©FYNDLAY EXAM SOLUTIONS 2024/2025
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BioC 3021 Exam 2 Questions And Answers
(Guaranteed A+)
Michaelis- Menten Equation - answer✔The velocity of an enzyme reaction (V) is equal to the
maximum reaction velocity (Vmax) times the substrate concentration (S) divided by substrate
concentration plus the Michaelis constant ( Km)
increases - answer✔Rate of product formation ____________ as the initial substrate
concentration is raised.
Velocity - answer✔How rapidly product is being formed by the reaction
Vmax - answer✔Fastest reaction rate possible
S - answer✔Substrate concentration
Km - answer✔Michaelis constant ( dimensions of concentration)
Linear Km reduces to V= K x S (equation for a straight line) - answer✔At low S values the plot is
_______
Curved
Need to use the entire Michaelis- Menten equation
+ 1/2 Vmax - answer✔At intermediate S values the plot is _____________
v= Vmax - answer✔At high S values the plot is ________
Active sites available - answer✔The rate of the reaction is limited by the number of
_________________.
Efficient - answer✔Enzymes having a LOW Km are _______ at low substrate concentrations
Inefficient - answer✔Enzymes having a HIGH Km are ________ at low substrate concentrations
1|Page
, ©FYNDLAY EXAM SOLUTIONS 2024/2025
ALL RIGHTS RESERVED.
Turnover number - answer✔The number of molecules of substate that can be converted per
second per molecule of enzyme of a specific enzyme
Line Weaver Burk Plot - answer✔Alternate plot used for plotting kinetic data can be derived by
inverting the Michaelis- Menten equation you plot 1/v + 1/s, now you get a straight line
1/ Vmax - answer✔1/ V intercept =
-1/ Km - answer✔1/S intercept =
Km/ Vmax - answer✔Slope of line =
Inhibitors - answer✔__________ interfere with enzymatic activity.
Reversible - answer✔
Irreversible - answer✔Covalently modify an enzyme and inhibition cannot be revered
Competitive - answer✔Bind to the active site of the enzyme and compete with the substrate
At high substrate levels the effect of the inhibitor can be overcome, at high inhibitory
concentrations it is very unlikely the substrate will bind
The ratio of [inhibitor] to [substrate] determines the degree of activity
Non- Competitive - answer✔Bind somewhere else on the enzyme (not the active site) and
inhibit by causing some change transmitted through the enzyme to the active site
Raising the substrate concentration does not effect the degree of activity
slow - answer✔Competitive inhibitors have _______ reaction rates
Competitive inhibitor can not bind - answer✔At high [S] there is so much S that _______ ____
The Vmax stays the same and the Km increases - answer✔If a competitive inhibitor is added to
an enzyme reaction then:
less negative; increases - answer✔The -1/km gets _______ indicating that the Km _____ in the
presence of an competitive inhibitor.
Non-competitive inhibitors - answer✔At high substrate levels the inhibited reactions never
reach the same Vmax of the non inhibited reactions
2|Page
ALL RIGHTS RESERVED.
BioC 3021 Exam 2 Questions And Answers
(Guaranteed A+)
Michaelis- Menten Equation - answer✔The velocity of an enzyme reaction (V) is equal to the
maximum reaction velocity (Vmax) times the substrate concentration (S) divided by substrate
concentration plus the Michaelis constant ( Km)
increases - answer✔Rate of product formation ____________ as the initial substrate
concentration is raised.
Velocity - answer✔How rapidly product is being formed by the reaction
Vmax - answer✔Fastest reaction rate possible
S - answer✔Substrate concentration
Km - answer✔Michaelis constant ( dimensions of concentration)
Linear Km reduces to V= K x S (equation for a straight line) - answer✔At low S values the plot is
_______
Curved
Need to use the entire Michaelis- Menten equation
+ 1/2 Vmax - answer✔At intermediate S values the plot is _____________
v= Vmax - answer✔At high S values the plot is ________
Active sites available - answer✔The rate of the reaction is limited by the number of
_________________.
Efficient - answer✔Enzymes having a LOW Km are _______ at low substrate concentrations
Inefficient - answer✔Enzymes having a HIGH Km are ________ at low substrate concentrations
1|Page
, ©FYNDLAY EXAM SOLUTIONS 2024/2025
ALL RIGHTS RESERVED.
Turnover number - answer✔The number of molecules of substate that can be converted per
second per molecule of enzyme of a specific enzyme
Line Weaver Burk Plot - answer✔Alternate plot used for plotting kinetic data can be derived by
inverting the Michaelis- Menten equation you plot 1/v + 1/s, now you get a straight line
1/ Vmax - answer✔1/ V intercept =
-1/ Km - answer✔1/S intercept =
Km/ Vmax - answer✔Slope of line =
Inhibitors - answer✔__________ interfere with enzymatic activity.
Reversible - answer✔
Irreversible - answer✔Covalently modify an enzyme and inhibition cannot be revered
Competitive - answer✔Bind to the active site of the enzyme and compete with the substrate
At high substrate levels the effect of the inhibitor can be overcome, at high inhibitory
concentrations it is very unlikely the substrate will bind
The ratio of [inhibitor] to [substrate] determines the degree of activity
Non- Competitive - answer✔Bind somewhere else on the enzyme (not the active site) and
inhibit by causing some change transmitted through the enzyme to the active site
Raising the substrate concentration does not effect the degree of activity
slow - answer✔Competitive inhibitors have _______ reaction rates
Competitive inhibitor can not bind - answer✔At high [S] there is so much S that _______ ____
The Vmax stays the same and the Km increases - answer✔If a competitive inhibitor is added to
an enzyme reaction then:
less negative; increases - answer✔The -1/km gets _______ indicating that the Km _____ in the
presence of an competitive inhibitor.
Non-competitive inhibitors - answer✔At high substrate levels the inhibited reactions never
reach the same Vmax of the non inhibited reactions
2|Page
