Enzyme Kinetics - MCQ Test Biotechnology Engineering (BT) Notes | EduRev

Biotechnology Engineering (BT) : Enzyme Kinetics - MCQ Test Biotechnology Engineering (BT) Notes | EduRev

 Page 1


BCH400/600       Name___________________ 
Exam 2 
March 4, 2002 
For questions 1 through 30mark the correct answer on the scantron answer sheet and this 
exam 
Multiple-choice questions (2 points per question) 
1) Allosteric enzymes _____________. 
(a) usually have quaternary structure. 
(b) do not behave according to Michaelis-Menton kinetics. 
(c) bind allosteric modulators at sites not associated with substrate binding. 
(d) often have separate catalytic and regulator domains. 
(e) all of the above. 
 
2) A catalyst can promote product formation during a chemical reaction by _____.      
(a) lowering the activation energy barrier. 
(b) stabilizing the transition state. 
(c) positioning reactants in the correct orientation. 
(d) bringing reactants together. 
(e) all of the above 
 
3) The rate of sucrose hydrolysis (sucrose + H
2
0 <-> fructose + glucose) is dependent 
on the concentration of sucrose and independent of the concentration of H
2
0. 
Therefore this reaction is a ______. 
(a) 1st order reaction in relation to water. 
(b) zero order reaction in relation to sucrose. 
(c) 1
st
 order reaction in relation to sucrose 
(d) 2
nd
 order reaction in relation to sucrose and water. 
(e) none of the above. 
 
4) The initial velocity assumption for Michaelis-Menton kinetic assumes that 
______. 
(a) The reaction is always running at V
max
. 
(b) the rate of E + P -> ES is negligible. 
(c) a large amount of product has formed. 
(d) k
-2 
is large. 
(e) none of the above. 
 
5) K
m
 is _______. 
(a) the substrate concentration at ½ V
max.
 
(b) = (k
-1
 + k
cat
)/k
1
 
(c) related to an enzymes affinity for a specific substrate. 
(d) the Michaelis Constant. 
(e) All of the above 
(f)  
6) Heterolytic carbon-carbon bond cleavage can result in the formation of_____. 
(a) a carbocation. 
(b) radical species. 
(c) a carbanion. 
(d) a and b 
(e) a and c 
 
Page 2


BCH400/600       Name___________________ 
Exam 2 
March 4, 2002 
For questions 1 through 30mark the correct answer on the scantron answer sheet and this 
exam 
Multiple-choice questions (2 points per question) 
1) Allosteric enzymes _____________. 
(a) usually have quaternary structure. 
(b) do not behave according to Michaelis-Menton kinetics. 
(c) bind allosteric modulators at sites not associated with substrate binding. 
(d) often have separate catalytic and regulator domains. 
(e) all of the above. 
 
2) A catalyst can promote product formation during a chemical reaction by _____.      
(a) lowering the activation energy barrier. 
(b) stabilizing the transition state. 
(c) positioning reactants in the correct orientation. 
(d) bringing reactants together. 
(e) all of the above 
 
3) The rate of sucrose hydrolysis (sucrose + H
2
0 <-> fructose + glucose) is dependent 
on the concentration of sucrose and independent of the concentration of H
2
0. 
Therefore this reaction is a ______. 
(a) 1st order reaction in relation to water. 
(b) zero order reaction in relation to sucrose. 
(c) 1
st
 order reaction in relation to sucrose 
(d) 2
nd
 order reaction in relation to sucrose and water. 
(e) none of the above. 
 
4) The initial velocity assumption for Michaelis-Menton kinetic assumes that 
______. 
(a) The reaction is always running at V
max
. 
(b) the rate of E + P -> ES is negligible. 
(c) a large amount of product has formed. 
(d) k
-2 
is large. 
(e) none of the above. 
 
5) K
m
 is _______. 
(a) the substrate concentration at ½ V
max.
 
(b) = (k
-1
 + k
cat
)/k
1
 
(c) related to an enzymes affinity for a specific substrate. 
(d) the Michaelis Constant. 
(e) All of the above 
(f)  
6) Heterolytic carbon-carbon bond cleavage can result in the formation of_____. 
(a) a carbocation. 
(b) radical species. 
(c) a carbanion. 
(d) a and b 
(e) a and c 
 
7) A reversible inhibitor that only binds to the ES complex is referred to as a _____. 
(a) competitive inhibitor. 
(b) non-competitive inhibitor. 
(c) uncompetitive inhibitor. 
(d) suicide inhibitor. 
(e) irreversible inhibitor. 
 
8) Chymotrypsin is an example of a  
(a) transferase. 
(b) hydrolase. 
(c) oxidoreductase. 
(d) lyase. 
(e) isomerase. 
 
9) NADH would function as a cofactor for a 
(a) transferase. 
(b) hydrolase. 
(c) oxidoreductase. 
(d) ligase. 
(e) isomerase. 
 
10)  Lipoamide is ____________. 
(a) a co-substrate. 
(b) a metabolite coenzyme. 
(c) a vitamin  
(d) a prosthetic group. 
(e) none of the above. 
 
11) ______________ is a cosubstrate. 
(a) Tetrahydrofolate. 
(b) NADH 
(c) Biotin 
(d) Thiamin pyrophosphate. 
(e) Pyridoxol phosphate 
 
12) _________ is the coenzyme involved in decarboxylation reactions. 
(a) Tetrahydrofolate. 
(b) NADH 
(c) Biotin 
(d) Thiamin pyrophosphate. 
(e) Pyridoxol phosphate. 
 
13)  The apparent K
m
 of an enzyme changes when the enzyme is treated with a_____. 
(a) competitive inhibitor. 
(b) uncompetitive inhibitor. 
(c) noncompetitive inhibitor 
(d)  a and b. 
(e) b and c. 
 
 
 
 
Page 3


BCH400/600       Name___________________ 
Exam 2 
March 4, 2002 
For questions 1 through 30mark the correct answer on the scantron answer sheet and this 
exam 
Multiple-choice questions (2 points per question) 
1) Allosteric enzymes _____________. 
(a) usually have quaternary structure. 
(b) do not behave according to Michaelis-Menton kinetics. 
(c) bind allosteric modulators at sites not associated with substrate binding. 
(d) often have separate catalytic and regulator domains. 
(e) all of the above. 
 
2) A catalyst can promote product formation during a chemical reaction by _____.      
(a) lowering the activation energy barrier. 
(b) stabilizing the transition state. 
(c) positioning reactants in the correct orientation. 
(d) bringing reactants together. 
(e) all of the above 
 
3) The rate of sucrose hydrolysis (sucrose + H
2
0 <-> fructose + glucose) is dependent 
on the concentration of sucrose and independent of the concentration of H
2
0. 
Therefore this reaction is a ______. 
(a) 1st order reaction in relation to water. 
(b) zero order reaction in relation to sucrose. 
(c) 1
st
 order reaction in relation to sucrose 
(d) 2
nd
 order reaction in relation to sucrose and water. 
(e) none of the above. 
 
4) The initial velocity assumption for Michaelis-Menton kinetic assumes that 
______. 
(a) The reaction is always running at V
max
. 
(b) the rate of E + P -> ES is negligible. 
(c) a large amount of product has formed. 
(d) k
-2 
is large. 
(e) none of the above. 
 
5) K
m
 is _______. 
(a) the substrate concentration at ½ V
max.
 
(b) = (k
-1
 + k
cat
)/k
1
 
(c) related to an enzymes affinity for a specific substrate. 
(d) the Michaelis Constant. 
(e) All of the above 
(f)  
6) Heterolytic carbon-carbon bond cleavage can result in the formation of_____. 
(a) a carbocation. 
(b) radical species. 
(c) a carbanion. 
(d) a and b 
(e) a and c 
 
7) A reversible inhibitor that only binds to the ES complex is referred to as a _____. 
(a) competitive inhibitor. 
(b) non-competitive inhibitor. 
(c) uncompetitive inhibitor. 
(d) suicide inhibitor. 
(e) irreversible inhibitor. 
 
8) Chymotrypsin is an example of a  
(a) transferase. 
(b) hydrolase. 
(c) oxidoreductase. 
(d) lyase. 
(e) isomerase. 
 
9) NADH would function as a cofactor for a 
(a) transferase. 
(b) hydrolase. 
(c) oxidoreductase. 
(d) ligase. 
(e) isomerase. 
 
10)  Lipoamide is ____________. 
(a) a co-substrate. 
(b) a metabolite coenzyme. 
(c) a vitamin  
(d) a prosthetic group. 
(e) none of the above. 
 
11) ______________ is a cosubstrate. 
(a) Tetrahydrofolate. 
(b) NADH 
(c) Biotin 
(d) Thiamin pyrophosphate. 
(e) Pyridoxol phosphate 
 
12) _________ is the coenzyme involved in decarboxylation reactions. 
(a) Tetrahydrofolate. 
(b) NADH 
(c) Biotin 
(d) Thiamin pyrophosphate. 
(e) Pyridoxol phosphate. 
 
13)  The apparent K
m
 of an enzyme changes when the enzyme is treated with a_____. 
(a) competitive inhibitor. 
(b) uncompetitive inhibitor. 
(c) noncompetitive inhibitor 
(d)  a and b. 
(e) b and c. 
 
 
 
 
14) When glucose cyclizes, _________. 
(a) it becomes a hemiketal. 
(b) it looses one chiral center. 
(c) the hydroxyl group associated with the anomeric carbon is always in the 
beta conformation 
(d) it usually forms a pyranose ring. 
(e) none of the above 
 
15) The amino acid ________ can function in proton transfer when present in the 
enzyme active site. 
(a) glutamate 
(b) aspartate 
(c) histidine 
(d) lysine 
(e) all of the above 
 
16) Which of the following coenzymes participates in enzymatic mechanisms by 
producing a free radical intermediate? 
(a) NADPH 
(b) Ubiquinone 
(c) Methylcobalamin 
(d) Biotin 
(e) Lipoamide 
 
17) Monosaccharides that differ at only one chiral center are referred to as _____. 
(a) isosaccharides. 
(b) enantiomers. 
(c) epimers. 
(d) anomers. 
(e) none of the above. 
 
18) N-linked oligosaccharides ____________. 
(a) are involved in targeting proteins to different subcellular organelles 
(b) are linked to amino acids with hydroxyl groups. 
(c) are not required for correct protein folding of N-linked glycosylated 
proteins. 
(d) have no affect on the physical properties of a protein. 
(e) All of the above 
 
True or false (2 points per question 
 
19) Under physiological conditions, the substrate concentration is < to the Km. 
(a) true 
(b) false 
 
20) The enzyme active site binds the substrate with higher affinity than the transition 
state. 
(a) true 
(b) false 
 
 
 
Page 4


BCH400/600       Name___________________ 
Exam 2 
March 4, 2002 
For questions 1 through 30mark the correct answer on the scantron answer sheet and this 
exam 
Multiple-choice questions (2 points per question) 
1) Allosteric enzymes _____________. 
(a) usually have quaternary structure. 
(b) do not behave according to Michaelis-Menton kinetics. 
(c) bind allosteric modulators at sites not associated with substrate binding. 
(d) often have separate catalytic and regulator domains. 
(e) all of the above. 
 
2) A catalyst can promote product formation during a chemical reaction by _____.      
(a) lowering the activation energy barrier. 
(b) stabilizing the transition state. 
(c) positioning reactants in the correct orientation. 
(d) bringing reactants together. 
(e) all of the above 
 
3) The rate of sucrose hydrolysis (sucrose + H
2
0 <-> fructose + glucose) is dependent 
on the concentration of sucrose and independent of the concentration of H
2
0. 
Therefore this reaction is a ______. 
(a) 1st order reaction in relation to water. 
(b) zero order reaction in relation to sucrose. 
(c) 1
st
 order reaction in relation to sucrose 
(d) 2
nd
 order reaction in relation to sucrose and water. 
(e) none of the above. 
 
4) The initial velocity assumption for Michaelis-Menton kinetic assumes that 
______. 
(a) The reaction is always running at V
max
. 
(b) the rate of E + P -> ES is negligible. 
(c) a large amount of product has formed. 
(d) k
-2 
is large. 
(e) none of the above. 
 
5) K
m
 is _______. 
(a) the substrate concentration at ½ V
max.
 
(b) = (k
-1
 + k
cat
)/k
1
 
(c) related to an enzymes affinity for a specific substrate. 
(d) the Michaelis Constant. 
(e) All of the above 
(f)  
6) Heterolytic carbon-carbon bond cleavage can result in the formation of_____. 
(a) a carbocation. 
(b) radical species. 
(c) a carbanion. 
(d) a and b 
(e) a and c 
 
7) A reversible inhibitor that only binds to the ES complex is referred to as a _____. 
(a) competitive inhibitor. 
(b) non-competitive inhibitor. 
(c) uncompetitive inhibitor. 
(d) suicide inhibitor. 
(e) irreversible inhibitor. 
 
8) Chymotrypsin is an example of a  
(a) transferase. 
(b) hydrolase. 
(c) oxidoreductase. 
(d) lyase. 
(e) isomerase. 
 
9) NADH would function as a cofactor for a 
(a) transferase. 
(b) hydrolase. 
(c) oxidoreductase. 
(d) ligase. 
(e) isomerase. 
 
10)  Lipoamide is ____________. 
(a) a co-substrate. 
(b) a metabolite coenzyme. 
(c) a vitamin  
(d) a prosthetic group. 
(e) none of the above. 
 
11) ______________ is a cosubstrate. 
(a) Tetrahydrofolate. 
(b) NADH 
(c) Biotin 
(d) Thiamin pyrophosphate. 
(e) Pyridoxol phosphate 
 
12) _________ is the coenzyme involved in decarboxylation reactions. 
(a) Tetrahydrofolate. 
(b) NADH 
(c) Biotin 
(d) Thiamin pyrophosphate. 
(e) Pyridoxol phosphate. 
 
13)  The apparent K
m
 of an enzyme changes when the enzyme is treated with a_____. 
(a) competitive inhibitor. 
(b) uncompetitive inhibitor. 
(c) noncompetitive inhibitor 
(d)  a and b. 
(e) b and c. 
 
 
 
 
14) When glucose cyclizes, _________. 
(a) it becomes a hemiketal. 
(b) it looses one chiral center. 
(c) the hydroxyl group associated with the anomeric carbon is always in the 
beta conformation 
(d) it usually forms a pyranose ring. 
(e) none of the above 
 
15) The amino acid ________ can function in proton transfer when present in the 
enzyme active site. 
(a) glutamate 
(b) aspartate 
(c) histidine 
(d) lysine 
(e) all of the above 
 
16) Which of the following coenzymes participates in enzymatic mechanisms by 
producing a free radical intermediate? 
(a) NADPH 
(b) Ubiquinone 
(c) Methylcobalamin 
(d) Biotin 
(e) Lipoamide 
 
17) Monosaccharides that differ at only one chiral center are referred to as _____. 
(a) isosaccharides. 
(b) enantiomers. 
(c) epimers. 
(d) anomers. 
(e) none of the above. 
 
18) N-linked oligosaccharides ____________. 
(a) are involved in targeting proteins to different subcellular organelles 
(b) are linked to amino acids with hydroxyl groups. 
(c) are not required for correct protein folding of N-linked glycosylated 
proteins. 
(d) have no affect on the physical properties of a protein. 
(e) All of the above 
 
True or false (2 points per question 
 
19) Under physiological conditions, the substrate concentration is < to the Km. 
(a) true 
(b) false 
 
20) The enzyme active site binds the substrate with higher affinity than the transition 
state. 
(a) true 
(b) false 
 
 
 
21)  Starch and glycogen are polysaccharides formed from alpha-1,4 and alpha-1,6 
linked glucose molecules. 
(a) true 
(b) false 
 
22) Starch forms a helical structure that can bind iodine to form a blue colored 
compound. 
(a) true 
(b) false 
  
23) Biotin forms a Schiff base in reactions with amine groups. 
(a) true 
(b) false 
 
24) All monosaccharides are reducing sugars. 
(a) true 
(b) false 
 
25) Lineweaver-Burk plots describe the equation of a rectangular hyperbolic curve. 
(a) true 
(b) false 
 
 
26) The coenzyme FADH always transfers two electrons in the form of a hydride ion 
during oxidation-reduction reactions. 
(a) true 
(b) false 
 
27) The coenzyme FADH can form a semiquinone intermediate and therefore can 
transfer electrons either one or two at a time.  
(a) true 
(b) false 
 
28) An uncompetitive inhibitor decreases both the K
m
 and the V
max
 of a biochemical 
reaction. 
(a) true 
(b) false 
 
29) Pyranose monosaccharides are most stable when in the boat conformation 
(a) true 
(b) false 
 
30)  Metal activated enzymes bind to metal ions tightly as prosthetic groups within 
the active site. 
(a) true 
(b) false 
 
Page 5


BCH400/600       Name___________________ 
Exam 2 
March 4, 2002 
For questions 1 through 30mark the correct answer on the scantron answer sheet and this 
exam 
Multiple-choice questions (2 points per question) 
1) Allosteric enzymes _____________. 
(a) usually have quaternary structure. 
(b) do not behave according to Michaelis-Menton kinetics. 
(c) bind allosteric modulators at sites not associated with substrate binding. 
(d) often have separate catalytic and regulator domains. 
(e) all of the above. 
 
2) A catalyst can promote product formation during a chemical reaction by _____.      
(a) lowering the activation energy barrier. 
(b) stabilizing the transition state. 
(c) positioning reactants in the correct orientation. 
(d) bringing reactants together. 
(e) all of the above 
 
3) The rate of sucrose hydrolysis (sucrose + H
2
0 <-> fructose + glucose) is dependent 
on the concentration of sucrose and independent of the concentration of H
2
0. 
Therefore this reaction is a ______. 
(a) 1st order reaction in relation to water. 
(b) zero order reaction in relation to sucrose. 
(c) 1
st
 order reaction in relation to sucrose 
(d) 2
nd
 order reaction in relation to sucrose and water. 
(e) none of the above. 
 
4) The initial velocity assumption for Michaelis-Menton kinetic assumes that 
______. 
(a) The reaction is always running at V
max
. 
(b) the rate of E + P -> ES is negligible. 
(c) a large amount of product has formed. 
(d) k
-2 
is large. 
(e) none of the above. 
 
5) K
m
 is _______. 
(a) the substrate concentration at ½ V
max.
 
(b) = (k
-1
 + k
cat
)/k
1
 
(c) related to an enzymes affinity for a specific substrate. 
(d) the Michaelis Constant. 
(e) All of the above 
(f)  
6) Heterolytic carbon-carbon bond cleavage can result in the formation of_____. 
(a) a carbocation. 
(b) radical species. 
(c) a carbanion. 
(d) a and b 
(e) a and c 
 
7) A reversible inhibitor that only binds to the ES complex is referred to as a _____. 
(a) competitive inhibitor. 
(b) non-competitive inhibitor. 
(c) uncompetitive inhibitor. 
(d) suicide inhibitor. 
(e) irreversible inhibitor. 
 
8) Chymotrypsin is an example of a  
(a) transferase. 
(b) hydrolase. 
(c) oxidoreductase. 
(d) lyase. 
(e) isomerase. 
 
9) NADH would function as a cofactor for a 
(a) transferase. 
(b) hydrolase. 
(c) oxidoreductase. 
(d) ligase. 
(e) isomerase. 
 
10)  Lipoamide is ____________. 
(a) a co-substrate. 
(b) a metabolite coenzyme. 
(c) a vitamin  
(d) a prosthetic group. 
(e) none of the above. 
 
11) ______________ is a cosubstrate. 
(a) Tetrahydrofolate. 
(b) NADH 
(c) Biotin 
(d) Thiamin pyrophosphate. 
(e) Pyridoxol phosphate 
 
12) _________ is the coenzyme involved in decarboxylation reactions. 
(a) Tetrahydrofolate. 
(b) NADH 
(c) Biotin 
(d) Thiamin pyrophosphate. 
(e) Pyridoxol phosphate. 
 
13)  The apparent K
m
 of an enzyme changes when the enzyme is treated with a_____. 
(a) competitive inhibitor. 
(b) uncompetitive inhibitor. 
(c) noncompetitive inhibitor 
(d)  a and b. 
(e) b and c. 
 
 
 
 
14) When glucose cyclizes, _________. 
(a) it becomes a hemiketal. 
(b) it looses one chiral center. 
(c) the hydroxyl group associated with the anomeric carbon is always in the 
beta conformation 
(d) it usually forms a pyranose ring. 
(e) none of the above 
 
15) The amino acid ________ can function in proton transfer when present in the 
enzyme active site. 
(a) glutamate 
(b) aspartate 
(c) histidine 
(d) lysine 
(e) all of the above 
 
16) Which of the following coenzymes participates in enzymatic mechanisms by 
producing a free radical intermediate? 
(a) NADPH 
(b) Ubiquinone 
(c) Methylcobalamin 
(d) Biotin 
(e) Lipoamide 
 
17) Monosaccharides that differ at only one chiral center are referred to as _____. 
(a) isosaccharides. 
(b) enantiomers. 
(c) epimers. 
(d) anomers. 
(e) none of the above. 
 
18) N-linked oligosaccharides ____________. 
(a) are involved in targeting proteins to different subcellular organelles 
(b) are linked to amino acids with hydroxyl groups. 
(c) are not required for correct protein folding of N-linked glycosylated 
proteins. 
(d) have no affect on the physical properties of a protein. 
(e) All of the above 
 
True or false (2 points per question 
 
19) Under physiological conditions, the substrate concentration is < to the Km. 
(a) true 
(b) false 
 
20) The enzyme active site binds the substrate with higher affinity than the transition 
state. 
(a) true 
(b) false 
 
 
 
21)  Starch and glycogen are polysaccharides formed from alpha-1,4 and alpha-1,6 
linked glucose molecules. 
(a) true 
(b) false 
 
22) Starch forms a helical structure that can bind iodine to form a blue colored 
compound. 
(a) true 
(b) false 
  
23) Biotin forms a Schiff base in reactions with amine groups. 
(a) true 
(b) false 
 
24) All monosaccharides are reducing sugars. 
(a) true 
(b) false 
 
25) Lineweaver-Burk plots describe the equation of a rectangular hyperbolic curve. 
(a) true 
(b) false 
 
 
26) The coenzyme FADH always transfers two electrons in the form of a hydride ion 
during oxidation-reduction reactions. 
(a) true 
(b) false 
 
27) The coenzyme FADH can form a semiquinone intermediate and therefore can 
transfer electrons either one or two at a time.  
(a) true 
(b) false 
 
28) An uncompetitive inhibitor decreases both the K
m
 and the V
max
 of a biochemical 
reaction. 
(a) true 
(b) false 
 
29) Pyranose monosaccharides are most stable when in the boat conformation 
(a) true 
(b) false 
 
30)  Metal activated enzymes bind to metal ions tightly as prosthetic groups within 
the active site. 
(a) true 
(b) false 
 
 
31) (10 points) Draw the Fischer and Haworth projections for beta-D-galactose. 
Circle the anomeric carbon. Make sure to include all hydrogens and hydroxyl 
groups. Determine the number of possible stereoisomers for both the open chain 
and cyclized forms. 
 
 
 
 
 
 
 
 
 
 
 
Read More
Offer running on EduRev: Apply code STAYHOME200 to get INR 200 off on our premium plan EduRev Infinity!

Content Category

Related Searches

Viva Questions

,

video lectures

,

study material

,

MCQs

,

Enzyme Kinetics - MCQ Test Biotechnology Engineering (BT) Notes | EduRev

,

Free

,

mock tests for examination

,

practice quizzes

,

Previous Year Questions with Solutions

,

Important questions

,

ppt

,

Semester Notes

,

Enzyme Kinetics - MCQ Test Biotechnology Engineering (BT) Notes | EduRev

,

pdf

,

Exam

,

Enzyme Kinetics - MCQ Test Biotechnology Engineering (BT) Notes | EduRev

,

Objective type Questions

,

past year papers

,

Sample Paper

,

Summary

,

Extra Questions

,

shortcuts and tricks

;