Uridine diphosphate glucose breakdown is mediated by a unique enzyme activated by fructose 2,6-bisphosphate in Solanum tuberosum.

In the presence of inorganic phosphate, uridine 5'-diphosphate glucose (UDPG) is specifically hydrolyzed to glucose 1-phosphate and UDP by a unique enzyme, UDPG phosphorylase. The activity of the enzyme was maximally stimulated by fructose 2,6-bisphosphate, a regulatory metabolite recently discovered in both plants and animals, and by 2-phosphoglyceric acid. At 1 muM, fructose 2,6-bisphosphate stimulated UDPG phosphorolysis 10-fold, whereas 2-phosphoglyceric acid was required at higher concentrations (100 muM) to produce a similar effect. Fructose 2,6-bisphosphate appears to increase the affinity of the enzyme for inorganic phosphate, with a change in K(m) from 1.6 mM to 0.3 mM. The results suggest that fructose 2,6-bisphosphate participates in the regulation of other pathways of carbohydrate metabolism in addition to playing its recognized role in glycolysis and gluconeogenesis.