Question

What type of bond would you expect to find associated with the primary structure of the enzyme phosphofructokinase (PFK)? In your own words, describe the reaction involved in the formation of this bond including the molecular components as needed.

Answer 1

ans:)Phosphofructokinase (PFK) is a glycolytic enzyme that catalyzes the transfer of a phosphoryl group from ATP to fructose-6-phosphate to yield ADP and fructose-1,6-bisphosphate.

* Living organisms, both unicellular and multicellular, require energy to live and function. Energy is stored andprovided in the form of adenosine triphosphate (ATP).

* ATP is produced by multiple cellular processes including glycolysis, as well as aerobic and anaerobic respiration

* PFK is the most important regulatory enzyme of glycolysis. It irreversibly catalyzes the rate-limiting step ofglycolysis: the conversion of fructose -6-phosphate and ATP to fructose-1, 6-diphosphate and ADP.PFK exists as a homotetramer in bacteria and mammals.

* Each of the four monomers of PFK is composed oftwo similar domains. One domain has an ATP binding pocket. The other domain contains the substratebinding site and the allosteric site.

* An allosteric site is a regulatory binding site that affects enzyme activity andis distinct from the substrate-binding site of an enzyme. Various activators and inhibitors regulate PFK.Examples of PFK activators are ADP, AMP and fructose 2, 6 diphosphate. Examples of PFK inhibitors are ATPphosphoglycerate and citrate.