You measure the initial velocity of an enzyme in the absence and presence of an inhibitor. In each case the inhibitor is at 10 µM. Show the primary data for all three cases and the Lineweaver–Burk plot. Calculate the KM and Vmax for each case both graphically and mathematically. Determine the mechanism for each inhibitor and where they will interact on the enzyme.
$\begin{array}{c}
\underline{\text { Initial Velocity ( } \mu \mathrm { mole } / \mathrm { ml } \mathrm { min } )}\
\begin{array} { c c c c }
[ \mathrm { S } ] \mathrm { mM } & \begin{array} { c }
\text { Enzyme } \
\text { alone }
\end{array} & \begin{array} { c }
\text { Enzyme } \
+ \text { inhibitor 1 }
\end{array} & \begin{array} { c }
\text { Enzyme } \
+ \text { inhibitor 2 }
\end{array} \
0.33 & 1.65 & 1.05 & 0.79 \
0.50 & 2.13 & 1.43 & 1.02 \
1.00 & 2.99 & 2.22 & 1.43 \
2.00 & 3.72 & 3.08 & 1.79 \
5.00 & 4.00 & 3.80 & 2.00
\end{array}
\end{array}$

Question

You measure the initial velocity of an enzyme in the absence and presence of an inhibitor.  In each case the inhibitor is at 10 µM.  Show the primary data for all three cases and the Lineweaver–Burk plot.  Calculate the KM and Vmax for each case both graphically and mathematically.  Determine the mechanism for each inhibitor and where they will interact on the enzyme.
$\begin{array}{c}
\underline{\text { Initial Velocity ( } \mu \mathrm { mole } / \mathrm { ml } \mathrm { min } )}\
\begin{array} { c c c c } 
 [ \mathrm { S } ] \mathrm { mM } & \begin{array} { c } 
\text { Enzyme } \
\text { alone }
\end{array} & \begin{array} { c } 
\text { Enzyme } \
+ \text { inhibitor 1 }
\end{array} & \begin{array} { c } 
\text { Enzyme } \
+ \text { inhibitor 2 }
\end{array} \
0.33 & 1.65 & 1.05 & 0.79 \
0.50 & 2.13 & 1.43 & 1.02 \
1.00 & 2.99 & 2.22 & 1.43 \
2.00 & 3.72 & 3.08 & 1.79 \
5.00 & 4.00 & 3.80 & 2.00
\end{array}
\end{array}$

Quizplus · Accepted Answer

The Answer of You measure the initial velocity of an enzyme in the absence and presence of an inhibitor.  In each case the inhibitor is at 10 µM.  Show the primary data for all three cases and the Lineweaver–Burk plot.  Calculate the KM and Vmax for each case both graphically and mathematically.  Determine the mechanism for each inhibitor and where they will interact on the enzyme.
$\begin{array}{c}
\underline{\text { Initial Velocity ( } \mu \mathrm { mole } / \mathrm { ml } \mathrm { min } )}\
\begin{array} { c c c c } 
 [ \mathrm { S } ] \mathrm { mM } & \begin{array} { c } 
\text { Enzyme } \
\text { alone }
\end{array} & \begin{array} { c } 
\text { Enzyme } \
+ \text { inhibitor 1 }
\end{array} & \begin{array} { c } 
\text { Enzyme } \
+ \text { inhibitor 2 }
\end{array} \
0.33 & 1.65 & 1.05 & 0.79 \
0.50 & 2.13 & 1.43 & 1.02 \
1.00 & 2.99 & 2.22 & 1.43 \
2.00 & 3.72 & 3.08 & 1.79 \
5.00 & 4.00 & 3.80 & 2.00
\end{array}
\end{array}$

You Measure the Initial Velocity of an Enzyme in the Absence