both presence and absence of an inhibitor. The enzyme concentration used in both experiments was $1\mathrm{.}5$M$.$ Vo is the initial rate of the catalyzed reaction, and $[$S$]$ is the substrate concentration.

Lineweaver$-$Burk Plot

$04$

$03$

$1/$V $($m

$02$

$0403020100\mathrm{.}10\mathrm{.}20\mathrm{.}30\mathrm{.}40\mathrm{.}50\mathrm{.}5$

$1/$S$]($mM

a$.$ What type of inhibition is displayed by this inhibitor?

b$.$ What are the values of Vmax and KM in the absence of the inhibitor? $($Show your calculations and be sure to include units.$)$

c$.$ How many reactions does each enzyme active site catalyze per second when saturated with substrate in the absence of the inhibitor?

d$.$ Is the maximum rate for the uninhibited reaction diffusion limited$?$ Explain:

e$.$ Where on the enzyme molecule does the inhibitor most likely bind? Explain:Q$3/$ Shown below are kinetics data for an enzyme that were collected in

both presence and absence of an inhibitor. The enzyme concentration

used in both experiments was $1\mathrm{.}5M.V_0$ is the initial rate of the

catalyzed reaction, and $S$ is the substrate concentration.

Lineweaver$-$Burk Plot

a$.$ What type of inhibition is displayed by this inhibitor?

b$.$ What are the values of Vmax and $KM$ in the absence of the

inhibitor? $($Show your calculations and be sure to include units.$)$

c$.$ How many reactions does each enzyme active site catalyze per

second when saturated with substrate in the absence of the

inhibitor?

d$.$ Is the maximum rate for the uninhibited reaction diffusion limited$?$

Explain:

e$.$ Where on the enzyme molecule does the inhibitor most likely bind?

Explain: