Exam 2 Flashcards
Which amino acid would most likely participate in general acid-base catalysis under basic conditions?
-Tyr
-Ala
-Gln
-Leu
Tyr
Which of the following mechanisms can affect enzymatic activity?
-substrate availability
-covalent modification
-cleavage of a zymogen
-all of the above
All of the above
Which of the following statements is FALSE about allosteric enzymes?
-They are most active in the relaxed (R) form
-They produce a sigmoidal curve
-The regulators associated with them bind only to the active site
-They work quickly and are direct
The regulators associated with them bind only to the active site
Which one of the following mechanisms is NOT known to play a role in the reversible alteration of enzyme activity?
-Alteration of the synthesis or degradation rate of an enzyme
-Allosteric response to a regulatory molecule
-Interactions between catalytic and regulatory subunits
-Activation by cleavage of an inactive zymogen
-Covalent modification of the enzyme
Activation by cleavage of an inactive zymogen.
(The activation of enzymes by proteolytic cleavage is irreversible.)
Which of the following statements regarding allosteric enzymes is true?
-They are always oligomeric
-They are generally found at regulatory sites in metabolic pathways
-They are subject to regulation by both positive and negative effectors.
-A plot of velocity vs. [substrate] often yields a sigmoidal curve
-All of the above
All of the above
Which form of protein regulation is irreversible?
Proteolytic cleavage
Which form of protein regulation occurs most quickly?
Allostery
Which form of protein regulation is most specific?
Allostery
Which form of protein regulation has broad specificity and is reversible?
Phosphorylation
The Lineweaver-Burk plot is also known as the double-_____ plot.
reciprocal
Allosterism…
-means “other shape”
-is induced by binding of another molecule to a protein
-is important to protein regulation
-leads to change in conformation and activity
-all of the above
All of the above
Proteins/enzymes that can be regulated allosterically…
i. show a hyperbolic Michaelis-Menten curve
ii. can be regulated by molecules that differ structurally from a substrate
iii. can be both activated and inhibited
iv. undergo only competitive inhibition
-i, ii, and iii
-i, iii, iv
-i and ii
-i, ii, iii, iv
-ii and iii
ii and iii
-Can be regulated by molecules that differ structurally from a substrate
-Can be both activated and inhibited
(Shows a sigmoidal Michaelis-Menten curve and competitive inhibition is associated with orthosteric regulation)
Enzymes that are allosterically regulated…
-show an activity vs. substrate concentration curve that is sigmoidal
-may be stimulated by allosteric activators
-when inhibited show an activity curve shifted to the right
-both A and B
-all of the above
All of the above
Which of the following statements about phosphorylation of enzymes is FALSE?
-The phosphorylation of an enzyme results in a change in its conformation, thereby increasing its activity.
-Phosphorylation is a reversible covalent modification
-The phosphorylation of enzymes is catalyzed by other enzymes called kinases
-The phosphorylation of enzymes is one mechanism via which hormones elicit an intracellular response.
The phosphorylation of an enzyme results in a change in its conformation, thereby increasing its activity.
(The phosphorylation of an enzyme does alter its conformation, but this may cause either an increase OR a decrease in activity.)
Zymogens are not enzymatically active because _____.
-they do not contain the cofactors required for catalysis
-they are the product of mutated genes
-their active sites are distorted and incapable of enzymatic activity
-the pH of their environment is not optimal for activity
-none of the above
their active sites are distorted and incapable of enzymatic activity
Protein kinases are involved in ______.
-the digestion of drugs to potentially toxic by-products
-the degradation of enzymes to the component amino acids
-the phosphorylation of a wide variety of proteins
-the metabolism of drugs to water soluble, excretable compounds
-all of the above
the phosphorylation of a wide variety of proteins
What is the difference between allosteric and orthosteric regulation?
-All enzymes are regulated orthosterically only.
-All enzymes are regulated allosterically only.
-Only in allosteric regulation of an enzyme does the substrate bind to the active site
-In allosteric regulation of an enzyme, the substrate binds to the allosteric site
-In allosteric regulation of an enzyme, a molecule other than the substrate binds a site other than the active site.
In allosteric regulation of an enzyme, a molecule other than the substrate binds a site other than the active site.
In the sequential model of allosterism, as regulatory molecules bind to allosteric sites,
-the active site-containing subunit shifts from T to R state
-the active site-containing subunit is activated
-the entire complex exists in the T or R state
-subunits in the T state have high affinity
-both A and B
Both A and B
Heterotropic regulation
i. occurs with a molecule other than the protein’s substrate
ii. occurs with regulator binding at a site other than the active site
iii. influences substrate binding
iv. is a type of competitive inhibition
-i and ii
-ii and iii
-ii, iii, and iv
-i, iii, and iv
-i, ii, and iii
i, ii, and iii
As associated with hemoglobin, heme is considered a ____.
-catalyst
-subunit
-coenzyme
-cofactor
-none of the above
cofactor
In its reduced form, the central ion of the heme group of hemoglobin is _____.
-Cu+
-Cu2+
-Fe2+
-Fe3+
-none of the above
Fe2+
Myoglobin is _____; hemoglobin is _____.
-monomeric; dimeric
-monomeric; trimeric
-monomeric; tetrameric
-dimeric; trimeric
-dimeric; tetrameric
Monomeric; tetrameric
The individual hemoglobin subunits and myoglobin share similar _____ structure but have rather different _____ structure.
-primary; secondary
-secondary; tertiary
-primary; tertiary
-secondary and tertiary; primary
-primary and secondary; tertiary
secondary and tertiary; primary
A plot of the binding of oxygen to myoglobin as a function of pO2 gives a ____ shape; a similar plot for hemoglobin gives a _____ shape.
-sigmoidal; sigmoidal
-sigmoidal; hyberbolic
-hyberbolic; sigmoidal
-hyperbolic; hyperbolic
-hyperbolic; exponential
hyperbolic; sigmoidal