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
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
(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
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
