Relationship between Pyrophosphate : Fructose-6-phosphate 1-phosphotransferase, Sucrose Breakdown, and Respiration

The aim of this work was to discover the role of pyrophosphate : fructose-6-phosphate 1-phosphotransferase [PFK(PP;)]. Substrates and enzymes of sucrose breakdown were measured during starch accumulation by the endosperm of wild type and the sh 1 shrunken mutant of Zea mays L. The results suggested that the mutant depended primarily on alkaline invertase to break down sucrose, and showed that the activities of PFK(PPi) and UDPglucose pyrophosphorylase and contents of pyrophosphate and fructose2, 6-bisphosphate (Fru-2,6-P2) were no lower in the mutant than in the wild type. Appreciable activities of PFK(PPi), which were not responsive to Fru-2,6-P2, were found in the following red algae, which lack sucrose: Audouninella purpurea, Polysiphonia sp., Mastocarpus stellatus, Rhodymenia pseudopalmata. No PFK(PP;) was found in the bacterium Paracoccus denitrificans. Addition of sucrose to starved suspension cultures of Glycine max L. led to increases in oxygen uptake and Fru-2,6-P2 content. Glucose produced the same effects. It is argued that, although one of the functions of PFK(PP;) is production of pyrophosphate for sucrose breakdown via sucrose synthase, the key role of the enzyme is the maintenance of the cytosolic concentration of pyrophosphate according to the supply and demand of the latter.