Which of the following is incorrect? a. None; all the other choices are correct O b. Reactions with multiple substrates do not follow the Michaelis-Menten kinetics C. Reactions catalyzed by allosteric enzymes follow the Michaelis-Menten kinetics d. Reactions proceeding via multiple steps do not follow the Michaelis-Menten kinetics
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- Question 23 An enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation... SHOW MORE V The Km for X will be affected if Y is present in the reaction mixture. a Y is a competitive inhibitor of X. The Km for X will increase. d. The V for X will be affected if Y is present in the reaction mixture. max pH dependence of Vmax reflects the ionization state of catalytic site e residues. Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X = 0.01 M and the Km for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of g products to reactants (Keg).1. Bzyines play an important role in biochemical reactions. Consider the following statements relating to enzyme-catalysed reactions 1. The shapes of the substrate and the active site of the enzyme are complementary 1. when enzymes are denatured, the shane and structure of the active sites are not altered HI. The substrate forms bonds with the active site of the enzyme Of these statements A. only I is true B. only III is true only I and Ilf are true all statements are true 2. Entropy of the system represents: A. The number and kind of bonds B. The absolute temperature of the reaction Randomness or disorder or the components of a chemical system D. The free energy change of the reaction E. All of the above 3. What is removed from pyruvate during its conversion into an acetyl group? A. Oxygen qB. ATP C. FAD* carbon dioxide 4 Cofactors A. increase activation energy B. help facilitate enzyme activity С. are very rare in living organisms X D break hydrogen bonds in proteins E. are linked to…Which of the followingdescribe superior properties of enzymes (biological catalysts) over traditional chemical catalysts? a. They are mostly and generally operative under mild temperature, pressure, and pH conditions b. They are regulated only by substrate concentration c. They do not effect the reaction equilibrium, but lower the reaction's activation energy d. They are recycled at the end of the reaction Choose all that apply
- a particular enzyme catalyzes a single reactant S to a single product P, following michaelis-menten kinetics rp=(VmaxCs) / (Km + Cs) 1. A reaction with this enzyme is carried out at very low substrate concentrations. Draw and label a curve on the plot that describes the reaction kinetics under those conditions.1. In zero order reaction, the reaction rate depends only on enzyme concentration. In first order reaction the reaction rate is directly porportional to substyrate concentration a. first statement is false and second statement is true b. both statement is true c. both statement is false d. first statement is true and second statement is false 2. These are catalyst that can be used in the monitoring and diagnosis of disease and their remarkable properties make them sensitive indicators of pathologic changes. a. enzymes b. electrolytes c. substrate d. none of these 3. ALT is stavle in serum at refrigirator or temp for up to 3 weeks, indefinitely if frozen AST has the same stability but markedly decreases with freezing a. both statement are true b. both statement are false c. first statement is true second is false d. second statement is true first statement is falseSucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify…
- A biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme BWhich of the following is TRUE concerning the induced fit model of enzyme catalysis? * (One correct answer only) A. The active site can be influenced by molecules binding elsewhere on an enzyme B. The initial binding of enzyme and substrate is the most tightly bound conformation C. The induced fit must occur prior to the initial binding of enzyme and substrate in order for the reaction to proceed D. The binding of enzyme and substrate is weakest in the transition stateSelect the correct option a.A holoenzyme is a catalytically inactive enzyme in the absence of its cofactor b.An enzyme cofactor is the amino acid side group in the enzyme active site c.Each of the option listed here is true d.An apoenzymes is catalytically active RNA molecule e.A co-substrate is a detachable enzyme cofactor required with another substrate for an enzyme reaction
- Although we have introduced catalytic strategies separately, an enzyme typically employs more than one during a reaction. The catalytic strategies employed by serine protease include: Select one or more: O a. reduction of ASt b. transition state stabilization Oc. metal-assisted catalysis O d. acid/base catalysis O e. covalent catalysisWhich of the following statements about the reaction shown is not necessarily true? LO'Na 15. NaOH H,C. A. This is a hydrolysis reaction. B. The unknown reactant in this reaction is an ester. C. The unknown reactant in this reaction is a carboxylic acid. D. This is an acid-base neutralization reaction. E. None of these statements is necessarily true about the reaction shown, but ALL of them are possibly true.Penícillin is an esxample of what type of enzyme inhíbitor? A. Competitive B. Noncompetitive C. Uncompetitive D. Irreveralble What type of Inhíbition ia observed from the ahift of the Lineweaver-Burke plot ahown in the graph below where the solid line represents the uninhibited enzymatic reaction while the broken line represents the inhibited enzymatic reaction? A. Irreveraible inhibition B. Noncompetitive inhibition C. Competitive inhíbition D. Uncompetitive inhibition Potaszium cyanide ia a polzon which combines with cytochrome A3 to prevent binding of oxygen to the enzyme without altering the Km of the reaction with reapect to reduced cytochrome c. Which type of inhíbition does this represent? 9. A. Irreveraible inhibition B. Noncompetitive inhibition C. Competitive inhibition D. Uncompetitive inhibition Which of the following enzyme clesses catalyze reactions in which two molecules become diasociated from each other? 10. A. Kinase В. Нydrolaae C. Isomerase D. Ligase 1. Which of the…