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25/11/2024 13:32PM
BioC 3021 Exam 2 Questions and Answers
Michaelis- Menten Equation - Answers✓✓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 - Answers✓✓Rate of product formation ____________ as the initial substrate
concentration is raised.
Velocity - Answers✓✓How rapidly product is being formed by the reaction
Vmax - Answers✓✓Fastest reaction rate possible
S - Answers✓✓Substrate concentration
Km - Answers✓✓Michaelis constant ( dimensions of concentration)
Linear Km reduces to V= K x S (equation for a straight line) - Answers✓✓At low S values the
plot is _______
Curved
Need to use the entire Michaelis- Menten equation
+ 1/2 Vmax - Answers✓✓At intermediate S values the plot is _____________
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25/11/2024 13:32PM
v= Vmax - Answers✓✓At high S values the plot is ________
Active sites available - Answers✓✓The rate of the reaction is limited by the number of
_________________.
Efficient - Answers✓✓Enzymes having a LOW Km are _______ at low substrate
concentrations
Inefficient - Answers✓✓Enzymes having a HIGH Km are ________ at low substrate
concentrations
Turnover number - Answers✓✓The number of molecules of substate that can be converted per
second per molecule of enzyme of a specific enzyme
Line Weaver Burk Plot - Answers✓✓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 - Answers✓✓1/ V intercept =
-1/ Km - Answers✓✓1/S intercept =
Km/ Vmax - Answers✓✓Slope of line =
Inhibitors - Answers✓✓__________ interfere with enzymatic activity.
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25/11/2024 13:32PM
Reversible - Answers✓✓
Irreversible - Answers✓✓Covalently modify an enzyme and inhibition cannot be revered
Competitive - Answers✓✓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 - Answers✓✓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 - Answers✓✓Competitive inhibitors have _______ reaction rates
Competitive inhibitor can not bind - Answers✓✓At high [S] there is so much S that _______
____
The Vmax stays the same and the Km increases - Answers✓✓If a competitive inhibitor is
added to an enzyme reaction then:
25/11/2024 13:32PM
BioC 3021 Exam 2 Questions and Answers
Michaelis- Menten Equation - Answers✓✓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 - Answers✓✓Rate of product formation ____________ as the initial substrate
concentration is raised.
Velocity - Answers✓✓How rapidly product is being formed by the reaction
Vmax - Answers✓✓Fastest reaction rate possible
S - Answers✓✓Substrate concentration
Km - Answers✓✓Michaelis constant ( dimensions of concentration)
Linear Km reduces to V= K x S (equation for a straight line) - Answers✓✓At low S values the
plot is _______
Curved
Need to use the entire Michaelis- Menten equation
+ 1/2 Vmax - Answers✓✓At intermediate S values the plot is _____________
, ©Themoon EXAM SOLUTIONS
25/11/2024 13:32PM
v= Vmax - Answers✓✓At high S values the plot is ________
Active sites available - Answers✓✓The rate of the reaction is limited by the number of
_________________.
Efficient - Answers✓✓Enzymes having a LOW Km are _______ at low substrate
concentrations
Inefficient - Answers✓✓Enzymes having a HIGH Km are ________ at low substrate
concentrations
Turnover number - Answers✓✓The number of molecules of substate that can be converted per
second per molecule of enzyme of a specific enzyme
Line Weaver Burk Plot - Answers✓✓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 - Answers✓✓1/ V intercept =
-1/ Km - Answers✓✓1/S intercept =
Km/ Vmax - Answers✓✓Slope of line =
Inhibitors - Answers✓✓__________ interfere with enzymatic activity.
, ©Themoon EXAM SOLUTIONS
25/11/2024 13:32PM
Reversible - Answers✓✓
Irreversible - Answers✓✓Covalently modify an enzyme and inhibition cannot be revered
Competitive - Answers✓✓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 - Answers✓✓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 - Answers✓✓Competitive inhibitors have _______ reaction rates
Competitive inhibitor can not bind - Answers✓✓At high [S] there is so much S that _______
____
The Vmax stays the same and the Km increases - Answers✓✓If a competitive inhibitor is
added to an enzyme reaction then:
