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C R Acad Sci III ; 305(10): 405-10, 1987.
Artigo em Francês | MEDLINE | ID: mdl-2824008

RESUMO

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.


Assuntos
Látex/metabolismo , Fosfotransferases/análise , Árvores , Citosol/enzimologia , Difosfatos/metabolismo , Glicólise , Látex/biossíntese , Fosfotransferases/metabolismo
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