The enzyme PFK was studied in mosquitos. The authors found that: PFK Vmax was 4.5 μmol/min with F-1,6-BP (along with ATP) as the substrates PFK KM using F-1,6-BP and ATP was 1.48 mM F-2,6-BP was a powerful activator for PFK PFK was inhibited by ATP PFK inhibition by ATP could not be overridden by AMP On the graph below, draw: a. A Michaelis-Menten curve for the normal mosquito PFK enzyme b. A Michaelis-Menten curve for the PFK enzyme activated by F-2,6-GP C. A Michaelis-Menten curve for the PFK enzyme inhibited by ATP d. A Michaelis-Menten curve for the PFK enzyme when ATP and AMP are both present

Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter21: Photosynthesis
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The enzyme PFK was studied in mosquitos. The authors found that:
PFK Vmax was 4.5 μmol/min with F-1,6-BP (along with ATP) as the substrates
PFK KM using F-1,6-BP and ATP was 1.48 mM
F-2,6-BP was a powerful activator for PFK
PFK was inhibited by ATP
PFK inhibition by ATP could not be overridden by AMP
On the graph below, draw:
a. A Michaelis-Menten curve for the normal mosquito PFK enzyme
b. A Michaelis-Menten curve for the PFK enzyme activated by F-2,6-GP
C. A Michaelis-Menten curve for the PFK enzyme inhibited by ATP
d. A Michaelis-Menten curve for the PFK enzyme when ATP and AMP are both present
Transcribed Image Text:The enzyme PFK was studied in mosquitos. The authors found that: PFK Vmax was 4.5 μmol/min with F-1,6-BP (along with ATP) as the substrates PFK KM using F-1,6-BP and ATP was 1.48 mM F-2,6-BP was a powerful activator for PFK PFK was inhibited by ATP PFK inhibition by ATP could not be overridden by AMP On the graph below, draw: a. A Michaelis-Menten curve for the normal mosquito PFK enzyme b. A Michaelis-Menten curve for the PFK enzyme activated by F-2,6-GP C. A Michaelis-Menten curve for the PFK enzyme inhibited by ATP d. A Michaelis-Menten curve for the PFK enzyme when ATP and AMP are both present
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