BIOC 3021 PRACTICE EXAM 2 EXAMQUESTIONS AND ANSWERS 2024/2025 |
VERIFIED
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
+ 1/2 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 -
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
VERIFIED
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
+ 1/2 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 -
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
