Prévôt J C, Jacob J L, Errchidi S, Vidal A
Laboratoire de Physiologie et de Biochimie de l'I.R.C.A.-C.I.R.A.D., Centre de Montpellier.
C R Acad Sci III. 1987;305(10):405-10.
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.
果糖-6-磷酸1-磷酸转移酶活性(EC 2.7.1.90)进行了表征。它是一种依赖镁离子的酶,对于1 mM的焦磷酸和10 mM的果糖-6-磷酸浓度,该阳离子在2.5至3 mM之间具有最佳效果。它被果糖-2,6-二磷酸的催化含量激活。其潜在活性高于依赖ATP的磷酸果糖激酶(EC 2.7.1.11)的40%。其最适pH在7.5 - 7.6之间;此时,该酶对焦磷酸的亲和力为0.3 mM,对果糖-6-磷酸的亲和力为3.5 mM。有人认为,该转移酶在焦磷酸代谢以及糖酵解能量效率的提高中发挥作用,因此在与胶乳产量相关的生化机制中起着重要作用。