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 substratesPFK KM using F-1,6-BP and ATP was 1.48 mMF-2,6-BP was a powerful activator for PFKPFK was inhibited by ATPPFK inhibition by ATP could not be overridden by AMPOn the graph below, draw:a. A Michaelis-Menten curve for the normal mosquito PFK enzymeb. A Michaelis-Menten curve for the PFK enzyme activated by F-2,6-GPC. A Michaelis-Menten curve for the PFK enzyme inhibited by ATPd. A Michaelis-Menten curve for the PFK enzyme when ATP and AMP are both present

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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PFK-1 is actually a tetramer with four identical active sites that produced fructose 1,6-bisphosphate. There are also allosteric sites for citrate and ATP/ADP on each subunit as well which influence how well the active sites are binding substrates or producing product. The arginine at position 48 on each PFK-1 subunit normally forms a salt bridge with a negatively charged oxygen on phosphate in the catalytic interface of PFK-1. Speculate on how the R48C mutation might change this function.
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