[Demonstration of a pyrophosphate-fructose 6-phosphate 1-phosphotransferase in the latex from Hevea brasiliensis].
A pyrophosphate: fructose-6-phosphate 1-phosphotransferase activity (EC 2.7.1.90) has been characterized in cytosol from Hevea brasiliensis latex. It is Mg+ dependent enzyme, and the cation has an optimal effect between 2.5 to 3 mM for a concentration of 1 mM of pyrophosphate and 10 mM of fructose-6-phosphate. It is activated by catalytic content of fructose-2,6-diphosphate. Its potential activity is higher than 40% of that of ATP dependent phosphofructokinase (EC 2.7.1.11). Its optimum pH is between 7.5-7.6; then, the enzyme affinity is 0.3 mM for pyrophosphate and 3.5 mM for fructose-6-phosphate. It is suggested that the transferase plays a role in the pyrophosphate metabolism and the increasing of the energetic efficiency of glycolysis and so takes a significant part in the biochemical mechanisms involved in the latex yield.
Prévôt
J C
JC
Laboratoire de Physiologie et de Biochimie de l'I.R.C.A.-C.I.R.A.D., Centre de Montpellier.
Jacob
J L
JL
Errchidi
S
S
Vidal
A
A
D003600:Cytosol / Q000201:enzymology; D011756:Diphosphates / Q000378:metabolism; D006019:Glycolysis; D007840:Latex / Q000096:biosynthesis / Q000378:metabolism*; D010770:Phosphotransferases / Q000032:analysis* / Q000378:metabolism; D014197:Trees
D011756:Diphosphates; D007840:Latex; D010770:Phosphotransferases; C022502:pyrophosphate-fructose 6-phosphate 1-phosphotransferase
Mise en évidence d'une pyrophosphate: fructose-6-phosphate phosphotransférase dans le latex d'Hevea brasiliensis.