$1.$ Select a value for the KM of an enzyme between $0\mathrm{.}1$ and $10$ mM$.$ Select a value for the Vmax of an enzyme between $1$ and $100\backslash$mu M$/$sec$.$

$2.$ Write down t

$3.$ Select a KI value for an pure noncompetitive inhibitor between $0\mathrm{.}01$ and $1$ mM$.$

$4.$ Write the modified Michaelis$-$Menten equation for your enzyme in the presence of its inhibitor.

$5.$ Select an inhibitor concentration between $0\mathrm{.}001$ and $10$ mM

$6.$ Draw$/$create a Michaelis$-$Menten graph and a Lineweaver$-$Burk graph of your enzyme in the absence of inhibitor and in the presence of the inhibitor concentration $7.$ Write $1-2$ sentences reflecting on the exercise. How effective is your inhibitor at the concentration you chose? How does this relate to the values you chose for KM$,$ KI$,$ and Vmax?