Pyrophosphate:fructose 6-phosphate 1-phosphotransferase and glycolysis in non-photosynthetic tissues of higher plants.
The activity of pyrophosphate:fructose-6-phosphate 1-phosphotransferase [PFK (PPi); EC 2.7.1.90] in extracts of the storage tissues of leek (Allium porrum), beetroot (Beta vulgaris) and roots of darnel (Lolium temulentum) exceeded 0.15 mumol/min per g fresh wt. As net flux from fructose 1,6-bisphosphate to fructose 6-phosphate in these tissues is unlikely, it is suggested that PFK (PPi) does not contribute to gluconeogenesis or starch synthesis. The maximum catalytic activities of PFK (PPi) in apex, stele and cortex of the root of pea (Pisum sativum) and in the developing and the thermogenic club of the spadix of cuckoo-pint (Arum maculatum) were measured and compared with those of phosphofructokinase, and to estimates of the rates of carbohydrate oxidation. PPi and fructose 2,6-bisphosphate in Arum clubs were measured. The above measurements are consistent with a glycolytic role for PFK (PPi) in tissues where there is marked biosynthesis, but not in the thermogenic club of Arum. The possibility that PFK (PPi) is a means of synthesizing pyrophosphate is discussed.
ap Rees
T
T
Green
J H
JH
Wilson
P M
PM
D005635:Fructosediphosphates / Q000378:metabolism; D006019:Glycolysis; D010732:Phosphofructokinase-1 / Q000378:metabolism; D010770:Phosphotransferases / Q000378:metabolism*; D063245:Plant Development; D010944:Plants / Q000201:enzymology*
D005635:Fructosediphosphates; C027652:fructose 2,6-diphosphate; D010770:Phosphotransferases; D010732:Phosphofructokinase-1; C022502:pyrophosphate-fructose 6-phosphate 1-phosphotransferase