare scores with friends on all Sporcle quizzes.
Join for Free
Log In

You Might Also Like...

Show Comments


Created Aug 11, 2011ReportFavoriteNominate

Top Quizzes Today

Score Distribution

Your Account Isn't Verified!

In order to create a playlist on Sporcle, you need to verify the email address you used during registration. Go to your Sporcle Settings to finish the process.

Report this User

Report this user for behavior that violates our Community Guidelines.