Allosteric regulatory properties of muscle phosphofructokinase

Abstract

We have reviewed the allosteric regulatory properties of skeletal muscle phosphofructokinase and recent results on the phosphorylation of this enzyme. The number and affinities of various ligand binding sites are described, and a simple three state model is presented to explain the kinetic and ligand-binding properties of the enzyme. Data describing a lack of fit to a concerted transition model are presented. The widespread occurrence of partial phosphorylation of phosphofructokinase at a specific site near the carboxyl terminus is documented, as well as the lack of significant kinetic consequences of such phosphorylation.

Purification and Properties of Phosphofructokinase from Dictyostelium Discoideum

“…Phosphorylation of PFruK from mammalian sources has also been reported [2] (and references therein), but it does not appear to play a major role in the regulation of the enzyme. In the case of D. discoideum PFruK, incubation of the purified enzyme with CAMP-dependent protein kinase for 30 min in the presence of [Y-~~PIATP resulted in the incorporation of radiolabel into PFruK, as revealed by autoradiography of a SDS/polyacrylamide gel (Fig.…”

“…PFruK is well-known to be a highly modulated allosteric enzyme whose activity exhibits positive cooperativity for fructose-6-P, i.e. a sigmoidal saturation curve, and responds to a variety of metabolic signals in many cells (reviewed in [l] and [2]). The regulatory properties of PFruK and their underlying molecular mechanisms are a matter of intense research.…”

Regulatory properties of 6-phosphofructokinase and control of glycolysis in boar spermatozoa

“…PFK catalyzes the highly exergonic reaction: fructose 6-phosphate (F6P)CATP/fructose 1,6-bisphosphate (F1,6P 2 )CADP. The activity of PFK is allosterically modulated by a number of effectors (for review see Kemp & Foe 1983, Krause & Wegener 1996b, 1996c. The control of PFK activity is based on allosteric inhibition by physiological concentrations of its cosubstrate ATP, which lowers the affinity for its substrate, so that physiological concentrations of F6P are not sufficient for PFK activity.…”

The effects of sodium bicarbonate supplementation on asoccer specific conditioning test in division III soccer players

“…4 Because elevated intramuscular [H + ] reduces ATP supply by inhibiting phosphofructokinase 5 , induced metabolic alkalosis has been suggested improve performance during high-intensity exercise by defending against H + -induced decreases in glycolytic enzymatic function. 6 In support of this hypothesis, induced metabolic alkalosis has been reported to increase blood lactate by 26-28% following high-intensityintermittent exercise. 7,8 Previous studies have used time motion analysis reports to develop cycle ergometry-based tests that emulate the metabolic demands of team-sports in order to investigate the ergogenic potential of induced metabolic alkalosis.…”