why does fructose 1,6-biphosphate bind to pyruvate kinase? What is this called?
Pyruvate kinase activity is most broadly regulated by allosteric effectors. The most significant pyruvate kinase regulator is fructose-1,6-bisphosphate which serves as an allosteric effector for the enzyme.
Allosteric regulation is the binding of an effector to a site on the protein other than the active site, causing a conformational change and altering the activity of that given protein or enzyme. Pyruvate kinase has been found to be allosterically activated by fructose 1,6 bisphosphate.
Get Answers For Free
Most questions answered within 1 hours.