Editing Pyruvate kinase (section)

==== Fructose-1,6-bisphosphate ====
FBP is the most significant source of regulation because it comes from within the glycolysis pathway. FBP is a glycolytic intermediate produced from the phosphorylation of [[fructose 6-phosphate]]. FBP binds to the allosteric binding site on domain C of pyruvate kinase and changes the conformation of the enzyme, causing the activation of pyruvate kinase activity.<ref>{{cite journal | vauthors = Ishwar A |title=Distinguishing the interactions in the fructose 1,6-bisphosphate binding site of human liver pyruvate kinase that contribute to allostery. |journal=Biochemistry |volume=54 |issue=7 |pages=1516–24 |date=24 February 2015 |pmid=25629396 |pmc=5286843 |doi=10.1021/bi501426w }}</ref> As an intermediate present within the glycolytic pathway, FBP provides [[feed forward (control)|feedforward stimulation]] because the higher the concentration of FBP, the greater the allosteric activation and magnitude of pyruvate kinase activity. Pyruvate kinase is most sensitive to the effects of FBP. As a result, the remainder of the regulatory mechanisms serve as secondary modification.<ref name="Valentini 18145–18152"/><ref>{{cite journal | vauthors = Jurica MS, Mesecar A, Heath PJ, Shi W, Nowak T, Stoddard BL | title = The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate | journal = Structure | volume = 6 | issue = 2 | pages = 195–210 | date = February 1998 | pmid = 9519410 | doi = 10.1016/S0969-2126(98)00021-5 | doi-access = free }}</ref>