Accounting
Anthropology
Archaeology
Art History
Banking
Biology & Life Science
Business
Business Communication
Business Development
Business Ethics
Business Law
Chemistry
Communication
Computer Science
Counseling
Criminal Law
Curriculum & Instruction
Design
Earth Science
Economic
Education
Engineering
Finance
History & Theory
Humanities
Human Resource
International Business
Investments & Securities
Journalism
Law
Management
Marketing
Medicine
Medicine & Health Science
Nursing
Philosophy
Physic
Psychology
Real Estate
Science
Social Science
Sociology
Special Education
Speech
Visual Arts
Chemistry
Q:
All of the following affect microtubule polymerization and are used in cancer chemotherapy EXCEPT:
a. Taxol.
b. colchicine.
c. vinblastine.
d. vincristine.
e. all are used.
Q:
The proposed sequence for kinesin movement along a microtubule is:
A. Leading head binds a new site on tubulin with ADP dissociation.
B. The kinesin head with ATP is bound to tubulin, and the kinesin head with ADP is ready to move ahead.
C. Conformation change in the neck linkers flipping the trailing head to the next tubulin binding site.
D. ADP and Pi dissociation and ATP binds leading head.
a. D, C, B, A
b. B, C, A, D
c. B, D, A, C
d. A, C, B, D
e. C, A, D, B
Q:
Kinesins are proteins that exhibit ATPase activity and are involved with:
a. movement of flagella.
b. movement of cilia.
c. movement of muscles.
d. intracellular movement of organelles and vesicles from the minus end to plus end of microtubules.
e. A-tubule and B-tubule movement within an axoneme.
Q:
Intracellular movement of organelles in axons occurs through:
a. axoneme motion through ATP-driven walking of dyneins along microtubules.
b. formation of ring-like structures around tubulin to move organelles.
c. progressive movement along DNA strands.
d. kinesin-mediated ATPase driven movement along microtubules.
e. all of the above.
Q:
All are true for ciliary motion EXCEPT:
a. complex bundles of microtubular fibers form axoneme.
b. axoneme are surrounded by plasma membrane that is continuous with the plasma membrane of the cell.
c. dynein molecules bridge between microtubules alternating their "walking" along both bridging microtubules.
d. ATP-driven sliding or walking of dyneins occurs along microtubules.
e. the result is a bending motion of axoneme and subsequent bending of the cilia.
Q:
All are functions of microtubules EXCEPT:
a. providing variations and maintenance of cell shape.
b. formation of the mitotic spindle during cell division.
c. unwinding DNA to single-stranded DNA (ssDNA).
d. movement of organelles.
e. forming intracellular scaffolds.
Q:
Treadmilling as carried out by microtubules means:a. ATP-hydrolysis-dependent movement over a plane.b. ATP-dependent addition of dimmers to the plus end.c. GTP-hydrolysis-dependent movement of -tubulin over -tubulin.d. GTP-dependent addition to the plus end and removal at the minus end.e. ATP-dependent "walking" along a surface in one place.
Q:
All of the following are characteristics of microtubules EXCEPT:
a. they are made up of two repeating subunits.
b. they grow at one end and are degraded at the other end.
c. they are static, helical structures.
d. they are hollow, cylindrical structures.
e. they are polar structures.
Q:
Self-assembly of microtubules occur by:
Q:
Microtubules are ____ structures formed from ____.
a. solid; myosin
b. self-assembling; phospholipids
c. hollow; membranes
d. self-assembling; tubulin
e. solid; tubulin
Q:
All are characteristics of molecular motors or motor proteins EXCEPT:
a. They must be able to associate and dissociate reversibly with a polymeric protein array, a surface or substructure in the cell.
b. They use chemical energy (e.g., ATP) to orchestrate movement.
c. They transfer ATP energy into mechanical energy.
d. ATP hydrolysis is presumed to drive and control protein conformational changes that result in sliding or walking movement of one molecule relative to another.
e. All are true.
Q:
Of the following, which promotes the release of oxygen by hemoglobin?
a. increase in [H+]
b. decrease in [CO2]
c. decrease in [2,3-bisphosphoglycerate]
d. Tyr HC2-Val FG5 hydrogen bond breaking
e. none of the above
Q:
Which of the following statements regarding enzyme regulation is true?
a. the conversion of trypsinogen to trypsin is an example of zymogen activation
b. allosteric effectors are always more powerful than covalent modification
c. addition of an inhibitor to a V system results in kinetics similar to addition of a competitive inhibitor to a typical hyperbolic system
d. the T state of an enzyme generally has more activity than the R state
e. none of the above
Q:
Which of the following will cause an increase in the activity of glycogen phosphorylase?
a. binding of ATP to the allosteric site
b. phosphorylation of the enzyme
c. high levels of glucose-6-phosphate
d. conversion from the relaxed to tense state
e. drinking coffee
Q:
The cause of cell sickling in sickle cell anemia is:
a. interaction of oxy-Hb S with the cell membrane.
b. precipitation of deoxy-Hb S into long, chain-like fibers.
c. formation of oxy-Hb S complexes and subsequent cell disruption.
d. precipitation of Hb S - Hb A hybrid molecules.
e. none of the above.
Q:
Fetal hemoglobin (Hb F) has an intrinsically greater affinity for O2
than adult hemoglobin (Hb A) because:
a. Hb F has a diminished capacity to bind BPG compared to Hb A.
b. Hb A has a greater affinity for oxygen than does Hb F.
c. BPG binds Hb F with greater affinity than it binds Hb A.
d. The pH of fetal blood is less than the pH of maternal blood.
e. All of the above are correct.
Q:
BPG shifts the oxygen saturation curve of Hb to the ____ because BPG binds to ____ making Hb an O2delivery system eminently suited for ____.
a. right; deoxyHb; humans and other primates
b. right; deoxyHb; cattle, sheep and goats
c. left; oxyHb; cattle, sheep and goats
d. left; oxyHb; humans and other primates
e. none of the above
Q:
All of the following are characteristics of hemoglobin's binding of oxygen EXCEPT:
a. CO2 promotes dissociation of O2 from hemoglobin by lowering the pH.
b. Protons promote binding of oxygen by Hb.
c. 2,3-Bisphosphoglycerate (BPG) promotes release of O2 by Hb.
d. CO2 can bind with Hb's free amino groups and stabilize deoxy-Hb.
e. BPG and O2 are mutually exclusive allosteric effectors of Hb.
Q:
Carbon dioxide affects O2binding to Hb by:a. Hb competing with carbonic anhydride for CO2.b. directly binding to heme-Fe in the oxygen binding site.c. forming iron carbonate with the heme-iron.d. forming H+ + HCO3- where the H+ is an antagonist to oxygen binding to Hb.e. forming HCO3- that combines with H+ to increase CO2 binding.
Q:
Which of the following is true regarding effectors of oxygen-hemoglobin binding?
a. actively metabolizing tissues produce acid which increases hemoglobin's affinity for oxygen
b. the presence of CO2 enhances the release of oxygen from hemoglobin
c. 2,3-bisphosphoglycerate must dissociate from hemoglobin before oxygen can be released
d. the presence of protons will counter the effect of CO2 on the realease of oxygen by hemoglobin
e. none of the above
Q:
The T form (tense or taut form) of deoxyhemoglobin differs from oxyhemoglobin (the R form or relaxed form) by all EXCEPT:a. covalent linkages between subunits.b. specific intrachain hydrogen bonds.c. between -subunit salt links (ion-pair bonds).d. between -subunits salt links (ion-pair bonds).e. intrachain salt bridges.
Q:
We are protected to some extent against low level CO poisoning because:
a. His F8 on Hb distorts the heme iron atom out of the heme plane and attracts O2, but not CO.
b. Affinity of Hb for O2 is much greater than for CO.
c. His E7 blocks perpendicular binding of CO to heme iron allowing for better binding competition by O2.
d. The competition of O2 for heme is much greater than CO for heme.
e. None of the above.
Q:
When O2binds to heme in hemoglobin, the ____ ion is drawn into the plane of the ____ causing a conformational change that is transmitted to adjacent subunits enhancing the ____ for additional O2binding.
a. Mg2+; globin; planarity
b. Fe3+; heme; folding
c. Mg2+; globin; attraction
d. Fe3+; porphyrin; affinity
e. Fe2+; porphyrin; affinity
Q:
Which statement below about contrasting Hb and Mb is FALSE?
a. Hb shows sigmoidal, whereas Mb shows hyperbolic oxygen saturation curves.
b. Hb shows cooperativity, whereas Mb does not.
c. Hb binds O2 more tightly than Mb.
d. Oxygen binds to a ferrous ion in both proteins.
e. Hb-oxygen binding is dependent on physiological changes in pH, whereas Mb-oxygen binding is not.
Q:
The polypeptide of myoglobin serves all of the following functions EXCEPT:
a. protects the heme iron from oxidation.
b. cradles the heme group.
c. provides a pocket for O2 to fit.
d. keeps the heme iron in the ferric form.
e. none of the above.
Q:
Adenylyl cyclase catalyzes the synthesis of cAMP, and cAMP hydrolysis is catalyzed by a 5'-phosphodiesterase. If caffeine inhibits 5'-phosphodiesterases, drinking a caffeinated beverage would ____ cAMP levels and ____ glycogen phosphorylase activity.
a. increase; decrease
b. increase; increase
c. decrease; decrease
d. decrease; increase
e. have no effect; have no effect
Q:
Glycogen phosphorylase displays allosteric activation and inhibition by multiple modes. Which of the following is a correct relation?
a. phosphate: positive heterotropic effector
b. AMP: negative heterotropic effector
c. ATP: positive heterotropic effector
d. glucose-6-phosphate: negative heterotropic effector
e. phosphorylation: covalent inhibitor
Q:
All are true for cAMP-dependent protein kinase EXCEPT:
a. also known as PKA.
b. phosphorylase kinase is a substrate.
c. consists of a pair of catalytic subunits.
d. two regulatory subunits block catalytic activity without cAMP binding.
e. phosphorylates glycogen phosphorylase.
Q:
The subunit of GTP-binding protein (G protein) has all of the following characteristics EXCEPT:a. activates adenylyl cyclase.b. hormone-receptor complex promotes release from .c. has a very active GTPase activity.d. binds GDP in the complex.e. GTP hydrolysis leads to -adenylyl cyclase dissociation.
Q:
The correct sequence for the hormone-activated enzymatic cascade that leads to activation of glycogen phosphorylase is:
A. Phosphorylation to activate phosphorylase kinase
B. Activation of G-protein
C. Activation of adenylyl cyclase to produce cAMP
D. Phosphorylation of glycogen phosphorylase
E. cAMP activation of protein kinase A (PKA)
a. A, B, C, D, E
b. B, C, E, A, D
c. C, B, A, D, E
d. B, D, E, A, C
e. E, A, D, C, B
Q:
For muscle glycogen phosphorylase, Pi(inorganic phosphate) is a:
a. positive homotropic effector.
b. negative homotropic effector.
c. positive heterotropic effector.
d. negative heterotropic effector.
e. none of the above.
Q:
Characteristics of glycogen phosphorylase include all EXCEPT:
a. covalently linked pyridoxal phosphate.
b. an active site at the center of each of two identical subunits.
c. regulatory phosphorylation site on a Ser residue.
d. allosteric effector sites for ATP and glucose-6-phosphate.
e. all are true.
Q:
The function of glycogen phosphorylase is:
a. the conversion of glucose-1-phosphate to glucose-6-phosphate.
b. to break down ATP.
c. to catalyze the phosphorolysis of glucose-1-phosphate from glycogen molecules.
d. to inhibit the production of glucose-1-phosphate.
e. to stimulate the build up of glycogen.
Q:
The addition of an effector to an enzyme that acts as a Ksystem of the MWC model causes the half-maximum velocity (K0.5) to ____ and Vmaxto ____.
a. remain constant; remain constant
b. remain constant; change
c. change; remain constant
d. change; change
e. none of the above
Q:
An enzyme that displays negative cooperativity has ____ activity when the substrate is present at concentrations ____ than the value of K0.5 when compared with enzymes that display no cooperativity.
a. increased; greater
b. increased; less
c. decreased; greater
d. decreased; less
e. both b and c are correct
Q:
The presence of a negative allosteric effector on an allosteric protein would:
a. cause a shift to the left in the sigmoidal curve.
b. increase the number of R conformations.
c. decrease the cooperativity of the substrate.
d. raise the apparent value of the equilibrium constant, L.
e. increase the likelihood of the binding of S.
Q:
When binding one equivalent of S to an allosteric protein enhances the binding of additional equivalents of S to the same protein molecule, it is termed a(n):
a. positive heterotropic effector.
b. positive homotropic effector.
c. negative heterotropic effector.
d. negative homotropic effector.
e. none of the above.
Q:
Which of the following statements regarding enzyme regulation is true?
a. addition of an inhibitor to a V system results in kinetics similar to addition of a competitive inhibitor to a typical hyperbolic system
b. allosteric effectors are always more powerful than covalent modification
c. addition of an allosteric activator to a K system changes the plot of V vs. [S] from a sigmoidal curve to a more hyperbolic curve
d. the T state of an enzyme generally has more activity than the R state
e. none of the above are true
Q:
All are properties of regulatory enzymes EXCEPT:
a. pathway end-products may act as allosteric inhibitors.
b. v vs [S] plots are sigmoid- or S-shaped.
c. substrate binding is cooperative.
d. monomeric enzymes with a single regulated active site.
e. may be stimulated by allosteric activators.
Q:
All are characteristic of allosteric enzymes EXCEPT:
a. Effectors may show stimulatory or inhibitory activity.
b. They have multiple subunits.
c. They obey Michaelis-Menten kinetics.
d. The regulatory effect is by altering conformation and interaction of subunits.
e. Binding one subunit impacts binding of substrate to other subunits.
Q:
All are true about isozymes of lactate dehydrogenase (LDH) that are present in a number of different tissues EXCEPT:
a. They have differing Km values for lactate.
b. The amount of subunit phosphorylation differs.
c. They have differing Km values for pyruvate.
d. The ratios of A and B subunits differ depending upon the tissue type
e. They have different kinetic parameters.
Q:
Which of the following statements is correct regarding isozymes?
a. they catalyze the same reaction but have vastly different structures
b. they are always monomeric proteins
c. their differences are based upon the type of tissue in which they are present
d. they often respond to different inhibitors and activators
e. both c and d are correct
Q:
Usually the quickest method of influencing an enzymatic activity is by:
a. allosteric regulation.
b. covalent modification.
c. enzyme induction.
d. activation of a zymogen.
e. enzyme destruction.
Q:
Regulation of metabolism by activation of the gene encoding a particular enzyme is called ____.
a. covalent modification
b. repression
c. induction
d. allosteric activation
e. none of the above
Q:
Proinsulin is converted into insulin by:
a. proteolytic excision of a specific peptide.
b. allosteric binding of glucose.
c. phosphorylation to the active form.
d. removal of phosphate by converter enzymes.
e. none of the above.
Q:
All of the following are examples of a zymogen and its activating protease EXCEPT:
a. chymotrypsinogen and chymotrypsin.
b. procarboxypeptidase and elastase.
c. proelastase and elastase.
d. pepsinogen and pepsin.
e. trypsinogen and trypsin.
Q:
All of the following are correct statements about enzyme regulation EXCEPT:
a. Enzymes can be inhibited by the products they produce.
b. Enzymes can be inactivated by the addition of a functional group.
c. Coenzyme and substrate availability can regulate enzyme reaction rate.
d. The reaction rate slows as equilibrium is approached.
e. The activity of an enzyme is covalently affected by allosteric regulators.
Q:
If the substrate for an enzyme catalyzed reaction contained a negative charge, which of the following amino acids would most likely be present in the active site to provide electrostatic destabilization of the ES complex?
a. Val
b. Asp
c. Arg
d. Ser
e. Gln
Q:
If the transition state of an enzyme catalyzed reaction contained a positive charge, which of the following amino acids would most likely be present in the active site to aid in transition state formation?
a. Lys
b. Val
c. Asn
d. Glu
e. Cys
Q:
Which of the following statements regarding enzymes is true?
a. stabilization of the transition state must be less than stabilization of ES for catalysis to occur
b. an enzyme mechanism is vastly different from the uncatalyzed reaction
c. binding of substrate to an enzyme often causes strain, thus promoting transition state formation
d. a random single displacement mechanisms requires that substrates bind to the enzyme in a specific order
e. none of the above
Q:
Which of the following are relevant to the reaction catalyzed by chorismate mutase?
a. the reaction involves a concerted intramolecular rearrangement of chorismate to prephenate during the synthesis of phenylalanine.
b. the enzyme catalyzed and uncatalyzed reactions follow almost identical routes
c. the enzymatic reaction is thought to involve transition state stabilization by 12 electrostatic and hydrogen bond interactions
d. the geometry of the enzyme active site is such that the difference in energy between ES and the near attack conformation is less than 1 kJ/mol
e. all of the above are true
Q:
Effective HIV-1 protease inhibitors should have all of the following characteristics EXCEPT:a. effective delivery in sufficient quantities to the desired site(s) of action in the organism.b. relative specificity for the HIV-1 protease.c. a backbone -OH group that forms a weak association with the two active-site carboxyl groups of the protease.d. results in inhibiting the production of new virus particles in cells of infected patients.e. broad spectrum enough to be effective against mutant viral forms.
Q:
HIV-1 protease is different from most mammalian aspartic acid proteases in that it has:
a. two subunits each with a two-aspartate active site.
b. two subunits each contributing an aspartate to the active site.
c. two active sites on one protein.
d. two subunits, one with an active site, and the other with a regulatory activity.
e. none of the above.
Q:
The mechanism of aspartate protease catalysis is proposed to be:
a. covalent nucleophilic catalysis.
b. covalent electrophilic catalysis.
c. specific base catalysis.
d. general base-general acid catalysis facilitated by a low barrier hydrogen bond.
e. all of the above.
Q:
Aspartate proteases display a variety of substrate specificities, but normally they are most active in cleavage of peptide bonds:
a. on the carboxyl side of the basic amino acids.
b. on the carboxyl side of aromatic amino acids.
c. on the carboxyl side of small, neutral residues.
d. between two hydrophobic amino acid residues.
e. none of the above.
Q:
In the chymotrypsin reaction mechanism there is a low-barrier hydrogen bond (LBHB) formed between:
a. Asp102 and Ser195.
b. Asp102 and His57.
c. His57 and Ser195.
d. Ser195 and carbonyl oxygen in the peptide bond.
e. None of the above.
Q:
The initial bond formation in the covalent intermediate in the chymotrypsin catalyzed reaction is between:
a. serine and the carbonyl carbon in the peptide backbone.
b. serine and the nitrogen in the peptide backbone.
c. histidine and the carbonyl carbon in the peptide backbone.
d. histidine and the nitrogen in the peptide backbone.
e. aspartate and the carbonyl carbon in the peptide backbone.
Q:
Organic fluorophosphates are ____ inhibitors of serine proteases such as chymotrypsin.
a. competitive
b. uncompetitive
c. noncompetitive
d. irreversible
e. mixed noncompetitive
Q:
In the hydrolysis of p-nitrophenylacetate by chymotrypsin all of the following are correct EXCEPT:
a. the first product is acetic acid.
b. an acetyl-enzyme intermediate forms during the mechanism.
c. attack of a water molecule on the acyl-enzyme intermediate yields the second product.
d. the active site contains a serine residue, an unprotonated histidine, and an unprotonated aspartate residue at pH 7.0 prior to binding the substrate.
e. none of the above.
Q:
In the catalytic triad common to many serine proteases, _____ increases the basicity of _____, thus allowing deprotonation of _____ to serve as a nucleophile.
a. Ser-His-Asp
b. His-Ser-Asp
c. Ser-His-His
d. Asp-His-Ser
e. Cys-His-Ser
Q:
The mechanism of chymotrypsin involves which of the following elements?
a. deprotonation of an active site Asp residue by His to start the reaction
b. formation of an acyl-enzyme intermediate that must be hydrolyzed to complete the reaction
c. stabilization of the positively charged His by a Gln residue
d. direct deprotonation of water by His to generate a hydroxide ion for initiation of the reaction
e. both a and b occur
Q:
Metal ion catalysis include all EXCEPT:
a. increased acidity of a nucleophile with an ionizable proton.
b. metal ion requirement to maintain the stable, native state of the enzyme.
c. metal binding weakly, perhaps only during the catalytic cycle.
d. electrophilic catalysis, stabilizing the increased electron density or negative charge that can develop during a reaction.
e. all are true.
Q:
The catalytic mechanism below is an example of: a. covalent nucleophilic catalysis.
b. covalent electrophilic catalysis.
c. specific base catalysis.
d. general base catalysis.
e. low barrier hydrogen bond catalysis.
Q:
All are true for low-barrier hydrogen bonds EXCEPT:
a. The hydrogen is centered between the two heteroatoms.
b. The interactions are more covalent.
c. The bond order approaches 0.5 for both Oï€H interactions.
d. The barrier that the hydrogen atom must surmount to exchange oxygens becomes lower.
e. All are true.
Q:
Because the pKais near 7, ____ side-chains are often involved in general acid-base catalysis.
a. cysteine
b. aspartate
c. glutamate
d. lysine
e. histidine
Q:
Which of the following amino acids would NOT provide a nucleophilic center for covalent catalysis?
a. alanine
b. lysine
c. glutamic acid
d. serine
e. cysteine
Q:
Since enzymes are not rigid molecules but rather flexible proteins, which of the following may be attributed to this fact?
a. active sites are able to conform to the shape of the substrate
b. catalytic residues are oriented in such as way to aid in bond breakage and bond formation
c. strain is placed upon the substrate while it binds to the enzyme
d. near-attack conformations are achieved during formation of the transition state during an enzyme catalyzed reaction
e. all of the above are correct
Q:
Most covalent catalysis is carried out by enzymes using a:
a. ping-pong kinetic mechanism.
b. sequential bisubstrate kinetic mechanism.
c. random bisubstrate kinetic mechanism.
d. simple unimolecular kinetic mechanism.
e. none of the above.
Q:
Transition-state analogs are:
a. approximations of the transition state that bind more tightly than the substrate.
b. compounds that compete for the active site, but are not necessarily very similar to the substrate.
c. stable molecules that can not be expected to resemble the true transition state too closely.
d. stable chemically and structurally similar molecules to the transition state.
e. all of the above.
Q:
The good transition state analog is one which would serve also as an extremely effective:
a. competitive inhibitor.
b. noncompetitive inhibitor.
c. allosteric inhibitor.
d. mixed-noncompetitive inhibitor.
e. irreversible inhibitor.
Q:
The transition state has an estimated life-time of about:a. microseconds (10-6 s).b. nanoseconds (10-9 s).c. (10-2 s).d. (10-14 to 10-13 s).e. milliseconds (10-3 s).
Q:
An enzyme-catalyzed reaction rate will be increased if the energy level of ES can be increased. Which of the following will not increase the energy level of ES?
a. destabilization of ES by strain caused by non-covalent interactions between E and S.
b. loss of entropy due to binding of E and S.
c. destabilization of ES by distortion.
d. destabilization of ES by solvation.
e. destabilization of ES by electrostatic effects.
Q:
Because the enzymatic reaction rate is determined by the difference in energy between ES and ____, the tighter binding of the substrate, the ____ the rate of reaction.
a. S; higher
b. P; lower
c. EX; lower
d. EX; higher
e. S; lower
Q:
Which of the following statements regarding enzymes and transition states is true?
a. stabilization of the transition state must be less than stabilization of ES for catalysis to occur
b. binding of substrate to an enzyme often causes strain, thus promoting transition state formation
c. the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state
d. formation of the transition state always assures that the reaction will proceed to product
e. none of the above are true
Q:
All are catalytic mechanisms or factors that contribute to the performance of enzymes EXCEPT:
a. entropy gain in ES formation.
b. covalent catalysis.
c. general acid or base catalysis.
d. proximity and orientation.
e. all are true.
Q:
All are true for the enzyme-transition state complex EXCEPT:
a. It is designated as EX.
b. The enzyme stabilizes the transition-state complex more than it stabilizes the substrate complex.
c. The enzyme is "designed" to bind the transition-state structure more tightly than the substrate or product.
d. The energy barrier between ES and EX is less than the energy barrier between S and X.
e. All are true.
Q:
Enzymes have active sites which have the greatest complementarity to the:
a. substrate.
b. transition state.
c. product.
d. both substrate and product.
e. none of the above.
Q:
Carbonic anhydrase has two substrates, carbon dioxide and bicarbonate, which are both converted to carbonic acid. Kinetic data for each is given below. Typical values for Kcat/Kmrange from less than 1 mM-1sec-1to as high as 2.8x105 mM-1sec-1. What can be said about the Kcat/Kmfor CO2? a. carbonic anhydrase binds CO2 well but poorly converts it to carbonic acidb. carbonic anhydrase binds CO2 poorly but effectively converts it to carbonic acidc. carbonic anhydrase binds CO2 well and converts it to carbonic acid very welld. carbonic anhydrase binds CO2 poorly and poorly converts it to carbonic acide. the data above is useless for this question
Q:
Carbonic anhydrase has two substrates, carbon dioxide and bicarbonate, which are both converted to carbonic acid. Kinetic data for each is given below. While determining the kinetics of HCO3-as a substrate, how would the addition of CO2 effect the reaction if the rate were measured by the disappearance of bicarbonate? a. CO2 would increase the activity of the enzymeb. CO2 would cause an apparent decrease in the Km for HCO3-c. CO2 would act as a noncompetitive inhibitord. CO2 would act as a competitive inhibitore. none of the above
Q:
Which of the following statements regarding inhibitors is correct?
a. a transition state analog binds covalently to the enzyme
b. a non-competitive inhibitor causes an increase in the Vmax
c. the presence of a competitive inhibitor can be overcome by addition of more inhibitor
d. a competitive inhibitor results in a higher apparent Km value
e. none of the above are correct