Bioc 3021 Exam 2 Questions and
Answers 100% Solved | Latest Update
Michaelis- Menten Equation - ✔✔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 - ✔✔Rate of product formation ____________ as the initial
substrate concentration is raised.
Velocity - ✔✔How rapidly product is being formed by the reaction
Vmax - ✔✔Fastest reaction rate possible
S - ✔✔Substrate concentration
Km - ✔✔Michaelis constant ( dimensions of concentration)
Linear Km reduces to V= K x S (equation for a straight line) - ✔✔At low S
values the plot is _______
Curved
Need to use the entire Michaelis- Menten equation
1
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,+ 1/2 Vmax - ✔✔At intermediate S values the plot is _____________
v= Vmax - ✔✔At high S values the plot is ________
Active sites available - ✔✔The rate of the reaction is limited by the number
of _________________.
Efficient - ✔✔Enzymes having a LOW Km are _______ at low substrate
concentrations
Inefficient - ✔✔Enzymes having a HIGH Km are ________ at low substrate
concentrations
Turnover number - ✔✔The number of molecules of substate that can be
converted per second per molecule of enzyme of a specific enzyme
Line Weaver Burk Plot - ✔✔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 - ✔✔1/ V intercept =
-1/ Km - ✔✔1/S intercept =
Km/ Vmax - ✔✔Slope of line =
Inhibitors - ✔✔__________ interfere with enzymatic activity.
Reversible - ✔✔
2
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, Irreversible - ✔✔Covalently modify an enzyme and inhibition cannot be
revered
Competitive - ✔✔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 - ✔✔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 - ✔✔Competitive inhibitors have _______ reaction rates
Competitive inhibitor can not bind - ✔✔At high [S] there is so much S that
_______ ____
The Vmax stays the same and the Km increases - ✔✔If a competitive
inhibitor is added to an enzyme reaction then:
3
©JOSHCLAY 2024/2025. YEAR PUBLISHED 2024.
Answers 100% Solved | Latest Update
Michaelis- Menten Equation - ✔✔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 - ✔✔Rate of product formation ____________ as the initial
substrate concentration is raised.
Velocity - ✔✔How rapidly product is being formed by the reaction
Vmax - ✔✔Fastest reaction rate possible
S - ✔✔Substrate concentration
Km - ✔✔Michaelis constant ( dimensions of concentration)
Linear Km reduces to V= K x S (equation for a straight line) - ✔✔At low S
values the plot is _______
Curved
Need to use the entire Michaelis- Menten equation
1
©JOSHCLAY 2024/2025. YEAR PUBLISHED 2024.
,+ 1/2 Vmax - ✔✔At intermediate S values the plot is _____________
v= Vmax - ✔✔At high S values the plot is ________
Active sites available - ✔✔The rate of the reaction is limited by the number
of _________________.
Efficient - ✔✔Enzymes having a LOW Km are _______ at low substrate
concentrations
Inefficient - ✔✔Enzymes having a HIGH Km are ________ at low substrate
concentrations
Turnover number - ✔✔The number of molecules of substate that can be
converted per second per molecule of enzyme of a specific enzyme
Line Weaver Burk Plot - ✔✔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 - ✔✔1/ V intercept =
-1/ Km - ✔✔1/S intercept =
Km/ Vmax - ✔✔Slope of line =
Inhibitors - ✔✔__________ interfere with enzymatic activity.
Reversible - ✔✔
2
©JOSHCLAY 2024/2025. YEAR PUBLISHED 2024.
, Irreversible - ✔✔Covalently modify an enzyme and inhibition cannot be
revered
Competitive - ✔✔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 - ✔✔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 - ✔✔Competitive inhibitors have _______ reaction rates
Competitive inhibitor can not bind - ✔✔At high [S] there is so much S that
_______ ____
The Vmax stays the same and the Km increases - ✔✔If a competitive
inhibitor is added to an enzyme reaction then:
3
©JOSHCLAY 2024/2025. YEAR PUBLISHED 2024.
