BCHM 307 Quiz 3 All Questions100% Solved
with Verified Solutions
An enzyme that forms a covalent bond with its substrate during the course of a reaction
is considered to undergo _____. - Answer covalent catalysis
Which protein in the blood is responsible for converting fibrinogen to fibrin? - Answer
thrombin
Different enzymes that catalyze the same reaction are known as _____. - Answer
isoenzymes
In an enzyme mechanism that generates a negative charge in the transition state, which
of the following would be most effective to have in the active site of the enzyme? -
Answer transition metal cation
The ability for an enzyme to change its shape upon substrate binding represents the
concept of _____. - Answer induced fit
Which of the following is true regarding heparin? - Answer -it is used clinically as an
anticoagulant
-it simultaneously binds to antithrombin and the target of antithrombin
-it is a sulfated polysaccharide
-it is an allosteric activator of antithrombin
If an enzyme-catalyzed reaction has a velocity of 2 mM/min and a Vmax of 10 mM/min
when the substrate concentration is 0.5 mM, what is the Km? - Answer 2 mM
, How are the kinetics of an enzyme-catalyzed reaction affected by a purely
noncompetitive inhibitor? - Answer Vmax decreased, KM unchanged
If a Lineweaver-Burk plot gave a line with an equation of y = 0.490 x + 0.059, what is the
velocity at a substrate concentration of 5 mM? The original units for substrate were in
mM and velocity in mM/s. - Answer 6.37 mM/s
Which of the following properly expresses the Michaelis-Menten equation? - Answer vo
= Vmax [S] / (Km + [S])
How is an enzyme-catalyzed reaction affected by the addition of more enzyme? -
Answer velocity will increase
Which of the following is true regarding transition state analogs? - Answer -they are
competitive inhibitors
-they bind to an active site with much higher affinity than most inhibitors
-they are much more stable than the transition state
-their affinity for an enzyme is often much greater that the substrate
A Lineweaver-Burk plot is a _____. - Answer double reciprocal plot
If a Lineweaver-Burk plot was made for an enzyme-catalyzed reaction, both with and
without a competitive inhibitor present, what difference would be seen? - Answer the
slope would be less for the inhibited reaction
A plot of velocity versus substrate concentration for a simple enzyme-catalyzed reaction
produces a _____. This indicates that at some point, the enzyme is _____. - Answer
hyperbolic curve; saturated with substrate
with Verified Solutions
An enzyme that forms a covalent bond with its substrate during the course of a reaction
is considered to undergo _____. - Answer covalent catalysis
Which protein in the blood is responsible for converting fibrinogen to fibrin? - Answer
thrombin
Different enzymes that catalyze the same reaction are known as _____. - Answer
isoenzymes
In an enzyme mechanism that generates a negative charge in the transition state, which
of the following would be most effective to have in the active site of the enzyme? -
Answer transition metal cation
The ability for an enzyme to change its shape upon substrate binding represents the
concept of _____. - Answer induced fit
Which of the following is true regarding heparin? - Answer -it is used clinically as an
anticoagulant
-it simultaneously binds to antithrombin and the target of antithrombin
-it is a sulfated polysaccharide
-it is an allosteric activator of antithrombin
If an enzyme-catalyzed reaction has a velocity of 2 mM/min and a Vmax of 10 mM/min
when the substrate concentration is 0.5 mM, what is the Km? - Answer 2 mM
, How are the kinetics of an enzyme-catalyzed reaction affected by a purely
noncompetitive inhibitor? - Answer Vmax decreased, KM unchanged
If a Lineweaver-Burk plot gave a line with an equation of y = 0.490 x + 0.059, what is the
velocity at a substrate concentration of 5 mM? The original units for substrate were in
mM and velocity in mM/s. - Answer 6.37 mM/s
Which of the following properly expresses the Michaelis-Menten equation? - Answer vo
= Vmax [S] / (Km + [S])
How is an enzyme-catalyzed reaction affected by the addition of more enzyme? -
Answer velocity will increase
Which of the following is true regarding transition state analogs? - Answer -they are
competitive inhibitors
-they bind to an active site with much higher affinity than most inhibitors
-they are much more stable than the transition state
-their affinity for an enzyme is often much greater that the substrate
A Lineweaver-Burk plot is a _____. - Answer double reciprocal plot
If a Lineweaver-Burk plot was made for an enzyme-catalyzed reaction, both with and
without a competitive inhibitor present, what difference would be seen? - Answer the
slope would be less for the inhibited reaction
A plot of velocity versus substrate concentration for a simple enzyme-catalyzed reaction
produces a _____. This indicates that at some point, the enzyme is _____. - Answer
hyperbolic curve; saturated with substrate
