This is all the information given. I am having an issue posting the photo of the plot, but I'm pretty sure all you need are the trendline equations for the inhibitor and without the inhibitor, which I have provided.
The Lineweaver-Burk plot (1/v vs 1/[S]) for an enzyme-catalyzed reaction in the presence and absence of an inhibitor provides the lines y = 0.663x + 0.0222 (no inhibitor) and y = 0.224x + 0.0224 (inhibitor). (The units for 1/v are mmol/min and the units for 1/[S] are mM.)
A) What type of inhibitor was used to obtain this data?
B) What are the KM and Vmax values for the non-inhibited enzyme?
C) What are the apparent KM of the inhibited enzyme?
D) What is the alpha value?
E) What is the KI of the inhibitor if 1 mM of inhibitor was used
Enzyme kinetics for biochemistry.
This is all the information given. I am having an issue posting the photo of the plot, but I'm pretty sure all you need are the trendline equations for the inhibitor and without the inhibitor, which I have provided.
The Lineweaver-Burk plot (1/v vs 1/[S]) for an enzyme-catalyzed reaction in the presence and absence of an inhibitor provides the lines y = 0.663x + 0.0222 (no inhibitor) and y = 0.224x + 0.0224 (inhibitor). (The units for 1/v are mmol/min and the units for 1/[S] are mM.)
A) What type of inhibitor was used to obtain this data?
B) What are the KM and Vmax values for the non-inhibited enzyme?
C) What are the apparent KM of the inhibited enzyme?
D) What is the alpha value?
E) What is the KI of the inhibitor if 1 mM of inhibitor was used
Enzyme kinetics for biochemistry.
