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Home⇒ Medical Science⇒ Bochemical Engineering⇒ Enzymes and kinetics
1-Dont try to cram or spend more time here just read it fast and cover syllabus then practice MCQ's cheptor of same topic to check your progress. . |
2-Wrong options are also given but dont concentrate there, Right answer is in bold format. |
Q21 ⇒ The rate equation in non-competitive inhibition based on Michaelis Menten equation is given by rmaxS/(Km + S)(1+I/Ki) [other wrong options] [Discuss in forum] rmaxE/(Km (1+I/Ki)+S)) VmaxS/(Km + S)(1+I/Ki) rmaxS/Km |
Q22 ⇒ The reciprocal equation for non competitive inhibition can be arranged to the equation for the Dixon plot [other wrong options] [Discuss in forum] Woolf-Augusteinsson-Hofstee plot Eadie-Scatchard plot Hanes-Woolf plot |
Q23 ⇒ Classical noncompetitive inhibition is obtained only under rapid equilibrium conditions [other wrong options] [Discuss in forum] slow equilibrium conditions moderate equilibrium conditions non-equilibrium conditions |
Q24 ⇒ The active site of an enzyme differs from an antibody-antigen binding site in that the enzyme active site catalyzes a chemical reaction [other wrong options] [Discuss in forum] contains modified amino acids is complementary to a specific ligand contains amino acids without side chains |
Q25 ⇒ The plot commonly used for determining the value of Vmax is all of these [other wrong options] [Discuss in forum] Lineweaver Burk plot Langmuir plot Eadie Hofstee plot |
Q26 ⇒ The usual method(s) to solve rate equation of simple enzyme kinetics is/are all of these [other wrong options] [Discuss in forum] Michaelis Menten approach Briggs-Haldane approach Numerical solution approach |
Q27 ⇒ Lock and key theory is based on the compatibility of enzyme and substrate [other wrong options] [Discuss in forum] enzyme and product enzyme and enzyme substrate complex enzyme substrate complex and product |
Q28 ⇒ If a reaction occurs in the absence of inhibitor with rate ν0 and in the presence of inhibitor with rate νi, the degree of inhibition is defined as (ν0 - νi)/ν0 [other wrong options] [Discuss in forum] (ν0 + νi)/ν0 (ν0νi)/ν0 (ν0-νi)/νi |
Q29 ⇒ The slope of Lineweaver Burk plot for Michaelis Menten equation is Km/Vmax [other wrong options] [Discuss in forum] Vmax/Km 1/Km Km.Vmax |
Q30 ⇒ The equation for the rate of product formation for simple enzyme reaction is given by (Where rmax, maximum reaction rate, Cs substrate concentration, Cp product concentration ES, CES enzyme-substrate concentration) rp = rmax Cs/(Km+Cs) [other wrong options] [Discuss in forum] rp= rmax CES/(Km+ CES) rp = rmax Cs/(Km+CES) rp = rmax Cs/(Km+Cp) |
Q31 ⇒ Linear inhibition is sometimes called as complete inhibition [other wrong options] [Discuss in forum] incomplete inhibtion partial inhibition mixed inhibition |
Q32 ⇒ Which category of enzymes belongs to class two in the international classification? Transferases [other wrong options] [Discuss in forum] Hydrolases Ligases Isomerase |
Q33 ⇒ Non-competitive inhibitor of an enzyme catalyzed reaction both (a) and (b) [other wrong options] [Discuss in forum] decreases Vmax binds to Michaelis complex (ES) can actually increase reaction velocity in rare cases |
Q34 ⇒ A classical uncompetitive inhibitor is a compound that binds reversibly to the enzyme substrate complex yielding an inactive ESI complex [other wrong options] [Discuss in forum] irreversibly to the enzyme substrate complex yielding an inactive ESI complex reversibly to the enzyme substrate complex yielding an active ESI complex irreversibly to the enzyme substrate complex yielding an active ESI complex |
Q35 ⇒ An enzyme has a Km of 4.7 x 10-5M. If the Vmax of the preparation is 22m moles liter-1 min-1, what velocity would be observed in the presence of 2.0 x 10-4M substrate and 5.0 x 10-5M of a competitive inhibitor? 13.54μ moles liter-1min-1 [other wrong options] [Discuss in forum] 6.68μ moles liter-1min-1 7.57μ moles liter-1min-1 17.8μ moles liter-1min-1 |
Q36 ⇒ A classical noncompetitive inhibitor has no effect on substrate binding and vice versa [other wrong options] [Discuss in forum] no effect on substrate binding significant effect on substrate binding significant effect on substrate binding and vice versa |
Q37 ⇒ Which category of enzymes belongs to class 5 in the international classification? Isomerases [other wrong options] [Discuss in forum] Hydrolases Oxido-reductases Cyclase |
Q38 ⇒ In competitive inhibition a factor is obtained from the measurement of KM [other wrong options] [Discuss in forum] Vmax Y-intercept in Lineweaver-Burk Plot None of these |
Q39 ⇒ Which of the following statements is true for enzymatically catalyzed reaction? The activation energy of the reaction is lowered so that a larger proportion of the substrate qualifies to overcome it [other wrong options] [Discuss in forum] Additional substrate molecules are energized to overcome the activation energy of the reaction The activation energy of the reaction is increased, thus decreasing the likelihood that any substrate molecules will overcome it The activation energy of the reaction is lowered so that a fewer substrate molecules can overcome it |
Q40 ⇒ Quasi steady state is also known as Pseudo steady state [other wrong options] [Discuss in forum] Michaelis Menten approach Briggs-Haldane approach all of the above |
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