@⇒ Short cut notes / rapid fire notes / best theory of Enzymes and kinetics ⇒ Biochemical Engineering ⇒ Medical Science Engineering Multiple Choice Questions / Objective type questions, MCQ's, with question and answers, download free PDF

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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.

Q1 ⇒ Given an enzyme with a K_m = 10m M and V_max = 100 m mol/min. If [S] = 100 m M, which of the following will be true?
A 10 fold increase in V_max would increase velocity 10 fold y
[other wrong options] [Discuss in forum] 1 -1

Q2 ⇒ The enzyme inhibition can occur by
Both (a) and (b)
[other wrong options] [Discuss in forum] 1 -2

Q3 ⇒ A noncompetitive inhibitor of an enzyme-catalyzed reaction
increases K_M and reduces V_max
[other wrong options] [Discuss in forum] 1 -1

Q4 ⇒ In the steady state the material balance equation for any component of a system is
rate of addition - rate of removal + rate of formation = 0
[other wrong options] [Discuss in forum] 2 -1

Q5 ⇒ Michaelis Menten equation can also be written as
All of these
[other wrong options] [Discuss in forum] 1 -1

Q6 ⇒ Enzymes are basically
proteins
[other wrong options] [Discuss in forum] 3 -1

Q7 ⇒ The conformational change in an enzyme after the substrate is bound that allows the chemical reaction to proceed, can be explained by
induced fit
[other wrong options] [Discuss in forum] 2 -3

Q8 ⇒ In a Lineweaver-Burk Plot, competitive inhibitor shows which of the following effect?
It changes the x-intercept
[other wrong options] [Discuss in forum] 1 -1

Q9 ⇒ An allosteric inhibitor of an enzyme usually
participates in feedback regulation
[other wrong options] [Discuss in forum] 2 -4

Q10 ⇒ For an enzyme that displays Michaelis-Menten kinetics, the reaction velocity (as a fraction of V_max) observed at [S] = 2 K_M will be
0.66
[other wrong options] [Discuss in forum] 2 -2

Q11 ⇒ Which of the following step is assumed to be the slowest step in the Michaelis Menten equation?
The product releasing step
[other wrong options] [Discuss in forum] 2 -1

Q12 ⇒ Which of the following refers to pseudo steady state ?
d(C_ES)/dt = 0
[other wrong options] [Discuss in forum] 1 -1

Q13 ⇒ The types of inhibition pattern based on Michaelis Menten equation are
all of the above
[other wrong options] [Discuss in forum] 4 -3

Q14 ⇒ The Woolf-Augusteinsson-Hofstee plot of ν versus ν/[S] and the Eadie-Scatchard plot of ν/[S] versus ν do not involve reciprocals of ν therefore are considered to be more reliable when the error in v is
significant
[other wrong options] [Discuss in forum] 1 -1

Q15 ⇒ Which of these proteases is not a cysteine active site protease?
Cathepsin D
[other wrong options] [Discuss in forum] 1 -1

Q16 ⇒ An enzyme and a reactant molecule maintain relationship as
a temporary association
[other wrong options] [Discuss in forum] 4 -4

Q17 ⇒ Which of the following common drugs is not a specific enzyme inhibitor?
Iodine
[other wrong options] [Discuss in forum] 1 -2

Q18 ⇒ Which graphical method is used to determine an enzyme degree of cooperativity?
Hill plot
[other wrong options] [Discuss in forum] 1 -1

Q19 ⇒ The rate-determining step of Michaelis Menten kinetics is
the complex dissociation step to produce product
[other wrong options] [Discuss in forum] 8 -6

Q20 ⇒ Which of these enzymes contains a Zinc (Zn) ion?
Carboxypeptidase A
[other wrong options] [Discuss in forum] 1 -1

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